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Conserved domains on  [gi|21735562|ref|NP_663304|]
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mitogen-activated protein kinase kinase kinase 7 isoform B [Homo sapiens]

Protein Classification

mitogen-activated protein kinase kinase kinase 7( domain architecture ID 10197246)

mitogen-activated protein kinase kinase kinase 7 (MAP3K7) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6

CATH:  1.10.510.10
EC:  2.7.11.25
Gene Symbol:  MAP3K7
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
42-292 0e+00

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 568.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLYNVLHGA 119
Cdd:cd14058   1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNqkPVCLVMEYAEGGSLYNVLHGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPE 199
Cdd:cd14058  81 EPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 200 VFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14058 161 VFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKRPSMKE 240
                       250
                ....*....|...
gi 21735562 280 IVKIMTHLMRYFP 292
Cdd:cd14058 241 IVKIMSHLMQFFP 253
 
Name Accession Description Interval E-value
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
42-292 0e+00

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 568.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLYNVLHGA 119
Cdd:cd14058   1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNqkPVCLVMEYAEGGSLYNVLHGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPE 199
Cdd:cd14058  81 EPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 200 VFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14058 161 VFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKRPSMKE 240
                       250
                ....*....|...
gi 21735562 280 IVKIMTHLMRYFP 292
Cdd:cd14058 241 IVKIMSHLMQFFP 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
36-284 8.02e-76

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 242.05  E-value: 8.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     36 IEVEEVVGRGAFGVVCKAKWRAK------DVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKggkkkvEVAVKTLkedASEQQIEEFLREARIMRKLDHPNVVKLLGVCTeeEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    105 EYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQT 184
Cdd:smart00219  81 EYMEGGDLLSYLRKNRP--KLSLSDLLSFALQIARGMEYLESKN---FIHRDLAARNCL-VGENLVVKISDFGLSRDLYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    185 HMTNNKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:smart00219 155 DDYYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGM--SNEEVLEYLKNGYRLPQPPNCPPEL 232
                          250       260
                   ....*....|....*....|....*
gi 21735562    260 ESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:smart00219 233 YDLMLQCWAEDPEDRPTFSELVEIL 257
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
36-284 4.88e-70

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 226.99  E-value: 4.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    36 IEVEEVVGRGAFGVVCKAKWRAK------DVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVM 104
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKegaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQgePLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   105 EYAEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT 184
Cdd:pfam07714  81 EYMPGGDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLESKN---FVHRDLAARNCLVSENLVV-KISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   185 HMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:pfam07714 155 DDYYRKRGGGklpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGM--SNEEVLEYLEDGYRLPQPENCPDE 232
                         250       260
                  ....*....|....*....|....*.
gi 21735562   259 IESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:pfam07714 233 LYDLMKQCWAYDPEDRPTFSELVEDL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-380 1.53e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 143.34  E-value: 1.53e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKwRAKDVAIKQIESESERKAFIV-----ELRQLSRVNHP-NIVKLYGAC--LNPVCLVMEYAE 108
Cdd:COG0515   3 RILRKLGEGSFGEVYLAR-DRKLVALKVLAKKLESKSKEVerflrEIQILASLNHPpNIVKLYDFFqdEGSLYLVMEYVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTAC-------- 180
Cdd:COG0515  82 GGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKG---IIHRDIKPENILLDRDGRVVKLIDFGLAKllpdpgst 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -DIQTHMTNNKGSAAWMAPEVFEGSN---YSEKCDVFSWGIILWEVITRRKPFDEIGGP-----AFRIMW-AVHNGTRPP 250
Cdd:COG0515 159 sSIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqTLKIILeLPTPSLASP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 251 LIKNLPKP----IESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADE-----PLQYPCQYSDEGQSNSATSTGSFMD 321
Cdd:COG0515 239 LSPSNPELiskaASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLsdllkPDDSAPLRLSLPPSLEALISSLNSL 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 322 IASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLP 380
Cdd:COG0515 319 AISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSS 377
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-279 1.03e-27

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 117.59  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   37 EVEEVVGRGAFGVVckakWRAKD------VAIKQIESESERKA-----FIVELRQLSRVNHPNIVKLY-----GAClnpV 100
Cdd:NF033483  10 EIGERIGRGGMAEV----YLAKDtrldrdVAVKVLRPDLARDPefvarFRREAQSAASLSHPNIVSVYdvgedGGI---P 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  101 CLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGtac 180
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMI---QILSALEHAHRNG---IVHRDIKPQNILITKDGRV-KVTDFG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  181 dI-----QTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRImwA---VHNGTRP 249
Cdd:NF033483 153 -IaralsSTTMTQTNsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFD--GDSPVSV--AykhVQEDPPP 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 21735562  250 P--LIKNLPKPIESLMTRCWSKDPSQRP-SMEE 279
Cdd:NF033483 228 PseLNPGIPQSLDAVVLKATAKDPDDRYqSAAE 260
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
41-290 3.03e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 100.09  E-value: 3.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   41 VVGR----GAFgVVCKAKWRAKDVAIKQIESESERKAFIV--ELRQLSRVNHPNIVKLYG--ACLNPVCLVMEYAEGGSL 112
Cdd:PTZ00267  74 LVGRnpttAAF-VATRGSDPKEKVVAKFVMLNDERQAAYArsELHCLAACDHFGIVKHFDdfKSDDKLLLIMEYGSGGDL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  113 YNVLHG--AEPLPY--YTAAhamswcLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGtVLKICDFG--------TAC 180
Cdd:PTZ00267 153 NKQIKQrlKEHLPFqeYEVG------LLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTG-IIKLGDFGfskqysdsVSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  181 DIQTHMTnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeigGPAFR-IMWAVHNGTRPPLIKNLPKPI 259
Cdd:PTZ00267 226 DVASSFC---GTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFK---GPSQReIMQQVLYGKYDPFPCPVSSGM 299
                        250       260       270
                 ....*....|....*....|....*....|.
gi 21735562  260 ESLMTRCWSKDPSQRPSMEEIVKimTHLMRY 290
Cdd:PTZ00267 300 KALLDPLLSKNPALRPTTQQLLH--TEFLKY 328
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
60-224 1.28e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 80.66  E-value: 1.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     60 VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL---VMEYAEGGSLYNVLHGAEPLPYYTAAHAM 131
Cdd:TIGR03903    6 VAIKllrtdAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLlfaVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    132 swcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVA--GGTVLKICDFGT--------ACDIQ--THMTNNKGSAAWMAPE 199
Cdd:TIGR03903   86 ---LQVLDALACAHN---QGIVHRDLKPQNIMVSQtgVRPHAKVLDFGIgtllpgvrDADVAtlTRTTEVLGTPTYCAPE 159
                          170       180
                   ....*....|....*....|....*
gi 21735562    200 VFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLT 184
 
Name Accession Description Interval E-value
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
42-292 0e+00

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 568.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLYNVLHGA 119
Cdd:cd14058   1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNqkPVCLVMEYAEGGSLYNVLHGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPE 199
Cdd:cd14058  81 EPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLTNGGTVLKICDFGTACDISTHMTNNKGSAAWMAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 200 VFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14058 161 VFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKRPSMKE 240
                       250
                ....*....|...
gi 21735562 280 IVKIMTHLMRYFP 292
Cdd:cd14058 241 IVKIMSHLMQFFP 253
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
42-284 8.67e-110

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 329.11  E-value: 8.67e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESE----RKAFIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYAEGGSLYNV 115
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDndelLKEFRREVSILSKLRHPNIVQFIGACLSPPplCIVTEYMPGGSLYDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTAC---DIQTHMTNNKGS 192
Cdd:cd13999  81 LH--KKKIPLSWSLRLKIALDIARGMNYLHSPP---IIHRDLKSLNILLDENFTV-KIADFGLSRiknSTTEKMTGVVGT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFrIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPS 272
Cdd:cd13999 155 PRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQI-AAAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPE 233
                       250
                ....*....|..
gi 21735562 273 QRPSMEEIVKIM 284
Cdd:cd13999 234 KRPSFSEIVKRL 245
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
36-284 8.02e-76

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 242.05  E-value: 8.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     36 IEVEEVVGRGAFGVVCKAKWRAK------DVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKggkkkvEVAVKTLkedASEQQIEEFLREARIMRKLDHPNVVKLLGVCTeeEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    105 EYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQT 184
Cdd:smart00219  81 EYMEGGDLLSYLRKNRP--KLSLSDLLSFALQIARGMEYLESKN---FIHRDLAARNCL-VGENLVVKISDFGLSRDLYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    185 HMTNNKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:smart00219 155 DDYYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGM--SNEEVLEYLKNGYRLPQPPNCPPEL 232
                          250       260
                   ....*....|....*....|....*
gi 21735562    260 ESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:smart00219 233 YDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
36-284 5.48e-75

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 239.76  E-value: 5.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     36 IEVEEVVGRGAFGVVCKAKWRAK------DVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKgdgkevEVAVKTLkedASEQQIEEFLREARIMRKLDHPNIVKLLGVCTeeEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    105 EYAEGGSLYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQT 184
Cdd:smart00221  81 EYMPGGDLLDYLRKNRP-KELSLSDLLSFALQIARGMEYLESKN---FIHRDLAARNCL-VGENLVVKISDFGLSRDLYD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    185 HMTNNKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:smart00221 156 DDYYKVKGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLgEEPYPGM--SNAEVLEYLKKGYRLPKPPNCPPEL 233
                          250       260
                   ....*....|....*....|....*
gi 21735562    260 ESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:smart00221 234 YKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
40-285 2.07e-70

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 227.81  E-value: 2.07e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAK-----DVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEG 109
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGdgktvDVAVKTLkedASESERKDFLKEARVMKKLGHPNVVRLLGVCTeeEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVL------HGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd00192  81 GDLLDFLrksrpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKK---FVHRDLAARNCLVGEDLVV-KISDFGLSRDIY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 -----THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPK 257
Cdd:cd00192 157 dddyyRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLgATPYPGL--SNEEVLEYLRKGYRLPKPENCPD 234
                       250       260
                ....*....|....*....|....*...
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd00192 235 ELYELMLSCWQLDPEDRPTFSELVERLE 262
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
36-284 4.88e-70

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 226.99  E-value: 4.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    36 IEVEEVVGRGAFGVVCKAKWRAK------DVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVM 104
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKegaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQgePLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   105 EYAEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT 184
Cdd:pfam07714  81 EYMPGGDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLESKN---FVHRDLAARNCLVSENLVV-KISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   185 HMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:pfam07714 155 DDYYRKRGGGklpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGM--SNEEVLEYLEDGYRLPQPENCPDE 232
                         250       260
                  ....*....|....*....|....*.
gi 21735562   259 IESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:pfam07714 233 LYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
37-282 1.87e-69

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 225.10  E-value: 1.87e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKtgKLVAIKVIkkkKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEdkLYLVMEYCEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    110 GSLYNVLHGAEPLPYYTAAHamsWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNN 189
Cdd:smart00220  82 GDLFDLLKKRGRLSEDEARF---YLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHV-KLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    190 K--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiGGPAFRIMWAVHNGTRPPLIK--NLPKPIESLMTR 265
Cdd:smart00220 155 TfvGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG-DDQLLELFKKIGKPKPPFPPPewDISPEAKDLIRK 233
                          250
                   ....*....|....*..
gi 21735562    266 CWSKDPSQRPSMEEIVK 282
Cdd:smart00220 234 LLVKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
37-282 4.63e-69

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 224.02  E-value: 4.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:pfam00069   2 EVLEKLGSGSFGTVykAKHRDTGKIVAIKKIkkekIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKdnLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   109 GGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGtVLKICDFGTACDI--QTHM 186
Cdd:pfam00069  82 GGSLFDLLSEKGAFSEREAKFIM---KQILEGLEYLHSN---GIVHRDLKPENILIDEDG-NLKITDFGLARQLnsGSSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMwAVHNGTRPPLI-KNLPKPIESLMTR 265
Cdd:pfam00069 155 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEL-IIDQPYAFPELpSNLSEEAKDLLKK 233
                         250
                  ....*....|....*..
gi 21735562   266 CWSKDPSQRPSMEEIVK 282
Cdd:pfam00069 234 LLKKDPSKRLTATEALQ 250
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
43-284 3.88e-62

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 204.43  E-value: 3.88e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRA--KDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNV 115
Cdd:cd00180   2 GKGSFGKVYKARDKEtgKKVAVKVIpkeKLKKLLEELLREIEILKKLNHPNIVKLYDVFEteNFLYLVMEYCEGGSLKDL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNKGS--- 192
Cdd:cd00180  82 LK--ENKGPLSEEEALSILRQLLSALEYLHSNG---IIHRDLKPENILLDSDGTV-KLADFGLAKDLDSDDSLLKTTggt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 --AAWMAPEVFEGSNYSEKCDVFSWGIILWEVitrrkpfdeiggpafrimwavhngtrppliknlpKPIESLMTRCWSKD 270
Cdd:cd00180 156 tpPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRRMLQYD 201
                       250
                ....*....|....
gi 21735562 271 PSQRPSMEEIVKIM 284
Cdd:cd00180 202 PKKRPSAKELLEHL 215
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
41-285 6.14e-60

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 200.31  E-value: 6.14e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKDVAIKQIESESE------RKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSL 112
Cdd:cd14061   1 VIGVGGFGKVYRGIWRGEEVAVKAARQDPDedisvtLENVRQEARLFWMLRHPNIIALRGVCLQPpnLCLVMEYARGGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPyytaAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPN-LLLVAGG------TVLKICDFGTACDIQ-- 183
Cdd:cd14061  81 NRVLAGRKIPP----HVLVDWAIQIARGMNYLHNEAPVPIIHRDLKSSNiLILEAIEnedlenKTLKITDFGLAREWHkt 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNnKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRpPLIKNLPKPIESLM 263
Cdd:cd14061 157 TRMSA-AGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTL-PIPSTCPEPFAQLM 234
                       250       260
                ....*....|....*....|..
gi 21735562 264 TRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd14061 235 KDCWQPDPHDRPSFADILKQLE 256
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
43-284 1.31e-59

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 199.03  E-value: 1.31e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKW--RAKDVAIK---QIESESErkafivelrQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYNV 115
Cdd:cd14060   2 GGGSFGSVYRAIWvsQDKEVAVKkllKIEKEAE---------ILSVLSHRNIIQFYGAILEApnYGIVTEYASYGSLFDY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGtVLKICDFGTA--CDIQTHMTNNkGSA 193
Cdd:cd14060  73 LNSNES-EEMDMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADG-VLKICDFGASrfHSHTTHMSLV-GTF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 194 AWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGpaFRIMW-AVHNGTRPPLIKNLPKPIESLMTRCWSKDPS 272
Cdd:cd14060 150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEG--LQVAWlVVEKNERPTIPSSCPRSFAELMRRCWEADVK 227
                       250
                ....*....|..
gi 21735562 273 QRPSMEEIVKIM 284
Cdd:cd14060 228 ERPSFKQIIGIL 239
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
37-281 1.07e-58

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 197.04  E-value: 1.07e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVckakWRAKD------VAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLY--GACLNPVCLV 103
Cdd:cd14014   3 RLVRLLGRGGMGEV----YRARDtllgrpVAIKVLrpelaEDEEFRERFLREARALARLSHPNIVRVYdvGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLPYytaAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPP---REALRILAQIADALAAAHRAG---IVHRDIKPANILLTEDGRV-KLTDFGIARALG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 ----THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRPPLI---KNLP 256
Cdd:cd14014 152 dsglTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFD--GDSPAAVLAKHLQEAPPPPSplnPDVP 229
                       250       260
                ....*....|....*....|....*.
gi 21735562 257 KPIESLMTRCWSKDPSQRP-SMEEIV 281
Cdd:cd14014 230 PALDAIILRALAKDPEERPqSAAELL 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
37-282 5.77e-55

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 187.02  E-value: 5.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQI--ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGG 110
Cdd:cd05122   3 EILEKIGKGGFGVVYKARHKKtgQIVAIKKInlESKEKKESILNEIAILKKCKHPNIVKYYGSYLkkDELWIVMEFCSGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGA-EPLPYYTAAhamSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNN 189
Cdd:cd05122  83 SLKDLLKNTnKTLTEQQIA---YVCKEVLKGLEYLHSHG---IIHRDIKAANILLTSDGEV-KLIDFGLSAQLSDGKTRN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMW-AVHNGtrPPLIKNLPKPIESLM--- 263
Cdd:cd05122 156 TfvGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSEL--PPMKALFlIATNG--PPGLRNPKKWSKEFKdfl 231
                       250
                ....*....|....*....
gi 21735562 264 TRCWSKDPSQRPSMEEIVK 282
Cdd:cd05122 232 KKCLQKDPEKRPTAEQLLK 250
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
41-285 1.51e-54

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 185.96  E-value: 1.51e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIV--ELRQLSRV----NHPNIVKLYGACLNP--VCLVMEYAEGGSL 112
Cdd:cd14148   1 IIGVGGFGKVYKGLWRGEEVAVKAARQDPDEDIAVTaeNVRQEARLfwmlQHPNIIALRGVCLNPphLCLVMEYARGGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTaahaMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVA-------GGTVLKICDFGTACDIQ-T 184
Cdd:cd14148  81 NRALAGKKVPPHVL----VNWAVQIARGMNYLHNEAIVPIIHRDLKSSNILILEpienddlSGKTLKITDFGLAREWHkT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAV-HNGTRPPLIKNLPKPIESLM 263
Cdd:cd14148 157 TKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREID--ALAVAYGVaMNKLTLPIPSTCPEPFARLL 234
                       250       260
                ....*....|....*....|..
gi 21735562 264 TRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd14148 235 EECWDPDPHGRPDFGSILKRLE 256
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
42-287 6.41e-54

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 183.46  E-value: 6.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESErkafiVELRQLSRVNHPNIVKLYGAC-LNPV-CLVMEYAEGGSLYNVLHGA 119
Cdd:cd14059   1 LGSGAQGAVFLGKFRGEEVAVKKVRDEKE-----TDIKHLRKLNHPNIIKFKGVCtQAPCyCILMEYCPYGQLYEVLRAG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTA---CDIQTHMTNnKGSAAWM 196
Cdd:cd14059  76 REI---TPSLLVDWSKQIASGMNYLHLHK---IIHRDLKSPNVL-VTYNDVLKISDFGTSkelSEKSTKMSF-AGTVAWM 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 197 APEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfrIMWAV-HNGTRPPLIKNLPKPIESLMTRCWSKDPSQRP 275
Cdd:cd14059 148 APEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSA--IIWGVgSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRP 225
                       250
                ....*....|..
gi 21735562 276 SMEEivkIMTHL 287
Cdd:cd14059 226 SFRQ---ILMHL 234
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
29-285 5.78e-53

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 182.16  E-value: 5.78e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  29 EEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESER--KAFIVELRQLSRV----NHPNIVKLYGACLNP--V 100
Cdd:cd14145   1 LEIDFSELVLEEIIGIGGFGKVYRAIWIGDEVAVKAARHDPDEdiSQTIENVRQEAKLfamlKHPNIIALRGVCLKEpnL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPLPYYTaahaMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVA-------GGTVLKI 173
Cdd:cd14145  81 CLVMEFARGGPLNRVLSGKRIPPDIL----VNWAVQIARGMNYLHCEAIVPVIHRDLKSSNILILEkvengdlSNKILKI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDI-QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVhNGTRPPLI 252
Cdd:cd14145 157 TDFGLAREWhRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAM-NKLSLPIP 235
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd14145 236 STCPEPFARLMEDCWNPDPHSRPPFTNILDQLT 268
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
32-287 8.79e-53

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 181.77  E-value: 8.79e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIV------ELRQLSRVNHPNIVKLYGACLNP--VCLV 103
Cdd:cd14147   1 SFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTaesvrqEARLFAMLAHPNIIALKAVCLEEpnLCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLPYYTaahaMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGT-------VLKICDF 176
Cdd:cd14147  81 MEYAAGGPLSRALAGRRVPPHVL----VNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIEnddmehkTLKITDF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDI-QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRpPLIKNL 255
Cdd:cd14147 157 GLAREWhKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTL-PIPSTC 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14147 236 PEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
41-285 2.15e-52

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 180.62  E-value: 2.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIV------ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSL 112
Cdd:cd14146   1 IIGVGGFGKVYRATWKGQEVAVKAARQDPDEDIKATaesvrqEAKLFSMLRHPNIIKLEGVCLEEpnLCLVMEFARGGTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTAAHAM------SWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVA-------GGTVLKICDFGTA 179
Cdd:cd14146  81 NRALAAANAAPGPRRARRIpphilvNWAVQIARGMLYLHEEAVVPILHRDLKSSNILLLEkiehddiCNKTLKITDFGLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDI-QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRpPLIKNLPKP 258
Cdd:cd14146 161 REWhRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTL-PIPSTCPEP 239
                       250       260
                ....*....|....*....|....*..
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd14146 240 FAKLMKECWEQDPHIRPSFALILEQLT 266
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
37-283 4.12e-51

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 176.88  E-value: 4.12e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd08215   3 EKIRVIGKGSFGSAYLVRRKSDGklYVLKEIDlsnmSEKEREEALNEVKLLSKLKHPNIVKYYESFEENgkLCIVMEYAD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL----HGAEPLPyytAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTAcdiqt 184
Cdd:cd08215  83 GGDLAQKIkkqkKKGQPFP---EEQILDWFVQICLALKYLHSRK---ILHRDLKTQNIFLTKDGVV-KLGDFGIS----- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAA--------WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD--EIGGPAFRIMwavhNGTRPPLIKN 254
Cdd:cd08215 151 KVLESTTDLAktvvgtpyYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEanNLPALVYKIV----KGQYPPIPSQ 226
                       250       260
                ....*....|....*....|....*....
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIVKI 283
Cdd:cd08215 227 YSSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
42-287 1.04e-49

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 173.61  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA-KDVAIKQIESE---SERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNV 115
Cdd:cd14066   1 IGSGGFGTVYKGVLENgTVVAVKRLNEMncaASKKEFLTELEMLGRLRHPNLVRLLGYCLesDEKLLVYEYMPNGSLEDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LH---GAEPLPYYTAahaMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI-----QTHMT 187
Cdd:cd14066  81 LHchkGSPPLPWPQR---LKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEP-KLTDFGLARLIppsesVSKTS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIM---WAVHNGT-------RPPLIKNLPK 257
Cdd:cd14066 157 AVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDlveWVESKGKeeledilDKRLVDDDGV 236
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21735562 258 PIESLMT------RCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14066 237 EEEEVEAllrlalLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
40-282 3.58e-49

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 171.25  E-value: 3.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVckakWRAKD------VAIKQIESESERKAFIVELRQ----LSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06627   6 DLIGRGAFGSV----YKGLNlntgefVAIKQISLEKIPKSDLKSVMGeidlLKKLNHPNIVKYIGSVKtkDSLYIILEYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTAcdiqTHMT 187
Cdd:cd06627  82 ENGSLASIIKKFGKFPESLVAVYIY---QVLEGLAYLHEQG---VIHRDIKGANILTTKDGLV-KLADFGVA----TKLN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNK-------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPIE 260
Cdd:cd06627 151 EVEkdensvvGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDL--QPMAALFRIVQDDHPPLPENISPELR 228
                       250       260
                ....*....|....*....|..
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06627 229 DFLLQCFQKDPTLRPSAKELLK 250
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
40-279 1.35e-48

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 170.01  E-value: 1.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGS 111
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDtgELMAVKEVElsgdSEEELEALEREIRILSSLKHPNIVRYLGTERTEntLNIFLEYVPGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPLPYYTAAhamSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNN-- 189
Cdd:cd06606  86 LASLLKKFGKLPEPVVR---KYTRQILEGLEYLHS---NGIVHRDIKGANILVDSDGVV-KLADFGCAKRLAEIATGEgt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 ---KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPA---FRIMwavHNGTRPPLIKNLPKPIESLM 263
Cdd:cd06606 159 kslRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVaalFKIG---SSGEPPPIPEHLSEEAKDFL 235
                       250
                ....*....|....*.
gi 21735562 264 TRCWSKDPSQRPSMEE 279
Cdd:cd06606 236 RKCLQRDPKKRPTADE 251
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
42-284 3.53e-48

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 168.86  E-value: 3.53e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACLN---PVCLVMEYAEGGSLY 113
Cdd:cd14064   1 IGSGSFGKVYKGRCRNKIVAIKRYRantycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDdpsQFAIVTQYVSGGSLF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSMqPKALIHRDLKPPNLLLVAGGTVLkICDFGTACDIQT----HMTNN 189
Cdd:cd14064  81 SLLHEQKRV--IDLQSKLIIAVDVAKGMEYLHNL-TQPIIHRDLNSHNILLYEDGHAV-VADFGESRFLQSldedNMTKQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGtRPPLIKNLPKPIESLMTRCWS 268
Cdd:cd14064 157 PGNLRWMAPEVFtQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHI-RPPIGYSIPKPISSLLMRGWN 235
                       250
                ....*....|....*.
gi 21735562 269 KDPSQRPSMEEIVKIM 284
Cdd:cd14064 236 AEPESRPSFVEIVALL 251
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
42-277 1.41e-47

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 167.63  E-value: 1.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK---WRAkDVAIKQIES----ESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd13978   1 LGSGGFGTVSKARhvsWFG-MVAIKCLHSspncIEERKALLKEAEKMERARHSYVLPLLGVCVerRSLGLVMEYMENGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLH-GAEPLPYYTAAHAMSwclQCSQGVAYLHSMQPKaLIHRDLKPPNLLLVAGGTVlKICDFGTA-CDIQTH----- 185
Cdd:cd13978  80 KSLLErEIQDVPWSLRFRIIH---EIALGMNFLHNMDPP-LLHHDLKPENILLDNHFHV-KISDFGLSkLGMKSIsanrr 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 --MTNNKGSAAWMAPEVFEGSNY--SEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPL--------IK 253
Cdd:cd13978 155 rgTENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAINPL-LIMQIVSKGDRPSLddigrlkqIE 233
                       250       260
                ....*....|....*....|....
gi 21735562 254 NLPKpIESLMTRCWSKDPSQRPSM 277
Cdd:cd13978 234 NVQE-LISLMIRCWDGNPDARPTF 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
35-279 1.59e-45

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 161.99  E-value: 1.59e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd06623   2 DLERVKVLGQGSSGVVYKVrhKPTGKIYALKKIhvdGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEgeISIVLEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLP-----YYTAahamswclQCSQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI 182
Cdd:cd06623  82 DGGSLADLLKKVGKIPepvlaYIAR--------QILKGLDYLH--TKRHIIHRDIKPSNLLINSKGEV-KIADFGISKVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF-RIMWAVHNGTRPPLIKNLPKP 258
Cdd:cd06623 151 ENTLDQCNtfvGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFfELMQAICDGPPPSLPAEEFSP 230
                       250       260
                ....*....|....*....|..
gi 21735562 259 -IESLMTRCWSKDPSQRPSMEE 279
Cdd:cd06623 231 eFRDFISACLQKDPKKRPSAAE 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
37-279 2.24e-45

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 161.10  E-value: 2.24e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKtgEEYAVKIIDkkklKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDknLYLVMELCT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLV--AGGTVLKICDFGTACDIQT-- 184
Cdd:cd05117  83 GGELFDRIVKKGSFSEREAAKIMK---QILSAVAYLHSQG---IVHRDLKPENILLAskDPDSPIKIIDFGLAKIFEEge 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNG---TRPPLIKNLPKPIES 261
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFY--GETEQELFEKILKGkysFDSPEWKNVSEEAKD 234
                       250
                ....*....|....*...
gi 21735562 262 LMTRCWSKDPSQRPSMEE 279
Cdd:cd05117 235 LIKRLLVVDPKKRLTAAE 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
40-282 3.26e-45

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 160.84  E-value: 3.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGACLNPVCL--VMEYAEGGSLYN 114
Cdd:cd06614   6 EKIGEGASGEVYKATDRAtgKEVAIKKMRLRKQNKELIInEILIMKECKHPNIVDYYDSYLVGDELwvVMEYMDGGSLTD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK---G 191
Cdd:cd06614  86 IITQNPV--RMNESQIAYVCREVLQGLEYLHSQN---VIHRDIKSDNILLSKDGSV-KLADFGFAAQLTKEKSKRNsvvG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 192 SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP-FDEiggPAFRIMWAVHNGTRPPL--IKNLPKPIESLMTRCWS 268
Cdd:cd06614 160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEE---PPLRALFLITTKGIPPLknPEKWSPEFKDFLNKCLV 236
                       250
                ....*....|....
gi 21735562 269 KDPSQRPSMEEIVK 282
Cdd:cd06614 237 KDPEKRPSAEELLQ 250
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
37-286 3.36e-45

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 160.76  E-value: 3.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14003   3 ELGKTLGEGSFGKVKLARHKLtgEKVAIKIIDksklKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETEnkIYLVMEYAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTHMTN 188
Cdd:cd14003  83 GGELFDYIVNNGRLSEDEARRFFQ---QLISAVDYCHSNG---IVHRDLKLENILLDKNG-NLKIIDFGLSNEFRGGSLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NK--GSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDeigGPAFRIM-WAVHNGTrPPLIKNLPKPIESLMT 264
Cdd:cd14003 156 KTfcGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFD---DDNDSKLfRKILKGK-YPIPSHLSPDARDLIR 231
                       250       260
                ....*....|....*....|..
gi 21735562 265 RCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd14003 232 RMLVVDPSKRITIEE---ILNH 250
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
31-285 4.69e-45

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 160.31  E-value: 4.69e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQI-ESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05059   1 IDPSELTFLKELGSGQFGVVHLGKWRGKiDVAIKMIkEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKqrPIFIVTEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTAC----DI 182
Cdd:cd05059  81 MANGCLLNYLRERRGK--FQTEQLLEMCKDVCEAMEYLES---NGFIHRDLAARNCL-VGEQNVVKVSDFGLARyvldDE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05059 155 YTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKmPYERFSNS--EVVEHISQGYRLYRPHLAPTEVYT 232
                       250       260
                ....*....|....*....|....
gi 21735562 262 LMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd05059 233 IMYSCWHEKPEERPTFKILLSQLT 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
33-280 5.55e-45

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 160.92  E-value: 5.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVVCKAKWRAKDV--AIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd13996   5 LNDFEEIELLGSGGFGSVYKVRNKVDGVtyAIKKIrltEKSSASEKVLREVKALAKLNHPNIVRYYTAWVeePPLYIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTACDI--- 182
Cdd:cd13996  85 LCEGGTLRDWIDRRNSSSKNDRKLALELFKQILKGVSYIHSKG---IVHRDLKPSNIFLDNDDLQVKIGDFGLATSIgnq 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 ---QTHMTNN-----------KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiggpAFRIMWAVHNGTR 248
Cdd:cd13996 162 kreLNNLNNNnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAME----RSTILTDLRNGIL 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 249 PPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd13996 238 PESFKAKHPKEADLIQSLLSKNPEERPSAEQL 269
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
30-287 2.74e-43

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 155.59  E-value: 2.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERK-AFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEY 106
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVMLGDYRGQKVAVKCLKDDSTAAqAFLAEASVMTTLRHPNLVQLLGVVLegNGLYIVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTHM 186
Cdd:cd05039  82 MAKGSLVDYLRSRGRA-VITRKDQLGFALDVCEGMEYLES---KKFVHRDLAARNVLVSEDN-VAKVSDFGLAKEASSNQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPIESLMTR 265
Cdd:cd05039 157 DGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRI--PLKDVVPHVEKGYRMEAPEGCPPEVYKVMKN 234
                       250       260
                ....*....|....*....|..
gi 21735562 266 CWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd05039 235 CWELDPAKRPTFKQLREKLEHI 256
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
32-279 4.89e-43

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 155.23  E-value: 4.89e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESE----RKAFIVELrQLSRVNHPNIVKLYGA--CLNPVCL--- 102
Cdd:cd13979   1 DWEPLRLQEPLGSGGFGSVYKATYKGETVAVKIVRRRRKnrasRQSFWAEL-NAARLRHENIVRVLAAetGTDFASLgli 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHG-AEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTA-- 179
Cdd:cd13979  80 IMEYCGNGTLQQLIYEgSEPLP---LAHRILISLDIARALRFCHS---HGIVHLDVKPANIL-ISEQGVCKLCDFGCSvk 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 ----CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKNL 255
Cdd:cd13979 153 lgegNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLR--QHVLYAVVAKDLRPDLSGLE 230
                       250       260
                ....*....|....*....|....*...
gi 21735562 256 PKPI----ESLMTRCWSKDPSQRPSMEE 279
Cdd:cd13979 231 DSEFgqrlRSLISRCWSAQPAERPNADE 258
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
31-276 7.89e-42

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 151.64  E-value: 7.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKD-VAIKQI-ESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05112   1 IDPSELTFVQEIGSGQFGLVHLGYWLNKDkVAIKTIrEGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEqaPICLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTAC----DI 182
Cdd:cd05112  81 MEHGCLSDYLRTQRGL--FSAETLLGMCLDVCEGMAYLEE---ASVIHRDLAARNCL-VGENQVVKVSDFGMTRfvldDQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFD-EIGGPAFRIMWAVHNGTRPPLIknlPKPIE 260
Cdd:cd05112 155 YTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEgKIPYEnRSNSEVVEDINAGFRLYKPRLA---STHVY 231
                       250
                ....*....|....*.
gi 21735562 261 SLMTRCWSKDPSQRPS 276
Cdd:cd05112 232 EIMNHCWKERPEDRPS 247
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
42-284 8.45e-42

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 151.73  E-value: 8.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD-----VAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLNP-VCLVMEYAEGGSL 112
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSgkeveVAVKTLKQEHEkagKKEFLREASVMAQLDHPCIVRLIGVCKGEpLMLVMELAPLGPL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAeplPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG------TACDIQTHM 186
Cdd:cd05060  83 LKYLKKR---REIPVSDLKELAHQVAMGMAYLES---KHFVHRDLAARNVLLVNRHQA-KISDFGmsralgAGSDYYRAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIESLMTR 265
Cdd:cd05060 156 TAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYgAKPYGEMKGP--EVIAMLESGERLPRPEECPQEIYSIMLS 233
                       250
                ....*....|....*....
gi 21735562 266 CWSKDPSQRPSMEEIVKIM 284
Cdd:cd05060 234 CWKYRPEDRPTFSELESTF 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
37-286 1.28e-41

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 150.70  E-value: 1.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIeseseRKAFIVEL---RQL-------SRVNHPNIVKLYGACLNP--VCL 102
Cdd:cd14007   3 EIGKPLGKGKFGNVYLAREKKSGfiVALKVI-----SKSQLQKSgleHQLrreieiqSHLRHPNILRLYGYFEDKkrIYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACdi 182
Cdd:cd14007  78 ILEYAPNGELYKELKKQKRFDEKEAAKYI---YQLALALDYLHS---KNIIHRDIKPENILLGSNG-ELKLADFGWSV-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 qtHMTNNK-----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfrIMWAVHNGtRPPLIKNLPK 257
Cdd:cd14007 149 --HAPSNRrktfcGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQE--TYKRIQNV-DIKFPSSVSP 223
                       250       260
                ....*....|....*....|....*....
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd14007 224 EAKDLISKLLQKDPSKRLSLEQ---VLNH 249
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
40-282 2.38e-41

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 150.29  E-value: 2.38e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAK--DVAIKQIESE---SERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSL 112
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDntEVAVKTCRETlppDLKRKFLQEARILKQYDHPNIVKLIGVCVQkqPIMIVMELVPGGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHM-TNNKG 191
Cdd:cd05041  81 LTFLRKKGA--RLTVKQLLQMCLDAAAGMEYLES---KNCIHRDLAARNCL-VGENNVLKISDFGMSREEEDGEyTVSDG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 192 ----SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPAFRIMwaVHNGTRPPLIKNLPKPIESLMTRC 266
Cdd:cd05041 155 lkqiPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLgATPYPGMSNQQTREQ--IESGYRMPAPELCPEAVYRLMLQC 232
                       250
                ....*....|....*.
gi 21735562 267 WSKDPSQRPSMEEIVK 282
Cdd:cd05041 233 WAYDPENRPSFSEIYN 248
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
43-284 3.69e-40

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 147.76  E-value: 3.69e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRAKDVAIK--QIESESER------------------KAFiVELRQ----LSRVNHPNIVKLYGACLN 98
Cdd:cd14000   3 GDGGFGSVYRASYKGEPVAVKifNKHTSSNFanvpadtmlrhlratdamKNF-RLLRQeltvLSHLHHPSIVYLLGIGIH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 PVCLVMEYAEGGSLYNVL-HGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLL----VAGGTVLKI 173
Cdd:cd14000  82 PLMLVLELAPLGSLDHLLqQDSRSFASLGRTLQQRIALQVADGLRYLHS---AMIIYRDLKSHNVLVwtlyPNSAIIIKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTAcdIQTHMTNNKGSA---AWMAPEVFEGS-NYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNGTRP 249
Cdd:cd14000 159 ADYGIS--RQCCRMGAKGSEgtpGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM--VGHLKFPNEFDIHGGLRP 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 250 PLIK---NLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd14000 235 PLKQyecAPWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
35-289 8.33e-40

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 146.34  E-value: 8.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHG-DVAIKLLNidylNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPphLAIVTSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlkICDFG---TACDIQTH 185
Cdd:cd14063  80 GRTLYSLIH--ERKEKFDFNKTVQIAQQICQGMGYLHA---KGIIHKDLKSKNIFLENGRVV--ITDFGlfsLSGLLQPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK-----GSAAWMAPEV----------FEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNGTRPP 250
Cdd:cd14063 153 RREDTlvipnGWLCYLAPEIiralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQ--PAESIIWQVGCGKKQS 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 251 L-IKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14063 231 LsQLDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERLPK 270
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
42-284 2.51e-39

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 145.25  E-value: 2.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKwrAKD----------VAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEY 106
Cdd:cd05044   3 LGSGAFGEVFEGT--AKDilgdgsgetkVAVKTLRkgaTDQEKAEFLKEAHLMSNFKHPNILKLLGVCLdnDPQYIILEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPL----PYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGT---VLKICDFGTA 179
Cdd:cd05044  81 MEGGDLLSYLRAARPTaftpPLLTLKDLLSICVDVAKGCVYLEDMH---FVHRDLAARNCLVSSKDYrerVVKIGDFGLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeiggPA---FRIMWAVHNGTR-- 248
Cdd:cd05044 158 RDIYKNDYYRKEGEGllpvrWMAPESLVDGVFTTQSDVWAFGVLMWEILTLgQQPY-----PArnnLEVLHFVRAGGRld 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 249 -PPlikNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05044 233 qPD---NCPDDLYELMLRCWSTDPEERPSFARILEQL 266
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
34-282 2.69e-39

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 144.72  E-value: 2.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEG 109
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKetGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFknTDLWIVMEYCGA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAE-PLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTN 188
Cdd:cd06612  83 GSVSDIMKITNkTL---TEEEIAAILYQTLKGLEYLHSNK---KIHRDIKAGNILLNEEGQA-KLADFGVSGQLTDTMAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVhnGTRPPliKNLPKPIE----- 260
Cdd:cd06612 156 RNtviGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDI--HPMRAIFMI--PNKPP--PTLSDPEKwspef 229
                       250       260
                ....*....|....*....|...
gi 21735562 261 -SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06612 230 nDFVKKCLVKDPEERPSAIQLLQ 252
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
35-282 3.32e-39

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 144.48  E-value: 3.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKwRAKD---VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVV-RKVDgrvYALKQIDisrmSRKMREEAIDEARVLSKLNSPYVIKYYDSFVdkGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHG--AEPLPYYTAahamsW--CLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTA-- 179
Cdd:cd08529  80 YAENGDLHSLIKSqrGRPLPEDQI-----WkfFIQTLLGLSHLHS---KKILHRDIKSMNIFLDKGDNV-KIGDLGVAki 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD--EIGGPAFRIMwavhNGTRPPLIKNLP 256
Cdd:cd08529 151 LSDTTNFAQTIvGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEaqNQGALILKIV----RGKYPPISASYS 226
                       250       260
                ....*....|....*....|....*.
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd08529 227 QDLSQLIDSCLTKDYRQRPDTTELLR 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
35-286 4.82e-39

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 144.41  E-value: 4.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06605   2 DLEYLGELGEGNGGVVSKVrhRPSGQIMAVKVIRLEIdeaLQKQILRELDVLHKCNSPYIVGFYGAFYseGDISICMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLP-YYTAAHAmswcLQCSQGVAYLHSMQpkALIHRDLKPPNLLLVAGGTVlKICDFGtacdIQTHM 186
Cdd:cd06605  82 DGGSLDKILKEVGRIPeRILGKIA----VAVVKGLIYLHEKH--KIIHRDVKPSNILVNSRGQV-KLCDFG----VSGQL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNK-----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPA----FRIMWAVHNGTrPPLIKN--L 255
Cdd:cd06605 151 VDSLaktfvGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmiFELLSYIVDEP-PPLLPSgkF 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd06605 230 SPDFQDFVSQCLQKDPTERPSYKE---LMEH 257
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
42-291 5.84e-39

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 144.68  E-value: 5.84e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK---WRAKdVAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGS 111
Cdd:cd14026   5 LSRGAFGTVSRARhadWRVT-VAIKCLKldspvGDSERNCLLKEAEILHKARFSYILPILGICNEPefLGIVTEYMTNGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPLPyytaahAMSWCL------QCSQGVAYLHSMQPkALIHRDLKPPNLLLvAGGTVLKICDFGTACDIQTH 185
Cdd:cd14026  84 LNELLHEKDIYP------DVAWPLrlrilyEIALGVNYLHNMSP-PLLHHDLKTQNILL-DGEFHVKIADFGLSKWRQLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAA--------WMAPEVFEGSNYSE---KCDVFSWGIILWEVITRRKPFDEIGGPaFRIMWAVHNGTRPPL-IK 253
Cdd:cd14026 156 ISQSRSSKSapeggtiiYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKIPFEEVTNP-LQIMYSVSQGHRPDTgED 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 254 NLPKPIE------SLMTRCWSKDPSQRPSMEEIVKIMTHLMRYF 291
Cdd:cd14026 235 SLPVDIPhratliNLIESGWAQNPDERPSFLKCLIELEPVLRTF 278
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
30-281 6.70e-39

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 144.07  E-value: 6.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKD-------VAIK---QIESESERKAFIVELRQLSRVNHPNIVKLYGACLN- 98
Cdd:cd05036   2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPgdpsplqVAVKtlpELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 -PVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAY-LHSMQPKALIHRDLKPPNLLLVAGGT--VLKIC 174
Cdd:cd05036  82 lPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAQDVAKgCRYLEENHFIHRDIAARNCLLTCKGPgrVAKIG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 175 DFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTR 248
Cdd:cd05036 162 DFGMARDIYRADYYRKGGKAmlpvkWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLgYMPYP--GKSNQEVMEFVTSGGR 239
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 249 --PPliKNLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05036 240 mdPP--KNCPGPVYRIMTQCWQHIPEDRPNFSTIL 272
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
30-282 1.40e-38

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 143.71  E-value: 1.40e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKD--------VAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACL 97
Cdd:cd05053   8 ELPRDRLTLGKPLGEGAFGQVVKAEAVGLDnkpnevvtVAVKMLKddaTEKDLSDLVSEMEMMKMIgKHKNIINLLGACT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 N--PVCLVMEYAEGGSLYNVLHGAEPLPYY-------------TAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNL 162
Cdd:cd05053  88 QdgPLYVVVEYASKGNLREFLRARRPPGEEaspddprvpeeqlTQKDLVSFAYQVARGMEYLAS---KKCIHRDLAARNV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 163 LlVAGGTVLKICDFGTACDIQT-----HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIGGPA 236
Cdd:cd05053 165 L-VTEDNVMKIADFGLARDIHHidyyrKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 237 -FRIMWAVHNGTRPPlikNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05053 244 lFKLLKEGHRMEKPQ---NCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
40-281 2.65e-38

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 142.10  E-value: 2.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKW-----RAKDVAIKQIESESERKA-----FIVELRQLSRVNHPNIVKLYGACL-NPVCLVMEYAE 108
Cdd:cd05040   1 EKLGDGSFGVVRRGEWttpsgKVIQVAVKCLKSDVLSQPnamddFLKEVNAMHSLDHPNLIRLYGVVLsSPLMMVTELAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG--TACDIQTHM 186
Cdd:cd05040  81 LGSLLDRLR--KDQGHFLISTLCDYAVQIANGMAYLES---KRFIHRDLAARNILLASKDKV-KIGDFGlmRALPQNEDH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 ----TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeIGGPAFRIMWAV-HNGTRPPLIKNLPKPIE 260
Cdd:cd05040 155 yvmqEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYgEEPW--LGLNGSQILEKIdKEGERLERPDDCPQDIY 232
                       250       260
                ....*....|....*....|.
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05040 233 NVMLQCWAHKPADRPTFVALR 253
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
31-287 2.87e-38

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 142.13  E-value: 2.87e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAK-----DVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPV 100
Cdd:cd05033   1 IDASYVTIEKVIGGGEFGEVCSGSLKLPgkkeiDVAIKTLKsgySDKQRLDFLTEASIMGQFDHPNVIRLEGVVTksRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLlVAGGTVLKICDFGTAC 180
Cdd:cd05033  81 MIVTEYMENGSLDKFLRENDG--KFTVTQLVGMLRGIASGMKYLSEM---NYVHRDLAARNIL-VNSDLVCKVSDFGLSR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQ----THMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKN 254
Cdd:cd05033 155 RLEdseaTYTTKGgKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYgERPYWDMSNQ--DVIKAVEDGYRLPPPMD 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd05033 233 CPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
40-280 4.50e-38

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 141.48  E-value: 4.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAK---WRAkDVAIKQIES----ESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSL 112
Cdd:cd14025   2 EKVGSGGFGQVYKVRhkhWKT-WLAIKCPPSlhvdDSERMELLEEAKKMEMAKFRHILPVYGICSEPVGLVMEYMETGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLhGAEPLPY---YTAAHamswclQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVlKICDFGTA-CDIQTH--- 185
Cdd:cd14025  81 EKLL-ASEPLPWelrFRIIH------ETAVGMNFLHCMKP-PLLHLDLKPANILLDAHYHV-KISDFGLAkWNGLSHshd 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 --MTNNKGSAAWMAPEVFEGSN--YSEKCDVFSWGIILWEVITRRKPFDEIGGpAFRIMWAVHNGTRP---PLIKNLPKP 258
Cdd:cd14025 152 lsRDGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAGENN-ILHIMVKVVKGHRPslsPIPRQRPSE 230
                       250       260
                ....*....|....*....|....*
gi 21735562 259 ---IESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14025 231 cqqMICLMKRCWDQDPRKRPTFQDI 255
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
36-288 6.62e-38

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 142.02  E-value: 6.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKA-----KWRA--KDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLV 103
Cdd:cd05045   2 LVLGKTLGEGEFGKVVKAtafrlKGRAgyTTVAVKMLKenaSSSELRDLLSEFNLLKQVNHPHVIKLYGACSQdgPLLLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLH------------------------GAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKP 159
Cdd:cd05045  82 VEYAKYGSLRSFLResrkvgpsylgsdgnrnssyldnpDERAL---TMGDLISFAWQISRGMQYLAEMK---LVHRDLAA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 160 PNlLLVAGGTVLKICDFGTACDI---QTHMTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIg 233
Cdd:cd05045 156 RN-VLVAEGRKMKISDFGLSRDVyeeDSYVKRSKGRipVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGI- 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 234 gPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05045 234 -APERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
34-289 6.65e-38

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 141.40  E-value: 6.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVE--EVVGRGAFGVVCKAKWRAK------DVAIKQIESESERKAFIVELRQ---LSRVNHPNIVKLYGACLNP-VC 101
Cdd:cd05057   5 KETELEkgKVLGSGAFGTVYKGVWIPEgekvkiPVAIKVLREETGPKANEEILDEayvMASVDHPHLVRLLGICLSSqVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC- 180
Cdd:cd05057  85 LITQLMPLGCLLDYVR--NHRDNIGSQLLLNWCVQIAKGMSYL---EEKRLVHRDLAARNVLVKTPNHV-KITDFGLAKl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 ----DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRppliknL 255
Cdd:cd05057 159 ldvdEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGI--PAVEIPDLLEKGER------L 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 256 PKP------IESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05057 231 PQPpictidVYMVLVKCWMIDAESRPTFKELANEFSKMAR 270
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
42-283 1.46e-37

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 140.13  E-value: 1.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKDV--AIK---QIESESERKAFIVELRQ----LSRVNHPNIVKLYGACLNPV---CLVMEYA 107
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVlyAVKeyrRRDDESKRKDYVKRLTSeyiiSSKLHHPNIVKVLDLCQDLHgkwCLVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAhamswCL--QCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTH 185
Cdd:cd13994  81 PGGDLFTLIEKADSLSLEEKD-----CFfkQILRGVAYLHSH---GIAHRDLKPENILLDEDG-VLKLTDFGTAEVFGMP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK-------GSAAWMAPEVFEGSNYSEK-CDVFSWGIILWEVITRRKPF-----DEIGGPAFRIMWAVHNGTRPPLI 252
Cdd:cd13994 152 AEKESpmsaglcGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWrsakkSDSAYKAYEKSGDFTNGPYEPIE 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVKI 283
Cdd:cd13994 232 NLLPSECRRLIYRMLHPDPEKRITIDEALND 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-380 1.53e-37

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 143.34  E-value: 1.53e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKwRAKDVAIKQIESESERKAFIV-----ELRQLSRVNHP-NIVKLYGAC--LNPVCLVMEYAE 108
Cdd:COG0515   3 RILRKLGEGSFGEVYLAR-DRKLVALKVLAKKLESKSKEVerflrEIQILASLNHPpNIVKLYDFFqdEGSLYLVMEYVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTAC-------- 180
Cdd:COG0515  82 GGSLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKG---IIHRDIKPENILLDRDGRVVKLIDFGLAKllpdpgst 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -DIQTHMTNNKGSAAWMAPEVFEGSN---YSEKCDVFSWGIILWEVITRRKPFDEIGGP-----AFRIMW-AVHNGTRPP 250
Cdd:COG0515 159 sSIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSsatsqTLKIILeLPTPSLASP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 251 LIKNLPKP----IESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADE-----PLQYPCQYSDEGQSNSATSTGSFMD 321
Cdd:COG0515 239 LSPSNPELiskaASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLsdllkPDDSAPLRLSLPPSLEALISSLNSL 318
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 322 IASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLP 380
Cdd:COG0515 319 AISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSS 377
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
30-284 1.68e-37

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 140.17  E-value: 1.68e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVV-------CKAKWRAKDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL-- 97
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVyeglakgVVKGEPETRVAIKTVnenASMRERIEFLNEASVMKEFNCHHVVRLLGVVStg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVCLVMEYAEGGSLYNVLHGAEP-------LPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV 170
Cdd:cd05032  82 QPTLVVMELMAKGDLKSYLRSRRPeaennpgLGPPTLQKFIQMAAEIADGMAYLAA---KKFVHRDLAARNCMVAEDLTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 171 lKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFdeIGGPAFRIMWAVH 244
Cdd:cd05032 159 -KIGDFGMTRDIYETDYYRKGGKGllpvrWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPY--QGLSNEEVLKFVI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 245 NGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05032 236 DGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSL 275
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
42-280 2.12e-37

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 139.45  E-value: 2.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP-VCLVMEYAEGGSLYNVL 116
Cdd:cd14062   1 IGSGSFGTVYKGRWHG-DVAVKKLNvtdpTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPqLAIVTQWCEGSSLYKHL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 117 HGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACdIQTHMTNNK------ 190
Cdd:cd14062  80 HVLET--KFEMLQLIDIARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEDLTV-KIGDFGLAT-VKTRWSGSQqfeqpt 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNG-TRPPLIK---NLPKPIESLM 263
Cdd:cd14062 153 GSILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRD-QILFMVGRGyLRPDLSKvrsDTPKALRRLM 231
                       250
                ....*....|....*..
gi 21735562 264 TRCWSKDPSQRPSMEEI 280
Cdd:cd14062 232 EDCIKFQRDERPLFPQI 248
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
30-280 2.15e-37

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 140.55  E-value: 2.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVV--CKA-------------KWRAKD---VAIKQIESESE---RKAFIVELRQLSRVNHPN 88
Cdd:cd05051   1 EFPREKLEFVEKLGEGQFGEVhlCEAnglsdltsddfigNDNKDEpvlVAVKMLRPDASknaREDFLKEVKIMSQLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  89 IVKLYGACLN--PVCLVMEYAEGGSLYNVLHGAEP---LPYYTAAHAMSW------CLQCSQGVAYLHSMQpkaLIHRDL 157
Cdd:cd05051  81 IVRLLGVCTRdePLCMIVEYMENGDLNQFLQKHEAetqGASATNSKTLSYgtllymATQIASGMKYLESLN---FVHRDL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 158 KPPNLLLVAGGTVlKICDFGT-----ACD---IQthmtnnkGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT- 224
Cdd:cd05051 158 ATRNCLVGPNYTI-KIADFGMsrnlySGDyyrIE-------GRAVlpirWMAWESILLGKFTTKSDVWAFGVTLWEILTl 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 225 -RRKPFDEIG--------GPAFRimwavHNGT-----RPPlikNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05051 230 cKEQPYEHLTdeqvienaGEFFR-----DDGMevylsRPP---NCPKEIYELMLECWRRDEEDRPTFREI 291
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
32-282 2.68e-37

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 139.36  E-value: 2.68e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVVCKAKWRAKD--VAIKQIE-SESERKAFIV-ELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd06613   1 DYELIQR---IGSGTYGDVYKARNIATGelAAVKVIKlEPGDDFEIIQqEISMLKECRHPNIVAYFGSYLrrDKLWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAmswCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTH 185
Cdd:cd06613  78 YCGGGSLQDIYQVTGPLSELQIAYV---CRETLKGLAYLHSTG---KIHRDIKGANILLTEDGDV-KLADFGVSAQLTAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK---GSAAWMAPEVFE---GSNYSEKCDVFSWGIILWEVITRRKPFDEIgGPAFRIMWAVHNGTRPPLIKNLPK-- 257
Cdd:cd06613 151 IAKRKsfiGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQPPMFDL-HPMRALFLIPKSNFDPPKLKDKEKws 229
                       250       260
                ....*....|....*....|....*.
gi 21735562 258 -PIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06613 230 pDFHDFIKKCLTKNPKKRPTATKLLQ 255
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
31-288 3.97e-37

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 138.84  E-value: 3.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQI-ESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05114   1 INPSELTFMKELGSGLFGVVRLGKWRAQyKVAIKAIrEGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQqkPIYIVTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC----DI 182
Cdd:cd05114  81 MENGCLLNYLR--QRRGKLSRDMLLSMCQDVCEGMEYL---ERNNFIHRDLAARNCLVNDTGVV-KVSDFGMTRyvldDQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGGpaFRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05114 155 YTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKmPFESKSN--YEVVEMVSRGHRLYRPKLASKSVYE 232
                       250       260
                ....*....|....*....|....*..
gi 21735562 262 LMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05114 233 VMYSCWHEKPEGRPTFADLLRTITEIA 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
41-291 4.05e-37

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 138.64  E-value: 4.05e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVV--CKAKWRAKDVAIKQIESE-------SERKAFIVELRQLSRVNHPNIVKLYGaCL---NPVCLVMEYAE 108
Cdd:cd06625   7 LLGQGAFGQVylCYDADTGRELAVKQVEIDpinteasKEVKALECEIQLLKNLQHERIVQYYG-CLqdeKSLSIFMEYMP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL--HGAeplpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT-- 184
Cdd:cd06625  86 GGSVKDEIkaYGA-----LTENVTRKYTRQILEGLAYLHSNM---IVHRDIKGANILRDSNGNV-KLGDFGASKRLQTic 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 ---HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPA--FRImwAVHNgTRPPLIKNLPKPI 259
Cdd:cd06625 157 sstGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAaiFKI--ATQP-TNPQLPPHVSEDA 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 260 ESLMTRCWSKDPSQRPSMEEivkimthLMRYF 291
Cdd:cd06625 234 RDFLSLIFVRNKKQRPSAEE-------LLSHS 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
43-280 6.03e-37

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 138.45  E-value: 6.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQ----------------LSRVNHPNIVKLYGACLNP----V 100
Cdd:cd14008   2 GRGSFGKVKLALDTETGqlYAIKIFNKSRLRKRREGKNDRgkiknalddvrreiaiMKKLDHPNIVRLYEVIDDPesdkL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPLPYyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAc 180
Cdd:cd14008  82 YLVLEYCEGGPVMELDSGDRVPPL-PEETARKYFRDLVLGLEYLHE---NGIVHRDIKPENLLLTADGTV-KISDFGVS- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 diqtHM--------TNNKGSAAWMAPEVFEGSN--YS-EKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRP 249
Cdd:cd14008 156 ----EMfedgndtlQKTAGTPAFLAPELCDGDSktYSgKAADIWALGVTLYCLVFGRLPFN--GDNILELYEAIQNQNDE 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 250 PLI-KNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14008 230 FPIpPELSPELKDLLRRMLEKDPEKRITLKEI 261
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
37-280 5.36e-36

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 135.60  E-value: 5.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKwRAKD---VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd08530   3 KVLKKLGKGSYGSVYKVK-RLSDnqvYALKEVNlgslSQKEREDSVNEIRLLASVNHPNIIRYKEAFLdgNRLCIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAE----PLPyytaaHAMSW--CLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACD 181
Cdd:cd08530  82 PFGDLSKLISKRKkkrrLFP-----EDDIWriFIQMLRGLKALHDQK---ILHRDLKSANILLSAGD-LVKIGDLGISKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIMwavhNGTRPPLIKNLPKP 258
Cdd:cd08530 153 LKKNLAKTQiGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFeaRTMQELRYKVC----RGKFPPIPPVYSQD 228
                       250       260
                ....*....|....*....|..
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd08530 229 LQQIIRSLLQVNPKKRPSCDKL 250
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
40-282 5.47e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 136.02  E-value: 5.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVvCkakWRAKDV------AIKQI--------ESESERKAFIVELRQLSRVNHPNIVKLYGAC-----LNpv 100
Cdd:cd06630   6 PLLGTGAFSS-C---YQARDVktgtlmAVKQVsfcrnsssEQEEVVEAIREEIRMMARLNHPNIVRMLGATqhkshFN-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 cLVMEYAEGGSLYNVLHGAEPlpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTAC 180
Cdd:cd06630  80 -IFVEWMAGGSVASLLSKYGA---FSENVIINYTLQILRGLAYLHDNQ---IIHRDLKGANLLVDSTGQRLRIADFGAAA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNK-------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD--EIGGP---AFRImwAVHNGTr 248
Cdd:cd06630 153 RLASKGTGAGefqgqllGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNaeKISNHlalIFKI--ASATTP- 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 249 PPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06630 230 PPIPEHLSPGLRDVTLRCLELQPEDRPPARELLK 263
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
42-280 5.52e-36

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 135.43  E-value: 5.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQ----LSRVNHPNIVKLYG--ACLNPVCLVMEYAEGGSLY 113
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGevVAIKEISRKKLNKKLQENLESeiaiLKSIKHPNIVRLYDvqKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGT--VLKICDFGTAcdiqTHMTNNK- 190
Cdd:cd14009  81 QYIRKRGRLPEAVARHFM---QQLASGLKFLRS---KNIIHRDLKPQNLLLSTSGDdpVLKIADFGFA----RSLQPASm 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 -----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeiGGPAF-----RIMWAVHNgTRPPLIKNLPKPIE 260
Cdd:cd14009 151 aetlcGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF---RGSNHvqllrNIERSDAV-IPFPIAAQLSPDCK 226
                       250       260
                ....*....|....*....|
gi 21735562 261 SLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14009 227 DLLRRLLRRDPAERISFEEF 246
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
32-282 7.26e-36

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 135.56  E-value: 7.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVVCKAKW--RAKDVAIKQIESEsERKAFIVELRQ----LSRVNHPNIVKLYGACLNPVCL--V 103
Cdd:cd06610   2 DYELIEV---IGSGATAVVYAAYClpKKEKVAIKRIDLE-KCQTSMDELRKeiqaMSQCNHPNVVSYYTSFVVGDELwlV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEP---LPYYTAAHAMSWCLQcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAC 180
Cdd:cd06610  78 MPLLSGGSLLDIMKSSYPrggLDEAIIATVLKEVLK---GLEYLHS---NGQIHRDVKAGNILLGEDGSV-KIADFGVSA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNK-------GSAAWMAPEVFE-GSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNGTRPPL- 251
Cdd:cd06610 151 SLATGGDRTRkvrktfvGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYSKY--PPMKVLMLTLQNDPPSLe 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 252 ----IKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06610 229 tgadYKKYSKSFRKMISLCLQKDPSKRPTAEELLK 263
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
31-281 1.62e-35

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 134.24  E-value: 1.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQI-ESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRGQyDVAIKMIkEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKqrPIFIITEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTAC----DI 182
Cdd:cd05113  81 MANGCLLNYLR--EMRKRFQTQQLLEMCKDVCEAMEYLESKQ---FLHRDLAARNCLVNDQGVV-KVSDFGLSRyvldDE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05113 155 YTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKmPYERFTNS--ETVEHVSQGLRLYRPHLASEKVYT 232
                       250       260
                ....*....|....*....|
gi 21735562 262 LMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05113 233 IMYSCWHEKADERPTFKILL 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
40-282 2.02e-35

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 134.10  E-value: 2.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV-CKAKWRAKDVAIKQIE--------SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAE 108
Cdd:cd06631   7 NVLGKGAYGTVyCGLTSTGQLIAVKQVEldtsdkekAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLedNVVSIFMEFVP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLP-----YYTAahamswclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTA---C 180
Cdd:cd06631  87 GGSIASILARFGALEepvfcRYTK--------QILEGVAYLHN---NNVIHRDIKGNNIMLMPNG-VIKLIDFGCAkrlC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNN------KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAV--HNGTRPPLI 252
Cdd:cd06631 155 INLSSGSQSqllksmRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADM--NPMAAIFAIgsGRKPVPRLP 232
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06631 233 DKFSPEARDFVHACLTRDQDERPSAEQLLK 262
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-280 2.73e-35

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 133.70  E-value: 2.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVV--CKAKWRAKDVAIKQIESES----ERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLV 103
Cdd:cd08220   1 KYEKIRV---VGRGAYGTVylCRRKDDNKLVIIKQIPVEQmtkeERQAALNEVKVLSMLHHPNIIEYYESFLedKALMIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQ 183
Cdd:cd08220  78 MEYAPGGTLFEYIQQRKGS-LLSEEEILHFFVQILLALHHVHS---KQILHRDLKTQNILLNKKRTVVKIGDFGISKILS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF--RIMWAVHNGTRPPLIKNLPKPI 259
Cdd:cd08220 154 SKSKAYTvvGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALvlKIMRGTFAPISDRYSEELRHLI 233
                       250       260
                ....*....|....*....|.
gi 21735562 260 ESLMtrcwSKDPSQRPSMEEI 280
Cdd:cd08220 234 LSML----HLDPNKRPTLSEI 250
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
43-278 2.85e-35

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 133.18  E-value: 2.85e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRAK-DVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGAC--LNPVCLVMEYAEGGSLYNVLHG 118
Cdd:cd05034   4 GAGQFGEVWMGVWNGTtKVAVKTLKPGTmSPEAFLQEAQIMKKLRHDKLVQLYAVCsdEEPIYIVTELMSKGSLLDYLRT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 119 AE----PLP--YYTAAhamswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTA----CDIQTHMTN 188
Cdd:cd05034  84 GEgralRLPqlIDMAA-------QIASGMAYLESRN---YIHRDLAARNIL-VGENNVCKVADFGLArlieDDEYTAREG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIESLMTRCW 267
Cdd:cd05034 153 AKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYgRVPYPGMTNR--EVLEQVERGYRMPKPPGCPDELYDIMLQCW 230
                       250
                ....*....|.
gi 21735562 268 SKDPSQRPSME 278
Cdd:cd05034 231 KKEPEERPTFE 241
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
31-280 9.08e-35

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 131.92  E-value: 9.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACL-NPVCLVMEYAEG 109
Cdd:cd05083   3 LNLQKLTLGEIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILhNGLYIVMELMSK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVL--HGAEPLPYYtaaHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTHMT 187
Cdd:cd05083  83 GNLVNFLrsRGRALVPVI---QLLQFSLDVAEGMEYLES---KKLVHRDLAARNILVSEDG-VAKISDFGLAKVGSMGVD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGgpAFRIMWAVHNGTR--PPliKNLPKPIESLMT 264
Cdd:cd05083 156 NSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYgRAPYPKMS--VKEVKEAVEKGYRmePP--EGCPPDVYSIMT 231
                       250
                ....*....|....*.
gi 21735562 265 RCWSKDPSQRPSMEEI 280
Cdd:cd05083 232 SCWEAEPGKRPSFKKL 247
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
43-288 9.30e-35

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 132.89  E-value: 9.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRAKD------VAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLNP----VCLVMEYAEG 109
Cdd:cd05038  13 GEGHFGSVELCRYDPLGdntgeqVAVKSLQPSGEeqhMSDFKREIEILRTLDHEYIVKYKGVCESPgrrsLRLIMEYLPS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTA----CDIQTH 185
Cdd:cd05038  93 GSLRDYLQRHRD--QIDLKRLLLFASQICKGMEYLGSQR---YIHRDLAARNIL-VESEDLVKISDFGLAkvlpEDKEYY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP-------FDEIGGPAFRIMWAVH------NGTRPP 250
Cdd:cd05038 167 YVKEPGEspIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPsqsppalFLRMIGIAQGQMIVTRllellkSGERLP 246
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 251 LIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05038 247 RPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
30-284 1.10e-34

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 132.16  E-value: 1.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKD-----VAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACL-NPV 100
Cdd:cd05056   2 EIQREDITLGRCIGEGQFGDVYQGVYMSPEnekiaVAVKTCKNCTSpsvREKFLQEAYIMRQFDHPHIVKLIGVITeNPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLH-GAEPLPYYTAahaMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFG-- 177
Cdd:cd05056  82 WIVMELAPLGELRSYLQvNKYSLDLASL---ILYAYQLSTALAYLESKR---FVHRDIAARNVL-VSSPDCVKLGDFGls 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQTHMTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKN 254
Cdd:cd05056 155 RYMEDESYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMLgVKPFQ--GVKNNDVIGRIENGERLPMPPN 232
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05056 233 CPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
37-283 1.15e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 131.78  E-value: 1.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV---------CKAKWRA-KDVAIKQIEsESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd08222   3 RVVRKLGSGNFGTVylvsdlkatADEELKVlKEISVGELQ-PDETVDANREAKLLSKLDHPAIVKFHDSFVEKesFCIVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLH-----GAEPlpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGgtVLKICDFGTA 179
Cdd:cd08222  82 EYCEGGDLDDKISeykksGTTI----DENQILDWFIQLLLAVQYMHERR---ILHRDLKAKNIFLKNN--VIKVGDFGIS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 ------CDIQTHMTnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRPPLIK 253
Cdd:cd08222 153 rilmgtSDLATTFT---GTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFD--GQNLLSVMYKIVEGETPSLPD 227
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIVKI 283
Cdd:cd08222 228 KYSKELNAIYSRMLNKDPALRPSAAEILKI 257
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
41-281 1.23e-34

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 132.99  E-value: 1.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKA-------KWRAKDVAIKQIESE---SERKAFIVELRQLSRV-NHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd05055  42 TLGAGAFGKVVEAtayglskSDAVMKVAVKMLKPTahsSEREALMSELKIMSHLgNHENIVNLLGACTigGPILVITEYC 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGgTVLKICDFGTACDIQtHMT 187
Cdd:cd05055 122 CYGDLLNFLRRKRE-SFLTLEDLLSFSYQVAKGMAFLAS---KNCIHRDLAARNVLLTHG-KIVKICDFGLARDIM-NDS 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 N--NKGSA----AWMAPE-VFEGSnYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRIMWA-------VHNGTRPPLIK 253
Cdd:cd05055 196 NyvVKGNArlpvKWMAPEsIFNCV-YTFESDVWSYGILLWEIFS-------LGSNPYPGMPVdskfyklIKEGYRMAQPE 267
                       250       260
                ....*....|....*....|....*...
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05055 268 HAPAEIYDIMKTCWDADPLKRPTFKQIV 295
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
34-282 1.38e-34

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 131.98  E-value: 1.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQI---ESESErkafIVELRQ----LSRVNHPNIVKLYGACLNPVCL-- 102
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGidKRTNQVVAIKVIdleEAEDE----IEDIQQeiqfLSQCDSPYITKYYGSFLKGSKLwi 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHgAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI 182
Cdd:cd06609  77 IMEYCGGGSVLDLLK-PGPLDETYIAFIL---REVLLGLEYLHS---EGKIHRDIKAANILLSEEGDV-KLADFGVSGQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAV--HNgtrPPLIK--NL 255
Cdd:cd06609 149 TSTMSKRNtfvGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLH--PMRVLFLIpkNN---PPSLEgnKF 223
                       250       260
                ....*....|....*....|....*..
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06609 224 SKPFKDFVELCLNKDPKERPSAKELLK 250
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
37-229 1.47e-34

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 131.22  E-value: 1.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14002   4 HVLELIGEGSFGKVYKGRRKytGQVVALKFIpkrgKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKkeFVVVTEYAQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GgSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTA--CDIQTH- 185
Cdd:cd14002  84 G-ELFQILEDDGTLP---EEEVRSIAKQLVSALHYLHS---NRIIHRDMKPQNILIGKGG-VVKLCDFGFAraMSCNTLv 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14002 156 LTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPF 199
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
38-289 3.43e-34

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 130.77  E-value: 3.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVVCKAKWR----AKDVAIKQIeseSERKA---FIV-----ELRQLSRVNHPNIVKLYGA--CLNPVCLV 103
Cdd:cd14080   4 LGKTIGEGSYSKVKLAEYTksglKEKVACKII---DKKKApkdFLEkflprELEILRKLRHPNIIQVYSIfeRGSKVFIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSL--YNVLHGAEPlpyytAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTA-- 179
Cdd:cd14080  81 MEYAEHGDLleYIQKRGALS-----ESQARIWFRQLALAVQYLHSLD---IAHRDLKCENILLDSNNNV-KLSDFGFArl 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNK---GSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDEiggpafrimwavhngtrppliKNL 255
Cdd:cd14080 152 CPDDDGDVLSKtfcGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDD---------------------SNI 210
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14080 211 KKMLKDQQNRKVRFPSSVKKLSPECKDLIDQLLE 244
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
42-279 3.43e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 130.89  E-value: 3.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVckakWRAKDV------AIKQIE-SESERKAF--IV-ELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEG 109
Cdd:cd06626   8 IGEGTFGKV----YTAVNLdtgelmAMKEIRfQDNDPKTIkeIAdEMKVLEGLDHPNLVRYYGVEVhrEEVYIFMEYCQE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLP-----YYTaahamswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQT 184
Cdd:cd06626  84 GTLEELLRHGRILDeavirVYT--------LQLLEGLAYLHE---NGIVHRDIKPANIFLDSNG-LIKLGDFGSAVKLKN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMT--------NNKGSAAWMAPEVFEGSNYSEK---CDVFSWGIILWEVITRRKPFDEIGGPaFRIMWAVHNGTRPPLIK 253
Cdd:cd06626 152 NTTtmapgevnSLVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRPWSELDNE-WAIMYHVGMGHKPPIPD 230
                       250       260
                ....*....|....*....|....*...
gi 21735562 254 NLPKPIE--SLMTRCWSKDPSQRPSMEE 279
Cdd:cd06626 231 SLQLSPEgkDFLSRCLESDPKKRPTASE 258
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
42-291 3.71e-34

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 130.33  E-value: 3.71e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDV--AIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKlyAMKVL-----RKKEIIKRKEvehtlnerniLERVNHPFIVKLHYAFQTEekLYLVLDYV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLP-----YYTAahamswclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI 182
Cdd:cd05123  76 PGGELFSHLSKEGRFPeerarFYAA--------EIVLALEYLHS---LGIIYRDLKPENILLDSDGHI-KLTDFGLAKEL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMwavHNGTRPPLikNLPKPI 259
Cdd:cd05123 144 SSDGDRTYtfcGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFY--AENRKEIY---EKILKSPL--KFPEYV 216
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21735562 260 ----ESLMTRCWSKDPSQRPSMEEIVKIMTHlmRYF 291
Cdd:cd05123 217 speaKSLISGLLQKDPTKRLGSGGAEEIKAH--PFF 250
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
32-284 5.34e-34

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 130.30  E-value: 5.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVVCKAKWR--AKDVAIKQIESESERKafIVELRQLSRVNHPNIVKLYGA------CLNP---- 99
Cdd:cd14047   7 DFKEIEL---IGSGGFGQVFKAKHRidGKTYAIKRVKLNNEKA--EREVKALAKLDHPNIVRYNGCwdgfdyDPETsssn 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 ------VCLV--MEYAEGGSLYNVL--HGAEPLpYYTAAHAMSwcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGT 169
Cdd:cd14047  82 ssrsktKCLFiqMEFCEKGTLESWIekRNGEKL-DKVLALEIF--EQITKGVEYIHS---KKLIHRDLKPSNIFLVDTGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 170 VlKICDFG--TACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpafRIMWAVHNGT 247
Cdd:cd14047 156 V-KIGDFGlvTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKS----KFWTDLRNGI 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 248 RPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd14047 231 LPDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
42-282 5.35e-34

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 129.92  E-value: 5.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNVLH 117
Cdd:cd14065   1 LGKGFFGEVYKVTHRetGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVkdNKLNFITEYVNGGTLEELLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 GA-EPLPYYTAAHamsWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLL--VAGGTVLKICDFGTACDIQTHMTNNK---- 190
Cdd:cd14065  81 SMdEQLPWSQRVS---LAKDIASGMAYLHSKN---IIHRDLNSKNCLVreANRGRNAVVADFGLAREMPDEKTKKPdrkk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 -----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIGG---PAFRIMWavhngtrpplIKNLP 256
Cdd:cd14065 155 rltvvGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPadpdylPRTMDFGldvRAFRTLY----------VPDCP 224
                       250       260
                ....*....|....*....|....*.
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14065 225 PSFLPLAIRCCQLDPEKRPSFVELEH 250
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
40-280 7.26e-34

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 129.67  E-value: 7.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQIESE--SERKA-FIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRADNtpVAVKSCRETlpPDLKAkFLQEARILKQYSHPNIVRLIGVCTqkQPIYIVMELVQGGDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTAAHAMSWclQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGS 192
Cdd:cd05084  82 LTFLRTEGPRLKVKELIRMVE--NAAAGMEYLES---KHCIHRDLAARNCL-VTEKNVLKISDFGMSREEEDGVYAATGG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 -----AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPAFRImwAVHNGTRPPLIKNLPKPIESLMTRC 266
Cdd:cd05084 156 mkqipVKWTAPEALNYGRYSSESDVWSFGILLWETFSLgAVPYANLSNQQTRE--AVEQGVRLPCPENCPDEVYRLMEQC 233
                       250
                ....*....|....
gi 21735562 267 WSKDPSQRPSMEEI 280
Cdd:cd05084 234 WEYDPRKRPSFSTV 247
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
31-287 7.52e-34

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 129.72  E-value: 7.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP---VCLVMEYA 107
Cdd:cd05082   3 LNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEkggLYIVTEYM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLH-------GAEPLpyytaahaMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTAC 180
Cdd:cd05082  83 AKGSLVDYLRsrgrsvlGGDCL--------LKFSLDVCEAMEYLEG---NNFVHRDLAARN-VLVSEDNVAKVSDFGLTK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:cd05082 151 EASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRI--PLKDVVPRVEKGYKMDAPDGCPPAV 228
                       250       260
                ....*....|....*....|....*...
gi 21735562 260 ESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd05082 229 YDVMKNCWHLDAAMRPSFLQLREQLEHI 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-282 5.93e-33

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 126.58  E-value: 5.93e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAFIV-ELRQLSRVN----HPNIVKLYGA----CLNPVCLVME 105
Cdd:cd05118   2 EVLRKIGEGAFGTVWLARDKVtgEKVAIKKIKNDFRHPKAALrEIKLLKHLNdvegHPNIVKLLDVfehrGGNHLCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAeGGSLYNVL-HGAEPLPYYtaaHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTACDIQT 184
Cdd:cd05118  82 LM-GMNLYELIkDYPRGLPLD---LIKSYLYQLLQALDFLHSNG---IIHRDLKPENILINLELGQLKLADFGLARSFTS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAAW-MAPEV-FEGSNYSEKCDVFSWGIILWEVITRR------KPFDEIggpaFRImwavhngtrpplIKNL- 255
Cdd:cd05118 155 PPYTPYVATRWyRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRplfpgdSEVDQL----AKI------------VRLLg 218
                       250       260
                ....*....|....*....|....*..
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05118 219 TPEALDLLSKMLKYDPAKRITASQALA 245
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-282 7.40e-33

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 126.89  E-value: 7.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYkeiEVEEVVGRGAFGVVCKAKwRAKD---VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP----V 100
Cdd:cd08217   1 DY---EVLETIGKGSFGTVRKVR-RKSDgkiLVWKEIDygkmSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRanttL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMsW--CLQCSQGVAYLHSMQPK--ALIHRDLKPPNLLLVAGGTVlKICDF 176
Cdd:cd08217  77 YIVMEYCEGGDLAQLIKKCKKENQYIPEEFI-WkiFTQLLLALYECHNRSVGggKILHRDLKPANIFLDSDNNV-KLGDF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDIQTH--MTN-NKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMwaVHNGTRPPLIK 253
Cdd:cd08217 155 GLARVLSHDssFAKtYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKK--IKEGKFPRIPS 232
                       250       260
                ....*....|....*....|....*....
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd08217 233 RYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
39-282 7.84e-33

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 126.57  E-value: 7.84e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVVCKA--KWRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGA----CLNPVCLVMEYAE 108
Cdd:cd13983   6 NEVLGRGSFKTVYRAfdTEEGIEVAWNEIKlrklPKAERQRFKQEIEILKSLKHPNIIKFYDSweskSKKEVIFITELMT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL--HGAEPLPYYTaahamSWCLQCSQGVAYLHSMQPKaLIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHM 186
Cdd:cd13983  86 SGTLKQYLkrFKRLKLKVIK-----SWCRQILEGLNYLHTRDPP-IIHRDLKCDNIFINGNTGEVKIGDLGLATLLRQSF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNN-KGSAAWMAPEVFEGsNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKP-IESLMT 264
Cdd:cd13983 160 AKSvIGTPEFMAPEMYEE-HYDEKVDIYAFGMCLLEMATGEYPYSECTNAA-QIYKKVTSGIKPESLSKVKDPeLKDFIE 237
                       250
                ....*....|....*...
gi 21735562 265 RCwSKDPSQRPSMEEIVK 282
Cdd:cd13983 238 KC-LKPPDERPSARELLE 254
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
35-289 8.01e-33

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 127.06  E-value: 8.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP-VCLVMEYAEG 109
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRGKWHG-DVAVKILKvtepTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPnFAIITQWCEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACdIQTHMTNN 189
Cdd:cd14150  80 SSLYRHLHVTET--RFDTMQLIDVARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEGLTV-KIGDFGLAT-VKTRWSGS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K------GSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPP----LIKNLP 256
Cdd:cd14150 153 QqveqpsGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRD-QIIFMVGRGYLSPdlskLSSNCP 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14150 232 KAMKRLLIDCLKFKREERPLFPQILVSIELLQR 264
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
30-286 9.85e-33

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 127.26  E-value: 9.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAkwRAKD---------VAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACL 97
Cdd:cd05050   1 EYPRNNIEYVRDIGQGAFGRVFQA--RAPGllpyepftmVAVKMLKEEASadmQADFQREAALMAEFDHPNIVKLLGVCA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 --NPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQ-------------------GVAYLHSmqpKALIHRD 156
Cdd:cd05050  79 vgKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSSARKCGLnplplscteqlciakqvaaGMAYLSE---RKFVHRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 157 LKPPNLLlVAGGTVLKICDFGTACDI--QTHMTNNKGSAA---WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFd 230
Cdd:cd05050 156 LATRNCL-VGENMVVKIADFGLSRNIysADYYKASENDAIpirWMPPESIFYNRYTTESDVWAYGVVLWEIFSYgMQPY- 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 231 eIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTH 286
Cdd:cd05050 234 -YGMAHEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
31-288 1.02e-32

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 126.52  E-value: 1.02e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKD-----VAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPV 100
Cdd:cd05066   1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGkreipVAIKTLKagyTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTrsKPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVL--HGAEplpyYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLlVAGGTVLKICDFGT 178
Cdd:cd05066  81 MIVTEYMENGSLDAFLrkHDGQ----FTVIQLVGMLRGIASGMKYLSDM---GYVHRDLAARNIL-VNSNLVCKVSDFGL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 AC----DIQTHMTNNKGSAA--WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPL 251
Cdd:cd05066 153 SRvledDPEAAYTTRGGKIPirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYgERPYWEMSNQ--DVIKAIEEGYRLPA 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 252 IKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05066 231 PMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
36-287 1.32e-32

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 127.22  E-value: 1.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKAKW-------RAKDVAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACLN---PVC 101
Cdd:cd05054   9 LKLGKPLGRGAFGKVIQASAfgidksaTCRTVAVKMLKegaTASEHKALMTELKILIHIgHHLNVVNLLGACTKpggPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHGA--------------------------EPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHR 155
Cdd:cd05054  89 VIVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddelykEPL---TLEDLICYSFQVARGMEFLAS---RKCIHR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 156 DLKPPNLLLvAGGTVLKICDFGTACDIQTHMTN-NKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfd 230
Cdd:cd05054 163 DLAARNILL-SENNVVKICDFGLARDIYKDPDYvRKGDArlplKWMAPESIFDKVYTTQSDVWSFGVLLWEIFS------ 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 231 eIGG---PAFRIMWAVHN----GTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd05054 236 -LGAspyPGVQMDEEFCRrlkeGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLGDL 298
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
30-288 1.43e-32

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 126.19  E-value: 1.43e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKA-----KWRAKDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL--NP 99
Cdd:cd05064   1 ELDNKSIKIERILGTGRFGELCRGclklpSKRELPVAIHTLRagcSDKQRRGFLAEALTLGQFDHSNIVRLEGVITrgNT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLlVAGGTVLKICDFGTA 179
Cdd:cd05064  81 MMIVTEYMSNGALDSFLRKHEG--QLVAGQLMGMLPGLASGMKYLSEM---GYVHKGLAAHKVL-VNSDLVCKISGFRRL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CD-----IQTHMtNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIK 253
Cdd:cd05064 155 QEdkseaIYTTM-SGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYgERPYWDMSGQ--DVIKAVEDGFRLPAPR 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05064 232 NCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
42-289 4.88e-32

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 124.51  E-value: 4.88e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL--VMEYAEGGSLYNVLH 117
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGqvMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLhaLTEYINGGNLEQLLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 GAEPLPYYTAAHAmswCLQCSQGVAYLHSmqpKALIHRDLKPPNLLL--VAGGTVLKICDFGTACDIQTHMTNNK----- 190
Cdd:cd14155  81 SNEPLSWTVRVKL---ALDIARGLSYLHS---KGIFHRDLTSKNCLIkrDENGYTAVVGDFGLAEKIPDYSDGKEklavv 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIGG---PAFRIMwavhngtrpplIKNLPKPIES 261
Cdd:cd14155 155 GSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQadpdylPRTEDFGldyDAFQHM-----------VGDCPPDFLQ 223
                       250       260
                ....*....|....*....|....*...
gi 21735562 262 LMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14155 224 LAFNCCNMDPKSRPSFHDIVKTLEEILE 251
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
33-282 4.99e-32

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 125.17  E-value: 4.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIVELRQ---LSRVNHPNIVKLYGACLNPVCLV--ME 105
Cdd:cd14046   5 LTDFEELQVLGKGAFGQVVKVRNKldGRYYAIKKIKLRSESKNNSRILREvmlLSRLNHQHVVRYYQAWIERANLYiqME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAahamsWCL--QCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd14046  85 YCEKSTLRDLIDSGLFQDTDRL-----WRLfrQILEGLAYIHS---QGIIHRDLKPVNIFLDSNGNV-KIGDFGLATSNK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 TH---------------------MTNNKGSAAWMAPEVFEG--SNYSEKCDVFSWGIILWEVItrrKPFDEiGGPAFRIM 240
Cdd:cd14046 156 LNvelatqdinkstsaalgssgdLTGNVGTALYVAPEVQSGtkSTYNEKVDMYSLGIIFFEMC---YPFST-GMERVQIL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21735562 241 WAVHN--GTRPPLIKNLPKPIESLMTRC-WSKDPSQRPSMEEIVK 282
Cdd:cd14046 232 TALRSvsIEFPPDFDDNKHSKQAKLIRWlLNHDPAKRPSAQELLK 276
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
30-278 6.08e-32

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 124.44  E-value: 6.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKW-RAKDVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd05068   4 EIDRKSLKLLRKLGSGQFGEVWEGLWnNTTPVAVKTLKPGTmDPEDFLREAQIMKKLRHPKLIQLYAVCTleEPIYIITE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHG---AEPLPYYTAAHAmswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTA--- 179
Cdd:cd05068  84 LMKHGSLLEYLQGkgrSLQLPQLIDMAA-----QVASGMAYLESQN---YIHRDLAARNVL-VGENNICKVADFGLArvi 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 --CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd05068 155 kvEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYgRIPYP--GMTNAEVLQQVERGYRMPCPPNCP 232
                       250       260
                ....*....|....*....|..
gi 21735562 257 KPIESLMTRCWSKDPSQRPSME 278
Cdd:cd05068 233 PQLYDIMLECWKADPMERPTFE 254
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
40-280 6.56e-32

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 124.05  E-value: 6.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAkWRAKD---VAIKQ---IESESERKAFIVELRQ----LSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06632   6 QLLGSGSFGSVYEG-FNGDTgdfFAVKEvslVDDDKKSRESVKQLEQeialLSKLRHPNIVQYYGTEReeDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPY-----YTAahamswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDI 182
Cdd:cd06632  85 PGGSIHKLLQRYGAFEEpvirlYTR--------QILSGLAYLHSRN---TVHRDIKGANILVDTNG-VVKLADFGMAKHV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 --QTHMTNNKGSAAWMAPEVF--EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFriMWAVHN-GTRPPLIKNLPK 257
Cdd:cd06632 153 eaFSFAKSFKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAA--IFKIGNsGELPPIPDHLSP 230
                       250       260
                ....*....|....*....|...
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd06632 231 DAKDFIRLCLQRDPEDRPTASQL 253
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
30-299 7.59e-32

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 124.86  E-value: 7.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWR--AKDVAIK--QIESESE-RKAFIVELRQLSRVNHPNIVKLYGACLNP---VC 101
Cdd:cd06620   1 DLKNQDLETLKDLGAGNGGSVSKVLHIptGTIMAKKviHIDAKSSvRKQILRELQILHECHSPYIVSFYGAFLNEnnnII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSMQpkALIHRDLKPPNLLLVAGGTVlKICDFGTACD 181
Cdd:cd06620  81 ICMEYMDCGSLDKILKKKGPFPEEVLGKIA---VAVLEGLTYLYNVH--RIIHRDIKPSNILVNSKGQI-KLCDFGVSGE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-------DEIGGPA--FRIMWAVHNGTRPPL 251
Cdd:cd06620 155 LINSIADTfVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFagsndddDGYNGPMgiLDLLQRIVNEPPPRL 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 252 IKN--LPKPIESLMTRCWSKDPSQRPSMEEIVKimthlMRYFPGADEPLQ 299
Cdd:cd06620 235 PKDriFPKDLRDFVDRCLLKDPRERPSPQLLLD-----HDPFIQAVRASD 279
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
37-282 7.79e-32

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 124.12  E-value: 7.79e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA------KWRAkdvaIKQIeseSERK---------AFIVELRQLSRVNHPNIVKLYGACLNP-- 99
Cdd:cd14098   3 QIIDRLGSGTFAEVKKAvevetgKMRA----IKQI---VKRKvagndknlqLFQREINILKSLEHPGIVRLIDWYEDDqh 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVL--HGAEPlpyytAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTV-LKICDF 176
Cdd:cd14098  76 IYLVMEYVEGGDLMDFImaWGAIP-----EQHARELTKQILEAMAYTHSM---GITHRDLKPENILITQDDPViVKISDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDIQ--THMTNNKGSAAWMAPEVFEGSN------YSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGT- 247
Cdd:cd14098 148 GLAKVIHtgTFLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFD--GSSQLPVEKRIRKGRy 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 248 -RPPLIK-NLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14098 226 tQPPLVDfNISEEAIDFILRLLDVDPEKRMTAAQALD 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-282 7.85e-32

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 124.51  E-value: 7.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAF------IVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEG 109
Cdd:cd06917   7 ELVGRGSYGAVYRGYHVKtgRVVALKVLNLDTDDDDVsdiqkeVALLSQLKLGQPKNIIKYYGSYLKgpSLWIIMDYCEG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHgAEPLPYYTAAHAMSWCLQcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNN 189
Cdd:cd06917  87 GSIRTLMR-AGPIAERYIAVIMREVLV---ALKFIHK---DGIIHRDIKAANILVTNTGNV-KLCDFGVAASLNQNSSKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K---GSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNgTRPPLI--KNLPKPIESLM 263
Cdd:cd06917 159 StfvGTPYWMAPEVItEGKYYDTKADIWSLGITTYEMATGNPPYSDV--DALRAVMLIPK-SKPPRLegNGYSPLLKEFV 235
                       250
                ....*....|....*....
gi 21735562 264 TRCWSKDPSQRPSMEEIVK 282
Cdd:cd06917 236 AACLDEEPKDRLSADELLK 254
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
30-276 9.87e-32

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 123.70  E-value: 9.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQIESESERKA--FIVELRQLSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:cd05148   2 ERPREEFTLERKLGSGYFGEVWEGLWKNRvRVAIKILKSDDLLKQqdFQKEVQALKRLRHKHLISLFAVCSvgEPVYIIT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQT 184
Cdd:cd05148  82 ELMEKGSLLAFLRSPEG-QVLPVASLIDMACQVAEGMAYLEE---QNSIHRDLAARNIL-VGEDLVCKVADFGLARLIKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HM---TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIE 260
Cdd:cd05148 157 DVylsSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQvPYP--GMNNHEVYDQITAGYRMPCPAKCPQEIY 234
                       250
                ....*....|....*.
gi 21735562 261 SLMTRCWSKDPSQRPS 276
Cdd:cd05148 235 KIMLECWAAEPEDRPS 250
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
41-284 1.59e-31

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 123.73  E-value: 1.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKD-------VAIKQIESESERK---AFIVELRQLSRVNHPNIVKLYGAC--LNPVCLVMEYAE 108
Cdd:cd05046  12 TLGRGEFGEVFLAKAKGIEeeggetlVLVKALQKTKDENlqsEFRRELDMFRKLSHKNVVRLLGLCreAEPHYMILEYTD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL----HGAEPL--PYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDI 182
Cdd:cd05046  92 LGDLKQFLratkSKDEKLkpPPLSTKQKVALCTQIALGMDHLSNAR---FVHRDLAARNCLVSSQREV-KVSLLSLSKDV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QT----HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGGPAF-------RIMWAVHNGTrpp 250
Cdd:cd05046 168 YNseyyKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGElPFYGLSDEEVlnrlqagKLELPVPEGC--- 244
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 251 liknlPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05046 245 -----PSRLYKLMTRCWAVNPKDRPSFSELVSAL 273
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
35-281 1.80e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 123.45  E-value: 1.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP---------- 99
Cdd:cd14048   7 DFEPIQCLGRGGFGVVFEAKNKVDDcnYAVKRIrlpNNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqekmd 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 ---VCLVMEYAEGGSLYNVLHGA---EPLPYYTAAHamsWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKI 173
Cdd:cd14048  87 evyLYIQMQLCRKENLKDWMNRRctmESRELFVCLN---IFKQIASAVEYLHS---KGLIHRDLKPSNVFFSLDDVV-KV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFG--TACD-------IQTHM------TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkPFDeIGGPAFR 238
Cdd:cd14048 160 GDFGlvTAMDqgepeqtVLTPMpayakhTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY---SFS-TQMERIR 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 239 IMWAVHNGTRPPLIKNlPKPIESLMT-RCWSKDPSQRPSMEEIV 281
Cdd:cd14048 236 TLTDVRKLKFPALFTN-KYPEERDMVqQMLSPSPSERPEAHEVI 278
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
28-289 1.88e-31

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 124.36  E-value: 1.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  28 FEEIDYKEIEVeevVGRGAFGVVCKAKWRAKD------VAIKQIESESERKA---FIVELRQLSRVNHPNIVKLYGACL- 97
Cdd:cd05108   4 LKETEFKKIKV---LGSGAFGTVYKGLWIPEGekvkipVAIKELREATSPKAnkeILDEAYVMASVDNPHVCRLLGICLt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVCLVMEYAEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLlVAGGTVLKICDFG 177
Cdd:cd05108  81 STVQLITQLMPFGCLLDYVR--EHKDNIGSQYLLNWCVQIAKGMNYL---EDRRLVHRDLAARNVL-VKTPQHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 -----TACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRppl 251
Cdd:cd05108 155 lakllGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGI--PASEISSILEKGER--- 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 252 iknLPKP------IESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05108 230 ---LPQPpictidVYMIMVKCWMIDADSRPKFRELIIEFSKMAR 270
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
37-282 4.91e-31

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 122.03  E-value: 4.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVE----LRQLSrvNHPNIVKLYGACLNPV--------CL 102
Cdd:cd06608   9 ELVEVIGEGTYGKVYKARHKKTGqlAAIKIMDIIEDEEEEIKLeiniLRKFS--NHPNIATFYGAFIKKDppggddqlWL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAHAMSW-CLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD 181
Cdd:cd06608  87 VMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYiLRETLRGLAYLHE---NKVIHRDIKGQNILLTEEAEV-KLVDFGVSAQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQThmTNNK-----GSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNGTRPPL 251
Cdd:cd06608 163 LDS--TLGRrntfiGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDM--HPMRALFKIPRNPPPTL 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 252 I--KNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06608 239 KspEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
60-285 7.42e-31

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 121.34  E-value: 7.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  60 VAIKQI-ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYNVLHGAEplpyytaaHAMSWCLQ 136
Cdd:cd13992  28 VAIKHItFSRTEKRTILQELNQLKELVHDNLNKFIGICINPpnIAVVTEYCTRGSLQDVLLNRE--------IKMDWMFK 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 137 CS------QGVAYLHSmQPKALiHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGSAA------WMAPEVFEGS 204
Cdd:cd13992 100 SSfikdivKGMNYLHS-SSIGY-HGRLKSSNCL-VDSRWVVKLTDFGLRNLLEEQTNHQLDEDAqhkkllWTAPELLRGS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 205 ----NYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAvHNGTRPPLI------KNLPKPIESLMTRCWSKDPSQR 274
Cdd:cd13992 177 llevRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVI-SGGNKPFRPelavllDEFPPRLVLLVKQCWAENPEKR 255
                       250
                ....*....|.
gi 21735562 275 PSMEEIVKIMT 285
Cdd:cd13992 256 PSFKQIKKTLT 266
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
30-289 8.13e-31

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 121.71  E-value: 8.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP-VCLVM 104
Cdd:cd14151   4 EIPDGQITVGQRIGSGSFGTVYKGKWHG-DVAVKMLNvtapTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPqLAIVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACdIQT 184
Cdd:cd14151  83 QWCEGSSLYHHLHIIET--KFEMIKLIDIARQTAQGMDYLHA---KSIIHRDLKSNNIFLHEDLTV-KIGDFGLAT-VKS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNN------KGSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLI--- 252
Cdd:cd14151 156 RWSGShqfeqlSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRD-QIIFMVGRGYLSPDLskv 234
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 253 -KNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14151 235 rSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR 272
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
40-285 1.03e-30

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 120.50  E-value: 1.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAK-DVAIKQIESE--SERK-AFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLY 113
Cdd:cd05085   2 ELLGKGNFGEVYKGTLKDKtPVAVKTCKEDlpQELKiKFLSEARILKQYDHPNIVKLIGVCTQrqPIYIVMELVPGGDFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKG-- 191
Cdd:cd05085  82 SFLRKKKD--ELKTKQLVKFSLDAAAGMAYLES---KNCIHRDLAARNCL-VGENNALKISDFGMSRQEDDGVYSSSGlk 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 192 --SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGGPAFRIMwaVHNGTRPPLIKNLPKPIESLMTRCWS 268
Cdd:cd05085 156 qiPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVcPYPGMTNQQAREQ--VEKGYRMSAPQRCPEDIYKIMQRCWD 233
                       250
                ....*....|....*..
gi 21735562 269 KDPSQRPSMEEIVKIMT 285
Cdd:cd05085 234 YNPENRPKFSELQKELA 250
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
36-282 1.65e-30

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 120.62  E-value: 1.65e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGR---GAFGVVCKAKWRAKDV--AIK--QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVM--EY 106
Cdd:cd06611   4 NDIWEIIGElgdGAFGKVYKAQHKETGLfaAAKiiQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWIliEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAE-PLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAC----D 181
Cdd:cd06611  84 CDGGALDSIMLELErGL---TEPQIRYVCRQMLEALNFLHS---HKVIHRDLKAGNILLTLDGDV-KLADFGVSAknksT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTnNKGSAAWMAPEV-----FEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIK--N 254
Cdd:cd06611 157 LQKRDT-FIGTPYWMAPEVvacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELN--PMRVLLKILKSEPPTLDQpsK 233
                       250       260
                ....*....|....*....|....*...
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06611 234 WSSSFNDFLKSCLVKDPDDRPTAAELLK 261
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
42-236 2.06e-30

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 120.68  E-value: 2.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQ------IESESERKAFIVELRQLSRVNHPNIVKLYG-ACLNP-VCLVMEYAEGGSLY 113
Cdd:cd14158  23 LGEGGFGVVFKGYINDKNVAVKKlaamvdISTEDLTKQFEQEIQVMAKCQHENLVELLGySCDGPqLCLVYTYMPNGSLL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPyytaahAMSWCLQC------SQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTA----CDIQ 183
Cdd:cd14158 103 DRLACLNDTP------PLSWHMRCkiaqgtANGINYLHE---NNHIHRDIKSANILL-DETFVPKISDFGLAraseKFSQ 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 184 THMTNN-KGSAAWMAPEVFEGSnYSEKCDVFSWGIILWEVITRRKPFDEIGGPA 236
Cdd:cd14158 173 TIMTERiVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDENRDPQ 225
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
40-287 2.21e-30

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 119.89  E-value: 2.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD-----VAIK---QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL---VMEYAE 108
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDSDgqkihCAVKslnRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSplvVLPYMK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI------ 182
Cdd:cd05058  81 HGDLRNFIRSETHNP--TVKDLIGFGLQVAKGMEYLAS---KKFVHRDLAARNCMLDESFTV-KVADFGLARDIydkeyy 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 --QTHmTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGgpAFRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:cd05058 155 svHNH-TGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRgAPPYPDVD--SFDITVYLLQGRRLLQPEYCPDPL 231
                       250       260
                ....*....|....*....|....*...
gi 21735562 260 ESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd05058 232 YEVMLSCWHPKPEMRPTFSELVSRISQI 259
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
37-282 2.54e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 119.68  E-value: 2.54e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESES----ERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAE 108
Cdd:cd08225   3 EIIKKIGEGSFGKIylAKAKSDSEHCVIKEIDLTKmpvkEKEASKKEVILLAKMKHPNIVTFFASFQenGRLFIVMEYCD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLY---NVLHGAeplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTH 185
Cdd:cd08225  83 GGDLMkriNRQRGV----LFSEDQILSWFVQISLGLKHIHD---RKILHRDIKSQNIFLSKNGMVAKLGDFGIARQLNDS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIESL 262
Cdd:cd08225 156 MELAYtcvGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE--GNNLHQLVLKICQGYFAPISPNFSRDLRSL 233
                       250       260
                ....*....|....*....|
gi 21735562 263 MTRCWSKDPSQRPSMEEIVK 282
Cdd:cd08225 234 ISQLFKVSPRDRPSITSILK 253
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
31-288 2.77e-30

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 119.97  E-value: 2.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKD-----VAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACLN--PV 100
Cdd:cd05065   1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPGkreifVAIKTLKsgyTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKsrPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTAC 180
Cdd:cd05065  81 MIITEFMENGALDSFLRQNDG--QFTVIQLVGMLRGIAAGMKYLSEMN---YVHRDLAARNIL-VNSNLVCKVSDFGLSR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAA--------WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPL 251
Cdd:cd05065 155 FLEDDTSDPTYTSSlggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYgERPYWDMSNQ--DVINAIEQDYRLPP 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 252 IKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05065 233 PMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
43-284 3.96e-30

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 118.90  E-value: 3.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPL 122
Cdd:cd14068   3 GDGGFGSVYRAVYRGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGSLDALLQQDNAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 123 PYYTAAHAMSwcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVA----GGTVLKICDFGTA---CDIQthMTNNKGSAAW 195
Cdd:cd14068  83 LTRTLQHRIA--LHVADGLRYLHSAM---IIYRDLKPHNVLLFTlypnCAIIAKIADYGIAqycCRMG--IKTSEGTPGF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 196 MAPEVFEGS-NYSEKCDVFSWGIILWEVIT--------RRKP--FDEIggpafrimwAVHnGTRPPLIKNL---PKP-IE 260
Cdd:cd14068 156 RAPEVARGNvIYNQQADVYSFGLLLYDILTcgerivegLKFPneFDEL---------AIQ-GKLPDPVKEYgcaPWPgVE 225
                       250       260
                ....*....|....*....|....
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd14068 226 ALIKDCLKENPQCRPTSAQVFDIL 249
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
33-292 4.83e-30

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 119.75  E-value: 4.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEV-----VGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYG-ACLNPVCL 102
Cdd:cd14149   6 YWEIEASEVmlstrIGSGSFGTVYKGKWHG-DVAVKILKvvdpTPEQFQAFRNEVAVLRKTRHVNILLFMGyMTKDNLAI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACdI 182
Cdd:cd14149  85 VTQWCEGSSLYKHLHVQET--KFQMFQLIDIARQTAQGMDYLHA---KNIIHRDMKSNNIFLHEGLTV-KIGDFGLAT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNK------GSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPP--- 250
Cdd:cd14149 158 KSRWSGSQqveqptGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRD-QIIFMVGRGYASPdls 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 251 -LIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFP 292
Cdd:cd14149 237 kLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLP 279
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
42-285 5.82e-30

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 119.14  E-value: 5.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKW-RAKDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYAEGGSLYNV 115
Cdd:cd14664   1 IGRGGAGTVYKGVMpNGTLVAVKRLKGEGtqgGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTtnLLVYEYMPNGSLGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEPlpyytAAHAMSW------CLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC---DIQTH- 185
Cdd:cd14664  81 LHSRPE-----SQPPLDWetrqriALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEA-HVADFGLAKlmdDKDSHv 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGP-AFRIMWAVHNGTRPPLIKNLPKP------ 258
Cdd:cd14664 155 MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDdGVDIVDWVRGLLEEKKVEALVDPdlqgvy 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 259 -IESLMT------RCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd14664 235 kLEEVEQvfqvalLCTQSSPMERPTMREVVRMLE 268
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
40-274 1.54e-29

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 118.62  E-value: 1.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKqIESESERKAFIVE--LRQLSRVNHPNIVKLYGACLNPVC-------LVMEYAEGG 110
Cdd:cd14054   1 QLIGQGRYGTVWKGSLDERPVAVK-VFPARHRQNFQNEkdIYELPLMEHSNILRFIGADERPTAdgrmeylLVLEYAPKG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHgaeplpyytaAHAMSW------CLQCSQGVAYLHS-----MQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGT 178
Cdd:cd14054  80 SLCSYLR----------ENTLDWmsscrmALSLTRGLAYLHTdlrrgDQYKpAIAHRDLNSRNVLVKADGSCV-ICDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDI--------QTHMTNNK-----GSAAWMAPEVFEGS-------NYSEKCDVFSWGIILWEVITR------------- 225
Cdd:cd14054 149 AMVLrgsslvrgRPGAAENAsisevGTLRYMAPEVLEGAvnlrdceSALKQVDVYALGLVLWEIAMRcsdlypgesvppy 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 226 RKPFD-EIGG-PAFRIM--WAVHNGTRP------PLIKNLPKPIESLMTRCWSKDPSQR 274
Cdd:cd14054 229 QMPYEaELGNhPTFEDMqlLVSREKARPkfpdawKENSLAVRSLKETIEDCWDQDAEAR 287
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
40-276 2.64e-29

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 117.43  E-value: 2.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKqIESESERKAFIVELR--QLSRVNHPNIVKLYGA--CLNPVC----LVMEYAEGGS 111
Cdd:cd14053   1 EIKARGRFGAVWKAQYLNRLVAVK-IFPLQEKQSWLTEREiySLPGMKHENILQFIGAekHGESLEaeywLITEFHERGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGaeplpyytaaHAMSW------CLQCSQGVAYLHSMQP-------KALIHRDLKPPNLLLVAGGTVLkICDFGT 178
Cdd:cd14053  80 LCDYLKG----------NVISWnelckiAESMARGLAYLHEDIPatngghkPSIAHRDFKSKNVLLKSDLTAC-IADFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDIQ-------THmtNNKGSAAWMAPEVFEGS-NYSE----KCDVFSWGIILWEVITR-----------RKPFDEIGG- 234
Cdd:cd14053 149 ALKFEpgkscgdTH--GQVGTRRYMAPEVLEGAiNFTRdaflRIDMYAMGLVLWELLSRcsvhdgpvdeyQLPFEEEVGq 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 235 -PAFRIM--WAVHNGTRP---------PLIKNLPKPIESlmtrCWSKDPSQRPS 276
Cdd:cd14053 227 hPTLEDMqeCVVHKKLRPqirdewrkhPGLAQLCETIEE----CWDHDAEARLS 276
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
34-289 2.84e-29

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 117.43  E-value: 2.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEE--VVGRGAFGVVCKAKWrAKD-------VAIKQIESESERKA---FIVELRQLSRVNHPNIVKLYGACL-NPV 100
Cdd:cd05109   5 KETELKKvkVLGSGAFGTVYKGIW-IPDgenvkipVAIKVLRENTSPKAnkeILDEAYVMAGVGSPYVCRLLGICLtSTV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNvlHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTA- 179
Cdd:cd05109  84 QLVTQLMPYGCLLD--YVRENKDRIGSQDLLNWCVQIAKGMSYLEEVR---LVHRDLAARNVL-VKSPNHVKITDFGLAr 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 -CDI---QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRPPLIKN 254
Cdd:cd05109 158 lLDIdetEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGI--PAREIPDLLEKGERLPQPPI 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05109 236 CTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMAR 270
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
40-282 3.36e-29

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 116.71  E-value: 3.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQIE---SESER---------KAFIVELRQLSRVNHPNIVKLYG--ACLNPVCLV 103
Cdd:cd06629   7 ELIGKGTYGRVylAMNATTGEMLAVKQVElpkTSSDRadsrqktvvDALKSEIDTLKDLDHPNIVQYLGfeETEDYFSIF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGT---AC 180
Cdd:cd06629  87 LEYVPGGSIGSCLRKYGKFEEDLVRFFTR---QILDGLAYLHS---KGILHRDLKADNILVDLEGIC-KISDFGIskkSD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DI--QTHMTNNKGSAAWMAPEVFE--GSNYSEKCDVFSWGIILWEVITRRKPFDEIggPAFRIMWAVHNGTRPPLIK--- 253
Cdd:cd06629 160 DIygNNGATSMQGSVFWMAPEVIHsqGQGYSAKVDIWSLGCVVLEMLAGRRPWSDD--EAIAAMFKLGNKRSAPPVPedv 237
                       250       260
                ....*....|....*....|....*....
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06629 238 NLSPEALDFLNACFAIDPRDRPTAAELLS 266
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
37-282 3.48e-29

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 117.20  E-value: 3.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd07829   2 EKLEKLGEGTYGVVYKAKDKKTGeiVALKKIRLDNEEEGIpstaLREISLLKELKHPNIVKLLDVIHTEnkLYLVFEYCD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GgSLYNVLHG-AEPLPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDIQ---- 183
Cdd:cd07829  82 Q-DLKKYLDKrPGPLPPNLIKSIM---YQLLRGLAYCHSHR---ILHRDLKPQNLLINRDG-VLKLADFGLARAFGiplr 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 --TH--MTnnkgsaAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF---------DEIggpaFRIMwavhnGT- 247
Cdd:cd07829 154 tyTHevVT------LWYrAPEILLGSkHYSTAVDIWSVGCIFAELITGKPLFpgdseidqlFKI----FQIL-----GTp 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 248 --------------RPPLIKNLPKPIES-----------LMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd07829 219 teeswpgvtklpdyKPTFPKWPKNDLEKvlprldpegidLLSKMLQYNPAKRISAKEALK 278
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
37-282 3.90e-29

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 116.35  E-value: 3.90e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAK--WRAKDVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYG--ACLNPVCLVMEYA 107
Cdd:cd14663   3 ELGRTLGEGTFAKVKFARntKTGESVAIKIIDKEQVAREGMVeqikrEIAIMKLLRHPNIVELHEvmATKTKIFFVMELV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTacdiqTHMT 187
Cdd:cd14663  83 TGGELFSKIAKNGRLKEDKARKYFQ---QLIDAVDYCHS---RGVFHRDLKPENLLLDEDGN-LKISDFGL-----SALS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNK----------GSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDEiggPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd14663 151 EQFrqdgllhttcGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDD---ENLMALYRKIMKGEFEYPRWFS 227
                       250       260
                ....*....|....*....|....*.
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14663 228 PGAKSLIKRILDPNPSTRITVEQIMA 253
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
42-278 3.94e-29

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 116.17  E-value: 3.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAK-DVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN-PVCLVMEYAEGGSLYNVLHG 118
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTtKVAIKTLKPGTmSPEAFLEEAQIMKKLRHDKLVQLYAVVSEePIYIVTEFMSKGSLLDFLKD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 119 AE----PLPYYTAAHAmswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGSAA 194
Cdd:cd14203  83 GEgkylKLPQLVDMAA-----QIASGMAYIERMN---YIHRDLRAANIL-VGDNLVCKIADFGLARLIEDNEYTARQGAK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 195 ----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSK 269
Cdd:cd14203 154 fpikWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYP--GMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRK 231

                ....*....
gi 21735562 270 DPSQRPSME 278
Cdd:cd14203 232 DPEERPTFE 240
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
30-280 4.14e-29

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 117.38  E-value: 4.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVV--CKAKW--------------RAKDVAIKQIESESERKA---FIVELRQLSRVNHPNIV 90
Cdd:cd05097   1 EFPRQQLRLKEKLGEGQFGEVhlCEAEGlaeflgegapefdgQPVLVAVKMLRADVTKTArndFLKEIKIMSRLKNPNII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  91 KLYGACL--NPVCLVMEYAEGGSL---------YNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKP 159
Cdd:cd05097  81 RLLGVCVsdDPLCMITEYMENGDLnqflsqreiESTFTHANNIPSVSIANLLYMAVQIASGMKYLASLN---FVHRDLAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 160 PNLLLVAGGTVlKICDFGTACDIQT-HMTNNKGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT--RRKPFD-- 230
Cdd:cd05097 158 RNCLVGNHYTI-KIADFGMSRNLYSgDYYRIQGRAVlpirWMAWESILLGKFTTASDVWAFGVTLWEMFTlcKEQPYSll 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 231 ------EIGGPAFRIMWAVHNGTRPPLIknlPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05097 237 sdeqviENTGEFFRNQGRQIYLSQTPLC---PSPVFKLMMRCWSRDIKDRPTFNKI 289
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
60-280 4.32e-29

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 116.54  E-value: 4.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  60 VAIKQIESESER--KAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYNVLHGaEPLpyytaahAMSWCL 135
Cdd:cd14042  33 VAIKKVNKKRIDltREVLKELKHMRDLQHDNLTRFIGACVDPpnICILTEYCPKGSLQDILEN-EDI-------KLDWMF 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 136 QCS------QGVAYLHSMQPKAliHRDLKPPNLLlVAGGTVLKICDFG-----TACDIQTHMTNNKGSAAWMAPEVFEGS 204
Cdd:cd14042 105 RYSlihdivKGMHYLHDSEIKS--HGNLKSSNCV-VDSRFVLKITDFGlhsfrSGQEPPDDSHAYYAKLLWTAPELLRDP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 205 NY----SEKCDVFSWGIILWEVITRRKPFDEIG---GPAFRIMWAVHNGTRPPL-----IKNLPKPIESLMTRCWSKDPS 272
Cdd:cd14042 182 NPpppgTQKGDVYSFGIILQEIATRQGPFYEEGpdlSPKEIIKKKVRNGEKPPFrpsldELECPDEVLSLMQRCWAEDPE 261

                ....*...
gi 21735562 273 QRPSMEEI 280
Cdd:cd14042 262 ERPDFSTL 269
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
30-278 6.25e-29

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 115.75  E-value: 6.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRA-KDVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN-PVCLVMEY 106
Cdd:cd05067   3 EVPRETLKLVERLGAGQFGEVWMGYYNGhTKVAIKSLKQGSmSPDAFLAEANLMKQLQHQRLVRLYAVVTQePIYIITEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYyTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQ-TH 185
Cdd:cd05067  83 MENGSLVDFLKTPSGIKL-TINKLLDMAAQIAEGMAFI---EERNYIHRDLRAANIL-VSDTLSCKIADFGLARLIEdNE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSA---AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05067 158 YTAREGAKfpiKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHgRIPYPGMTNP--EVIQNLERGYRMPRPDNCPEELYQ 235
                       250
                ....*....|....*..
gi 21735562 262 LMTRCWSKDPSQRPSME 278
Cdd:cd05067 236 LMRLCWKERPEDRPTFE 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
42-279 6.44e-29

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 115.54  E-value: 6.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAK---DVAIKQIESESERKAFIV---ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLY 113
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKpdlPVAIKCITKKNLSKSQNLlgkEIKILKELSHENVVALLDCQETSssVYLVMEYCNGGDLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYYTAAHAMSwclqcsQGVAYLHSMQPKALIHRDLKPPNLLLVAGG--------TVLKICDFGTACDIQTH 185
Cdd:cd14120  81 DYLQAKGTLSEDTIRVFLQ------QIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndIRLKIADFGFARFLQDG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLM 263
Cdd:cd14120 155 MMAATlcGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIPSGTSPALKDLL 234
                       250
                ....*....|....*.
gi 21735562 264 TRCWSKDPSQRPSMEE 279
Cdd:cd14120 235 LGLLKRNPKDRIDFED 250
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
77-280 6.66e-29

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 115.43  E-value: 6.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  77 ELRQLSRVNHPNIVKLYGACLNP----VCLVMEYAeGGSLYNVLHGAePLPYYTAAHAMSWCLQCSQGVAYLHSmqpKAL 152
Cdd:cd14119  44 EIQILRRLNHRNVIKLVDVLYNEekqkLYMVMEYC-VGGLQEMLDSA-PDKRLPIWQAHGYFVQLIDGLEYLHS---QGI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 153 IHRDLKPPNLLLVAGGTvLKICDFGTACDIQ-----THMTNNKGSAAWMAPEVFEGSNYSE--KCDVFSWGIILWEVITR 225
Cdd:cd14119 119 IHKDIKPGNLLLTTDGT-LKISDFGVAEALDlfaedDTCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTG 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 226 RKPFDeiGGPAFRIMWAVHNG--TRPPlikNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14119 198 KYPFE--GDNIYKLFENIGKGeyTIPD---DVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
37-306 1.03e-28

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 116.13  E-value: 1.03e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAF-------IVELRQLSRVNHPNIVKL---YGACLNpVCLVM 104
Cdd:cd07841   3 EKGKKLGEGTYAVVYKARDKETGriVAIKKIKLGERKEAKdginftaLREIKLLQELKHPNIIGLldvFGHKSN-INLVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGgSLYNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDI-- 182
Cdd:cd07841  82 EFMET-DLEKVIKDKSIV--LTPADIKSYMLMTLRGLEYLHS---NWILHRDLKPNNLLIASDG-VLKLADFGLARSFgs 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 -QTHMTNNKGSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITrRKPF-------DEIGgpafRIMWAVhnGT----RP 249
Cdd:cd07841 155 pNRKMTHQVVTRWYRAPELLFGARhYGVGVDMWSVGCIFAELLL-RVPFlpgdsdiDQLG----KIFEAL--GTpteeNW 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 250 PLIKNLPKPIE---------------------SLMTRCWSKDPSQRPSMEEIVKimthlMRYFpgADEPlqYPCQYSD 306
Cdd:cd07841 228 PGVTSLPDYVEfkpfpptplkqifpaasddalDLLQRLLTLNPNKRITARQALE-----HPYF--SNDP--APTPPSQ 296
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
40-280 1.21e-28

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 115.14  E-value: 1.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAK----DVAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd05047   1 DVIGEGNFGQVLKARIKKDglrmDAAIKRMKeyaSKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRgyLYLAIEYAPH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPL---PYYTAAHAMSWCLQCSQGVAY-------LHSMQPKALIHRDLKPPNLLlVAGGTVLKICDFGTA 179
Cdd:cd05047  81 GNLLDFLRKSRVLetdPAFAIANSTASTLSSQQLLHFaadvargMDYLSQKQFIHRDLAARNIL-VGENYVAKIADFGLS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRIMWAVHNGTRPPLIKNLPK 257
Cdd:cd05047 160 RGQEVYVKKTMGRlpVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS-------LGGTPYCGMTCAELYEKLPQGYRLEK 232
                       250       260
                ....*....|....*....|....*....
gi 21735562 258 P------IESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05047 233 PlncddeVYDLMRQCWREKPYERPSFAQI 261
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
30-284 1.43e-28

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 115.14  E-value: 1.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWR-AKDVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVME 105
Cdd:cd05072   3 EIPRESIKLVKKLGAGQFGEVWMGYYNnSTKVAVKTLKPGTmSVQAFLEEANLMKTLQHDKLVRLYAVVTKeePIYIITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEP----LPyytaaHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLlVAGGTVLKICDFGTACD 181
Cdd:cd05072  83 YMAKGSLLDFLKSDEGgkvlLP-----KLIDFSAQIAEGMAYI---ERKNYIHRDLRAANVL-VSESLMCKIADFGLARV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQ-THMTNNKGSA---AWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDeiGGPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd05072 154 IEdNEYTAREGAKfpiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKiPYP--GMSNSDVMSALQRGYRMPRMENCP 231
                       250       260
                ....*....|....*....|....*...
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05072 232 DELYDIMKTCWKEKAEERPTFDYLQSVL 259
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
30-301 1.47e-28

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 115.17  E-value: 1.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN-PVCLVMEY 106
Cdd:cd05070   5 EIPRESLQLIKRLGNGQFGEVWMGTWNGNtKVAIKTLKPGTmSPESFLEEAQIMKKLKHDKLVQLYAVVSEePIYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAE----PLPYYTAAHAmswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDI 182
Cdd:cd05070  85 MSKGSLLDFLKDGEgralKLPNLVDMAA-----QVAAGMAYIERMN---YIHRDLRSANIL-VGNGLICKIADFGLARLI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPK 257
Cdd:cd05070 156 EDNEYTARQGAKfpikWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYP--GMNNREVLEQVERGYRMPCPQDCPI 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEeivKIMTHLMRYFPgADEPLQYP 301
Cdd:cd05070 234 SLHELMIHCWKKDPEERPTFE---YLQGFLEDYFT-ATEPQYQP 273
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
72-280 1.48e-28

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 114.90  E-value: 1.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  72 KAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYNVLHgAEPLPYYTAAHAMswcLQCSQGVAYLHSmqp 149
Cdd:cd14027  36 EALLEEGKMMNRLRHSRVVKLLGVILEEgkYSLVMEYMEKGNLMHVLK-KVSVPLSVKGRII---LEIIEGMAYLHG--- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 150 KALIHRDLKPPNLLlVAGGTVLKICDFGTAC----------------DIQTHMTNNKGSAAWMAPEVFEGSNY--SEKCD 211
Cdd:cd14027 109 KGVIHKDLKPENIL-VDNDFHIKIADLGLASfkmwskltkeehneqrEVDGTAKKNAGTLYYMAPEHLNDVNAkpTEKSD 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21735562 212 VFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPP---LIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14027 188 VYSFAIVLWAIFANKEPYENAINED-QIIMCIKSGNRPDvddITEYCPREIIDLMKLCWEANPEARPTFPGI 258
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
37-291 1.53e-28

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 115.49  E-value: 1.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAE 108
Cdd:cd07833   4 EVLGVVGEGAYGVVLKCRNKATGeiVAIKKFkeseDDEDVKKTALREVKVLRQLRHENIVNLKEAFRrkGRLYLVFEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 ggslYNVLHGAEPLPYYTAAHAMSWCL-QCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTA----CDIQ 183
Cdd:cd07833  84 ----RTLLELLEASPGGLPPDAVRSYIwQLLQAIAYCHSHN---IIHRDIKPENILVSESG-VLKLCDFGFAraltARPA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF------DEIggpaFRIMWAVhnGTRPP-----L 251
Cdd:cd07833 156 SPLTDYVATRWYRAPELLVGDtNYGKPVDVWAIGCIMAELLDGEPLFpgdsdiDQL----YLIQKCL--GPLPPshqelF 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 252 IKNL---------PKPIESL---------------MTRCWSKDPSQRPSMEEIVKimthlMRYF 291
Cdd:cd07833 230 SSNPrfagvafpePSQPESLerrypgkvsspaldfLKACLRMDPKERLTCDELLQ-----HPYF 288
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
39-285 1.53e-28

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 115.80  E-value: 1.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVV--CKA----------------KWRAKDVAIKQIESESERKA---FIVELRQLSRVNHPNIVKLYGACL 97
Cdd:cd05096  10 KEKLGEGQFGEVhlCEVvnpqdlptlqfpfnvrKGRPLLVAVKILRPDANKNArndFLKEVKILSRLKDPNIIRLLGVCV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 --NPVCLVMEYAEGGSLYNVLHG----------------AEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKP 159
Cdd:cd05096  90 deDPLCMITEYMENGDLNQFLSShhlddkeengndavppAHCLPAISYSSLLHVALQIASGMKYLSSLN---FVHRDLAT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 160 PNLLlVAGGTVLKICDFGtacdiqthMTNN---------KGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT-- 224
Cdd:cd05096 167 RNCL-VGENLTIKIADFG--------MSRNlyagdyyriQGRAVlpirWMAWECILMGKFTTASDVWAFGVTLWEILMlc 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 225 RRKPFDEI--------GGPAFRIMWAVHNGTRPPLIknlPKPIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd05096 238 KEQPYGELtdeqvienAGEFFRDQGRQVYLFRPPPC---PQGLYELMLQCWSRDCRERPSFSDIHAFLT 303
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
35-279 1.62e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 114.72  E-value: 1.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAK---DVAIKQIESESERKAFIV---ELRQLSRVNHPNIVKLYG--ACLNPVCLVMEY 106
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKEKhdlEVAVKCINKKNLAKSQTLlgkEIKILKELKHENIVALYDfqEIANSVYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGG--------TVLKICDFGT 178
Cdd:cd14202  83 CNGGDLADYLHTMRTLSEDTIRLFLQ---QIAGAMKMLHS---KGIIHRDLKPQNILLSYSGgrksnpnnIRIKIADFGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDIQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd14202 157 ARYLQNNMMAATlcGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETS 236
                       250       260
                ....*....|....*....|...
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14202 237 SHLRQLLLGLLQRNQKDRMDFDE 259
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
42-288 1.76e-28

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 115.83  E-value: 1.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKW---------RAKDVAIKQIESESERK--AFIVELRQLSRV--NHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05099  20 LGEGCFGQVVRAEAygidksrpdQTVTVAVKMLKDNATDKdlADLISEMELMKLigKHKNIINLLGVCTQegPLYVIVEY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEP-LPYYTA------------AHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKI 173
Cdd:cd05099 100 AAKGNLREFLRARRPpGPDYTFditkvpeeqlsfKDLVSCAYQVARGMEYLES---RRCIHRDLAARNVL-VTEDNVMKI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDIQ-----THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIggpaFRIMWA 242
Cdd:cd05099 176 ADFGLARGVHdidyyKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGspypgiPVEEL----FKLLRE 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 243 VHNGTRPPlikNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05099 252 GHRMDKPS---NCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
42-282 1.90e-28

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 114.46  E-value: 1.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQ--IESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYN- 114
Cdd:cd06648  15 IGEGSTGIVCIAtdKSTGRQVAVKKmdLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLvgDELWVVMEFLEGGALTDi 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHG--AEPlpyytaaHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK-- 190
Cdd:cd06648  95 VTHTrmNEE-------QIATVCRAVLKALSFLHS---QGVIHRDIKSDSILLTSDGRV-KLSDFGFCAQVSKEVPRRKsl 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 -GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP-FDEiggPAFRIMWAVHNgTRPPLIKNLPK---PIESLMTR 265
Cdd:cd06648 164 vGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPyFNE---PPLQAMKRIRD-NEPPKLKNLHKvspRLRSFLDR 239
                       250
                ....*....|....*..
gi 21735562 266 CWSKDPSQRPSMEEIVK 282
Cdd:cd06648 240 MLVRDPAQRATAAELLN 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
34-276 2.81e-28

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 114.44  E-value: 2.81e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLNP----VCLVM 104
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNtkTIFALKTITTDPNpdvQKQILRELEINKSCASPYIVKYYGAFLDEqdssIGIAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCS-QGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd06621  81 EYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVlKGLSYLHS---RKIIHRDIKPSNILLTRKGQV-KLCDFGVSGELV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIG----GPAFRIMWAVHngTRPPLIKNLP-- 256
Cdd:cd06621 157 NSLAGTfTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGepplGPIELLSYIVN--MPNPELKDEPen 234
                       250       260
                ....*....|....*....|....*
gi 21735562 257 -----KPIESLMTRCWSKDPSQRPS 276
Cdd:cd06621 235 gikwsESFKDFIEKCLEKDGTRRPG 259
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
37-286 3.17e-28

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 113.90  E-value: 3.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd08224   3 EIEKKIGKGQFSVVYRArcLLDGRLVALKKVQifemmDAKARQDCLKEIDLLQQLNHPNIIKYLASFIenNELNIVLELA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVL-HGAE---PLPYYTAahamsW--CLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTA-- 179
Cdd:cd08224  83 DAGDLSRLIkHFKKqkrLIPERTI-----WkyFVQLCSALEHMHS---KRIMHRDIKPANVFITANG-VVKLGDLGLGrf 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNL-PK 257
Cdd:cd08224 154 FSSKTTAAHSLvGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNLYSLCKKIEKCEYPPLPADLySQ 233
                       250       260
                ....*....|....*....|....*....
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEIVKIMTH 286
Cdd:cd08224 234 ELRDLVAACIQPDPEKRPDISYVLDVAKR 262
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
42-282 3.57e-28

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 114.72  E-value: 3.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKW---------RAKDVAIKQIESESERKAF---IVELRQLSRV-NHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05098  21 LGEGCFGQVVLAEAigldkdkpnRVTKVAVKMLKSDATEKDLsdlISEMEMMKMIgKHKNIINLLGACTQdgPLYVIVEY 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEP--LPY-YTAAHA----------MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKI 173
Cdd:cd05098 101 ASKGNLREYLQARRPpgMEYcYNPSHNpeeqlsskdlVSCAYQVARGMEYLAS---KKCIHRDLAARNVL-VTEDNVMKI 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDIQ-----THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIggpaFRIMWA 242
Cdd:cd05098 177 ADFGLARDIHhidyyKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGspypgvPVEEL----FKLLKE 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 243 VHNGTRPpliKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05098 253 GHRMDKP---SNCTNELYMMMRDCWHAVPSQRPTFKQLVE 289
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
29-226 4.68e-28

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 114.14  E-value: 4.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  29 EEIDYKeieVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAFivELRQLSRVNHPNIVKLYGA----------- 95
Cdd:cd14137   2 VEISYT---IEKVIGSGSFGVVYQAKLLEtgEVVAIKKVLQDKRYKNR--ELQIMRRLKHPNIVKLKYFfyssgekkdev 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  96 CLNpvcLVMEYAEgGSLYNVLHgaeplPYYTAAHAMSWCL------QCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGT 169
Cdd:cd14137  77 YLN---LVMEYMP-ETLYRVIR-----HYSKNKQTIPIIYvklysyQLFRGLAYLHSLG---ICHRDIKPQNLLVDPETG 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 170 VLKICDFGTACDIQTHMTNNK--GSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITRR 226
Cdd:cd14137 145 VLKLCDFGSAKRLVPGEPNVSyiCSRYYRAPELIFGAtDYTTAIDIWSAGCVLAELLLGQ 204
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
30-284 8.41e-28

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 112.81  E-value: 8.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKW-RAKDVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACL-NPVCLVMEY 106
Cdd:cd05073   7 EIPRESLKLEKKLGAGQFGEVWMATYnKHTKVAVKTMKPGSmSVEAFLAEANVMKTLQHDKLVKLHAVVTkEPIYIITEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAE----PLPyytaaHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLlVAGGTVLKICDFGTACDI 182
Cdd:cd05073  87 MAKGSLLDFLKSDEgskqPLP-----KLIDFSAQIAEGMAFI---EQRNYIHRDLRAANIL-VSASLVCKIADFGLARVI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKNLPK 257
Cdd:cd05073 158 EDNEYTAREGAKfpikWTAPEAINFGSFTIKSDVWSFGILLMEIVTYgRIPYPGMSNP--EVIRALERGYRMPRPENCPE 235
                       250       260
                ....*....|....*....|....*..
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05073 236 ELYNIMMRCWKNRPEERPTFEYIQSVL 262
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
30-288 8.54e-28

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 112.76  E-value: 8.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKD-----VAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGAC--LNP 99
Cdd:cd05063   1 EIHPSHITKQKVIGAGEFGEVFRGILKMPGrkevaVAIKTLKpgyTEKQRQDFLSEASIMGQFSHHNIIRLEGVVtkFKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVL--HGAEplpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFG 177
Cdd:cd05063  81 AMIITEYMENGALDKYLrdHDGE----FSSYQLVGMLRGIAAGMKYLSDMN---YVHRDLAARNIL-VNSNLECKVSDFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQ-----THMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPP 250
Cdd:cd05063 153 LSRVLEddpegTYTTSGgKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFgERPYWDMSNH--EVMKAINDGFRLP 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 251 LIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05063 231 APMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
37-279 1.03e-27

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 117.59  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   37 EVEEVVGRGAFGVVckakWRAKD------VAIKQIESESERKA-----FIVELRQLSRVNHPNIVKLY-----GAClnpV 100
Cdd:NF033483  10 EIGERIGRGGMAEV----YLAKDtrldrdVAVKVLRPDLARDPefvarFRREAQSAASLSHPNIVSVYdvgedGGI---P 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  101 CLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGtac 180
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMI---QILSALEHAHRNG---IVHRDIKPQNILITKDGRV-KVTDFG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  181 dI-----QTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRImwA---VHNGTRP 249
Cdd:NF033483 153 -IaralsSTTMTQTNsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFD--GDSPVSV--AykhVQEDPPP 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 21735562  250 P--LIKNLPKPIESLMTRCWSKDPSQRP-SMEE 279
Cdd:NF033483 228 PseLNPGIPQSLDAVVLKATAKDPDDRYqSAAE 260
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
33-288 1.16e-27

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 113.17  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVVCKA-------KWRAKDVAIKQIESESERKAFIVELRQLSRV-NHPNIVKLYGACLNP--VCL 102
Cdd:cd05089   1 WEDIKFEDVIGEGNFGQVIKAmikkdglKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRgyLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPL---PYYTAAHAMSWCLQCSQGVAY-------LHSMQPKALIHRDLKPPNLLlVAGGTVLK 172
Cdd:cd05089  81 AIEYAPYGNLLDFLRKSRVLetdPAFAKEHGTASTLTSQQLLQFasdvakgMQYLSEKQFIHRDLAARNVL-VGENLVSK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 173 ICDFGTACDIQTHMTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRIMWAVH------ 244
Cdd:cd05089 160 IADFGLSRGEEVYVKKTMGRlpVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS-------LGGTPYCGMTCAElyeklp 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 245 NGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05089 233 QGYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRML 276
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
45-282 1.21e-27

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 113.09  E-value: 1.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  45 GAFGVVckakWRAKD------VAIKQIESESERKAF-IVELRQ---LSRVNHPNIVKL----YGACLNPVCLVMEYAEGg 110
Cdd:cd07843  16 GTYGVV----YRARDkktgeiVALKKLKMEKEKEGFpITSLREiniLLKLQHPNIVTVkevvVGSNLDKIYMVMEYVEH- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVL-HGAEPlpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQ---THM 186
Cdd:cd07843  91 DLKSLMeTMKQP---FLQSEVKCLMLQLLSGVAHLHD---NWILHRDLKTSNLLLNNRG-ILKICDFGLAREYGsplKPY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKGSAAWMAPEVFEG-SNYSEKCDVFSWGIILWEVITRR-------------KPFDEIGGPAFRImWavhngtrpPLI 252
Cdd:cd07843 164 TQLVVTLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKKplfpgkseidqlnKIFKLLGTPTEKI-W--------PGF 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 253 KNLP-----KPIE--------------------SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd07843 235 SELPgakkkTFTKypynqlrkkfpalslsdngfDLLNRLLTYDPAKRISAEDALK 289
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
37-279 1.24e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 113.77  E-value: 1.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLY-------GACLNPVCLV 103
Cdd:cd07834   3 ELLKPIGSGAYGVVCSAydKRTGRKVAIKKIsnvfDDLIDAKRILREIKILRHLKHENIIGLLdilrppsPEEFNDVYIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEgGSLYNVLHGAEPLpyyTAAHaMSWCL-QCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKICDFGTACDI 182
Cdd:cd07834  83 TELME-TDLHKVIKSPQPL---TDDH-IQYFLyQILRGLKYLHSAG---VIHRDLKPSNILVNSNCD-LKICDFGLARGV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHmtnnkGSAAWM----------APEV-FEGSNYSEKCDVFSWGIILWEVITRRkpfdeiggPAFRIMWAVHN------ 245
Cdd:cd07834 154 DPD-----EDKGFLteyvvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRK--------PLFPGRDYIDQlnlive 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 246 --GTRPP-------------LIKNLP----KPIES-----------LMTRCWSKDPSQRPSMEE 279
Cdd:cd07834 221 vlGTPSEedlkfissekarnYLKSLPkkpkKPLSEvfpgaspeaidLLEKMLVFNPKKRITADE 284
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
40-282 1.35e-27

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 112.47  E-value: 1.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA-KWRA-KDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL--VMEYAEGGSL 112
Cdd:cd06641  10 EKIGKGSFGEVFKGiDNRTqKVVAIKIIdleEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLwiIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLhgaEPLPYyTAAHAMSWCLQCSQGVAYLHSMQPkalIHRDLKPPNLLLVAGGTVlKICDFGTA---CDIQTHMTNN 189
Cdd:cd06641  90 LDLL---EPGPL-DETQIATILREILKGLDYLHSEKK---IHRDIKAANVLLSEHGEV-KLADFGVAgqlTDTQIKRN*F 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSK 269
Cdd:cd06641 162 VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELH--PMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNK 239
                       250
                ....*....|...
gi 21735562 270 DPSQRPSMEEIVK 282
Cdd:cd06641 240 EPSFRPTAKELLK 252
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
28-281 1.56e-27

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 112.78  E-value: 1.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  28 FEEIDYKEIEVEEVVGRGAFGVVCKAKWRAK----DVAIKQIE---SESERKAFIVELRQLSRVN-HPNIVKLYGACLNP 99
Cdd:cd05088   1 YPVLEWNDIKFQDVIGEGNFGQVLKARIKKDglrmDAAIKRMKeyaSKDDHRDFAGELEVLCKLGhHPNIINLLGACEHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 --VCLVMEYAEGGSLYNVLHGAEPL---PYYTAAHAMSWCLQCSQGVAY-------LHSMQPKALIHRDLKPPNLLlVAG 167
Cdd:cd05088  81 gyLYLAIEYAPHGNLLDFLRKSRVLetdPAFAIANSTASTLSSQQLLHFaadvargMDYLSQKQFIHRDLAARNIL-VGE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 168 GTVLKICDFGTACDIQTHMTNNKGS--AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRIMWAVHN 245
Cdd:cd05088 160 NYVAKIADFGLSRGQEVYVKKTMGRlpVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS-------LGGTPYCGMTCAEL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 246 GTRPPLIKNLPKPIE------SLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05088 233 YEKLPQGYRLEKPLNcddevyDLMRQCWREKPYERPSFAQIL 274
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
32-286 1.61e-27

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 112.31  E-value: 1.61e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKeieVEEVVGRGAFGVVCKAKWRA--KDVAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL-- 102
Cdd:cd05581   2 DFK---FGKPLGEGSYSTVVLAKEKEtgKEYAIKvldkrHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLyf 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLP-----YYTAahamswclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG 177
Cdd:cd05581  79 VLEYAPNGDLLEYIRKYGSLDekctrFYTA--------EIVLALEYLHS---KGIIHRDLKPENILLDEDMH-IKITDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQT----------------HMTNNK----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAF 237
Cdd:cd05581 147 TAKVLGPdsspestkgdadsqiaYNQARAasfvGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR--GSNEY 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 238 RIMWAVHNGT------RPPLIKNLpkpIESLMTRcwskDPSQRPSMEEI---VKIMTH 286
Cdd:cd05581 225 LTFQKIVKLEyefpenFPPDAKDL---IQKLLVL----DPSKRLGVNENggyDELKAH 275
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
40-284 1.63e-27

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 112.30  E-value: 1.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD------VAIKQIESE---SERKAFIVELRQLSRVNHPNIVKLYGACLNP----VCLVMEY 106
Cdd:cd05080  10 RDLGEGHFGKVSLYCYDPTNdgtgemVAVKALKADcgpQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggksLQLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLhgaePLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTACDIQT-H 185
Cdd:cd05080  90 VPLGSLRDYL----PKHSIGLAQLLLFAQQICEGMAYLHS---QHYIHRDLAARNVLL-DNDRLVKIGDFGLAKAVPEgH 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 M-----TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-------RKPFDEIGGPA------FRIMWAVHNGT 247
Cdd:cd05080 162 EyyrvrEDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHcdssqspPTKFLEMIGIAqgqmtvVRLIELLERGE 241
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 248 RPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05080 242 RLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPIL 278
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
30-301 2.41e-27

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 111.70  E-value: 2.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQIESESER-KAFIVELRQLSRVNHPNIVKLYGACLN-PVCLVMEY 106
Cdd:cd05069   8 EIPRESLRLDVKLGQGCFGEVWMGTWNGTtKVAIKTLKPGTMMpEAFLQEAQIMKKLRHDKLVPLYAVVSEePIYIVTEF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQ-TH 185
Cdd:cd05069  88 MGKGSLLDFLKEGDG-KYLKLPQLVDMAAQIADGMAYIERMN---YIHRDLRAANIL-VGDNLVCKIADFGLARLIEdNE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSA---AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05069 163 YTARQGAKfpiKWTAPEAALYGRFTIKSDVWSFGILLTELVTKgRVPYP--GMVNREVLEQVERGYRMPCPQGCPESLHE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 262 LMTRCWSKDPSQRPSMEeivKIMTHLMRYFPgADEPLQYP 301
Cdd:cd05069 241 LMKLCWKKDPDERPTFE---YIQSFLEDYFT-ATEPQYQP 276
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
33-291 2.68e-27

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 111.47  E-value: 2.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVeevVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQ---LSRVN-HPNIVKLYGACL--NPVCLVM 104
Cdd:cd07830   1 YKVIKQ---LGDGTFGSVYLARNKETGelVAIKKMKKKFYSWEECMNLREvksLRKLNeHPNIVKLKEVFRenDELYFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGgSLYNVL--HGAEPLPYYTAAhamSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDI 182
Cdd:cd07830  78 EYMEG-NLYQLMkdRKGKPFSESVIR---SIIYQILQGLAHIHK---HGFFHRDLKPEN-LLVSGPEVVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QthmtnNKG------SAAWM-APEVF-EGSNYSEKCDVFSWGIILWEVITRRKPF------DEI-------GGP------ 235
Cdd:cd07830 150 R-----SRPpytdyvSTRWYrAPEILlRSTSYSSPVDIWALGCIMAELYTLRPLFpgsseiDQLykicsvlGTPtkqdwp 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 236 -----AFRIMWAVHNGTRPPLIKNLPKPIES---LMTRCWSKDPSQRPSMEEIVKimthlMRYF 291
Cdd:cd07830 225 egyklASKLGFRFPQFAPTSLHQLIPNASPEaidLIKDMLRWDPKKRPTASQALQ-----HPYF 283
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
30-280 2.68e-27

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 111.35  E-value: 2.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVckakWRAKD------VAIKQIESESERKA--FIVELRQLSRVNHPNIVKLYGACL-NPV 100
Cdd:cd06624   4 EYEYDESGERVVLGKGTFGVV----YAARDlstqvrIAIKEIPERDSREVqpLHEEIALHSRLSHKNIVQYLGSVSeDGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLV-MEYAEGGSLYNVLHGA-EPLP-------YYTAahamswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVL 171
Cdd:cd06624  80 FKIfMEQVPGGSLSALLRSKwGPLKdnentigYYTK--------QILEGLKYLHDNK---IVHRDIKGDNVLVNTYSGVV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 172 KICDFGTA---CDIQTHMTNNKGSAAWMAPEVFEGS--NYSEKCDVFSWGIILWEVITRRKPFDEIGGPA---FRI-MWA 242
Cdd:cd06624 149 KISDFGTSkrlAGINPCTETFTGTLQYMAPEVIDKGqrGYGPPADIWSLGCTIIEMATGKPPFIELGEPQaamFKVgMFK 228
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 243 VHngtrPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd06624 229 IH----PEIPESLSEEAKSFILRCFEPDPDKRATASDL 262
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
30-284 2.89e-27

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 111.40  E-value: 2.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWR-------AKDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL-- 97
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYnlepeqdKMLVAVKTLKdasSPDARKDFEREAELLTNLQHENIVKFYGVCTeg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVCLVMEYAEGGSLYNVL--HG--AEPLPYYTAAHA-------MSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVA 166
Cdd:cd05049  81 DPLLMVFEYMEHGDLNKFLrsHGpdAAFLASEDSAPGeltlsqlLHIAVQIASGMVYLASQH---FVHRDLATRNCL-VG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 167 GGTVLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIM 240
Cdd:cd05049 157 TNLVVKIGDFGMSRDIYSTDYYRVGGHTmlpirWMPPESILYRKFTTESDVWSFGVVLWEIFTYgKQPWFQLSNT--EVI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 241 WAVHNGT--RPPliKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05049 235 ECITQGRllQRP--RTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
36-280 3.50e-27

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 110.85  E-value: 3.50e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKAKWR--AKDVAIKQIeseSERKA---FIV-----ELRQLSRVNHPNIVKLYGA--CLNPVCLV 103
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTkhKCKVAIKIV---SKKKApedYLQkflprEIEVIKGLKHPNLICFYEAieTTSRVYII 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVL--HGAEPLPyytaaHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTACD 181
Cdd:cd14162  79 MELAENGDLLDYIrkNGALPEP-----QARRWFRQLVAGVEYCHS---KGVVHRDLKCENLLLDKNNN-LKITDFGFARG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 iQTHMTNNK--------GSAAWMAPEVFEGSNYSEK-CDVFSWGIILWEVITRRKPFDEIGGPAfrIMWAVHNGTRPPLI 252
Cdd:cd14162 150 -VMKTKDGKpklsetycGSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRLPFDDSNLKV--LLKQVQRRVVFPKN 226
                       250       260
                ....*....|....*....|....*...
gi 21735562 253 KNLPKPIESLMTRCWSKDPsQRPSMEEI 280
Cdd:cd14162 227 PTVSEECKDLILRMLSPVK-KRITIEEI 253
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
40-282 3.89e-27

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 110.92  E-value: 3.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA-KWRAKDV-AIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd06642  10 ERIGKGSFGEVYKGiDNRTKEVvAIKIIdleEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLkgTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLhgaEPLPYyTAAHAMSWCLQCSQGVAYLHSMQPkalIHRDLKPPNLLLVAGGTVlKICDFGTA---CDIQTHMTNN 189
Cdd:cd06642  90 LDLL---KPGPL-EETYIATILREILKGLDYLHSERK---IHRDIKAANVLLSEQGDV-KLADFGVAgqlTDTQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSK 269
Cdd:cd06642 162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLH--PMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNK 239
                       250
                ....*....|...
gi 21735562 270 DPSQRPSMEEIVK 282
Cdd:cd06642 240 DPRFRPTAKELLK 252
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
36-282 3.95e-27

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 110.90  E-value: 3.95e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKAKwRAKD---VAIK---------QIESESERKAFIVELRQLSRV-NHPNIVKLYGACLNPVC- 101
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAV-DLRTgrkYAIKclyksgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAi 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 -LVMEYAEGGSLYNVLHgaEPLPYYTAAHAM-SWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFGTA 179
Cdd:cd13993  81 yIVLEYCPNGDLFEAIT--ENRIYVGKTELIkNVFLQLIDAVKHCHS---LGIYHRDIKPENILLSQDEGTVKLCDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGSAAWMAPEVF-----EGSNYS-EKCDVFSWGIILWEVITRRKPFdEIGGPAfRIMWAVHNGTRPPLIK 253
Cdd:cd13993 156 TTEKISMDFGVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPW-KIASES-DPIFYDYYLNSPNLFD 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 254 NLPkPIE----SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd13993 234 VIL-PMSddfyNLLRQIFTVNPNNRILLPELQL 265
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
30-287 4.52e-27

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 112.40  E-value: 4.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKW-------RAKDVAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACLN 98
Cdd:cd14207   3 EFARERLKLGKSLGRGAFGKVVQASAfgikkspTCRVVAVKMLKegaTASEYKALMTELKILIHIgHHLNVVNLLGACTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 ---PVCLVMEYAEGGSLYNVLH-----------------------GAEPLP----------------------------- 123
Cdd:cd14207  83 sggPLMVIVEYCKYGNLSNYLKskrdffvtnkdtslqeelikekkEAEPTGgkkkrlesvtssesfassgfqedkslsdv 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 124 ---------YY----TAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTACDIQTHMTN-N 189
Cdd:cd14207 163 eeeeedsgdFYkrplTMEDLISYSFQVARGMEFLSS---RKCIHRDLAARNILL-SENNVVKICDFGLARDIYKNPDYvR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGG---PAFRI----MWAVHNGTRPPLIKNLPKP 258
Cdd:cd14207 239 KGDArlplKWMAPESIFDKIYSTKSDVWSYGVLLWEIFS-------LGAspyPGVQIdedfCSKLKEGIRMRAPEFATSE 311
                       330       340
                ....*....|....*....|....*....
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14207 312 IYQIMLDCWQGDPNERPRFSELVERLGDL 340
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
43-282 4.67e-27

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 110.04  E-value: 4.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWR--AKDVAIKQIESES----------ERKAFIVELrqlsrVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14081  10 GKGQTGLVKLAKHCvtGQKVAIKIVNKEKlskesvlmkvEREIAIMKL-----IEHPNVLKLYDVYENKkyLYLVLEYVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT-HMT 187
Cdd:cd14081  85 GGELFDYLVKKGRLTEKEARKFFR---QIISALDYCHSHS---ICHRDLKPENLLLDEKNNI-KIADFGMASLQPEgSLL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNK-GSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDeigGPAFR-IMWAVHNGTrPPLIKNLPKPIESLMT 264
Cdd:cd14081 158 ETScGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFD---DDNLRqLLEKVKRGV-FHIPHFISPDAQDLLR 233
                       250
                ....*....|....*...
gi 21735562 265 RCWSKDPSQRPSMEEIVK 282
Cdd:cd14081 234 RMLEVNPEKRITIEEIKK 251
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
35-285 4.90e-27

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 110.50  E-value: 4.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRA--KDVAIK-QIESESER-KAFIVELRQLSRV-NHPNIVKLYGACLNP------VCLV 103
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNtgRRYALKrMYFNDEEQlRVAIKEIEIMKRLcGHPNIVQYYDSAILSsegrkeVLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAeGGSLYNVLHGAEPLPYyTAAHAMSWCLQCSQGVAYLHSMQPKaLIHRDLKPPNLLLVAGGTvLKICDFGTAC--- 180
Cdd:cd13985  81 MEYC-PGSLVDILEKSPPSPL-SEEEVLRIFYQICQAVGHLHSQSPP-IIHRDIKIENILFSNTGR-FKLCDFGSATteh 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 --------------DIQTHMTnnkgsAAWMAPE---VFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiggpaFRIMWAV 243
Cdd:cd13985 157 ypleraeevniieeEIQKNTT-----PMYRAPEmidLYSKKPIGEKADIWALGCLLYKLCFFKLPFDE-----SSKLAIV 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 244 hNGTRP-PLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd13985 227 -AGKYSiPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
42-282 5.31e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 110.29  E-value: 5.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFG--VVCKAKWRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL--VMEYAEGGSLY 113
Cdd:cd08218   8 IGEGSFGkaLLVKSKEDGKQYVIKEINiskmSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLyiVMDYCDGGDLY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK--- 190
Cdd:cd08218  88 KRINAQRGVLF-PEDQILDWFVQLCLALKHVHD---RKILHRDIKSQNIFLTKDGII-KLGDFGIARVLNSTVELARtci 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKD 270
Cdd:cd08218 163 GTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFE--AGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240
                       250
                ....*....|..
gi 21735562 271 PSQRPSMEEIVK 282
Cdd:cd08218 241 PRDRPSINSILE 252
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
40-279 5.69e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 110.07  E-value: 5.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA--KWRAKD-VAIKQIESESERKA----FIVELRQLSRVNHPNIVKL----------YgaclnpvcL 102
Cdd:cd14121   1 EKLGSGTYATVYKAyrKSGAREvVAVKCVSKSSLNKAstenLLTEIELLKKLKHPHIVELkdfqwdeehiY--------L 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGT-VLKICDFGTAcd 181
Cdd:cd14121  73 IMEYCSGGDLSRFIRSRRTLPESTVRRFLQ---QLASALQFLRE---HNISHMDLKPQNLLLSSRYNpVLKLADFGFA-- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 iqTHMTNN------KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeiggpAFRIMWAVHNGTRPPLIKNL 255
Cdd:cd14121 145 --QHLKPNdeahslRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPF------ASRSFEELEEKIRSSKPIEI 216
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 256 PKPIES------LMTRCWSKDPSQRPSMEE 279
Cdd:cd14121 217 PTRPELsadcrdLLLRLLQRDPDRRISFEE 246
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
40-282 7.44e-27

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 110.14  E-value: 7.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA--KWRAKDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd06640  10 ERIGKGSFGEVFKGidNRTQQVVAIKIIdleEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLkgTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHgAEPLPYYTAAHAMSWCLQcsqGVAYLHSMQPkalIHRDLKPPNLLLVAGGTVlKICDFGTA---CDIQTHMTNN 189
Cdd:cd06640  90 LDLLR-AGPFDEFQIATMLKEILK---GLDYLHSEKK---IHRDIKAANVLLSEQGDV-KLADFGVAgqlTDTQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSK 269
Cdd:cd06640 162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMH--PMRVLFLIPKNNPPTLVGDFSKPFKEFIDACLNK 239
                       250
                ....*....|...
gi 21735562 270 DPSQRPSMEEIVK 282
Cdd:cd06640 240 DPSFRPTAKELLK 252
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
30-317 9.46e-27

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 111.27  E-value: 9.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKW---------RAKDVAIKQIESESERKAF---IVELRQLSRV-NHPNIVKLYGAC 96
Cdd:cd05100   8 ELSRTRLTLGKPLGEGCFGQVVMAEAigidkdkpnKPVTVAVKMLKDDATDKDLsdlVSEMEMMKMIgKHKNIINLLGAC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 LN--PVCLVMEYAEGGSLYNVLHGAEP-----------LP--YYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPN 161
Cdd:cd05100  88 TQdgPLYVLVEYASKGNLREYLRARRPpgmdysfdtckLPeeQLTFKDLVSCAYQVARGMEYLAS---QKCIHRDLAARN 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 162 LLlVAGGTVLKICDFGTACDIQT-----HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFD 230
Cdd:cd05100 165 VL-VTEDNVMKIADFGLARDVHNidyykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGspypgiPVE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 231 EIggpaFRIMWAVHNGTRPpliKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRyFPGADEPLQYPC---QYSDE 307
Cdd:cd05100 244 EL----FKLLKEGHRMDKP---ANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLT-VTSTDEYLDLSVpfeQYSPG 315
                       330
                ....*....|.
gi 21735562 308 GQ-SNSATSTG 317
Cdd:cd05100 316 CPdSPSSCSSG 326
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
34-229 1.43e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 110.15  E-value: 1.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVckakWRAKD------VAIKQIESESERKAFIV----ELRQLSRVNHPNIVKLY----GACLNP 99
Cdd:cd07845   7 TEFEKLNRIGEGTYGIV----YRARDttsgeiVALKKVRMDNERDGIPIsslrEITLLLNLRHPNIVELKevvvGKHLDS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAE---GGSLYNVlhgaePLPYyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDF 176
Cdd:cd07845  83 IFLVMEYCEqdlASLLDNM-----PTPF-SESQVKCLMLQLLRGLQYLHE---NFIIHRDLKVSNLLLTDKG-CLKIADF 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 177 GTA---CDIQTHMTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITrRKPF 229
Cdd:cd07845 153 GLArtyGLPAKPMTPKVVTLWYRAPELLLGCtTYTTAIDMWAVGCILAELLA-HKPL 208
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
37-284 1.46e-26

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 109.27  E-value: 1.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEevVGRGAFGVVCKAKWRAK----DVAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGAC-LNPVCLVMEYAE 108
Cdd:cd05115   9 EVE--LGSGNFGCVKKGVYKMRkkqiDVAIKVLKQGNEkavRDEMMREAQIMHQLDNPYIVRMIGVCeAEALMLVMEMAS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGA-EPLPYYTAAHAMSwclQCSQGVAYLhsmQPKALIHRDLKPPNLLLVaGGTVLKICDFGTACDI----- 182
Cdd:cd05115  87 GGPLNKFLSGKkDEITVSNVVELMH---QVSMGMKYL---EEKNFVHRDLAARNVLLV-NQHYAKISDFGLSKALgadds 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 -QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIE 260
Cdd:cd05115 160 yYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYgQKPYKKMKGP--EVMSFIEQGKRMDCPAECPPEMY 237
                       250       260
                ....*....|....*....|....
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05115 238 ALMSDCWIYKWEDRPNFLTVEQRM 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
40-282 1.57e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 108.92  E-value: 1.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIEsESERKAFIVELRQLSRVNHPNIVKLYgACL---NPVCLVMEYAEGGSLYN 114
Cdd:cd14010   6 DEIGRGKHSVVYKGRRKGtiEFVAIKCVD-KSKRPEVLNEVRLTHELKHPNVLKFY-EWYetsNHLWLVVEYCTGGDLET 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEPLPYYTAahaMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTA--------------C 180
Cdd:cd14010  84 LLRQDGNLPESSV---RKFGRDLVRGLHYIHS---KGIIYCDLKPSNILLDGNGT-LKLSDFGLArregeilkelfgqfS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNK-----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIMWAVHNGTRPPLIK 253
Cdd:cd14010 157 DEGNVNKVSKkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFvaESFTELVEKILNEDPPPPPPKVSS 236
                       250       260
                ....*....|....*....|....*....
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14010 237 KPSPDFKSLLKGLLEKDPAKRLSWDELVK 265
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
40-287 1.82e-26

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 109.45  E-value: 1.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKqIESESERKAFIVELRQLSRVN--HPNIVKLYGA------CLNPVCLVMEYAEGGS 111
Cdd:cd13998   1 EVIGKGRFGEVWKASLKNEPVAVK-IFSSRDKQSWFREKEIYRTPMlkHENILQFIAAderdtaLRTELWLVTAFHPNGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGaeplpyytaaHAMSWCLQC------SQGVAYLHS-----MQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTA 179
Cdd:cd13998  80 L*DYLSL----------HTIDWVSLCrlalsvARGLAHLHSeipgcTQGKpAIAHRDLKSKNILVKNDGTCC-IADFGLA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 C---------DIQTHmtNNKGSAAWMAPEVFEGS-NYS-----EKCDVFSWGIILWEVITRRK-----------PF-DEI 232
Cdd:cd13998 149 VrlspstgeeDNANN--GQVGTKRYMAPEVLEGAiNLRdfesfKRVDIYAMGLVLWEMASRCTdlfgiveeykpPFySEV 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 233 GG-PAFRIMWAV--HNGTRPplikNLP---------KPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd13998 227 PNhPSFEDMQEVvvRDKQRP----NIPnrwlshpglQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
44-286 2.32e-26

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 108.84  E-value: 2.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  44 RGAFGVV--CKAKWRAKDVAIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd05579   3 RGAYGRVylAKKKSTGDLYAIKVI-----KKRDMIRKNQvdsvlaerniLSQAQNPFVVKLYYSfqGKKNLYLVMEYLPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTvLKICDFGTACDIQTHMTNN 189
Cdd:cd05579  78 GDLYSLLENVGALDEDVARIYIA---EIVLALEYLHSH---GIIHRDLKPDNILIDANGH-LKLTDFGLSKVGLVRRQIK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAA------------------WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-----DEIggpaF------RIM 240
Cdd:cd05579 151 LSIQKksngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFhaetpEEI----FqnilngKIE 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 241 WavhngtrpPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTH 286
Cdd:cd05579 227 W--------PEDPEVSDEAKDLISKLLTPDPEKRLGAKGIEEIKNH 264
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
34-281 2.50e-26

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 108.02  E-value: 2.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAK--WRAKDVAIKQIESESERKA-----FIVELRQLSRVNHPNIVKLYGaCL---NPVCLV 103
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTdmSTGKVYAGKVVPKSSLTKPkqrekLKSEIKIHRSLKHPNIVKFHD-CFedeENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLPYYTAAHamsWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd14099  80 LELCSNGSLMELLKRRKALTEPEVRY---FMRQILSGVKYLHS---NRIIHRDLKLGNLFLDENMNV-KIGDFGLAARLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNNK---GSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITRRKPFD-----EIggpAFRImwaVHNGTRPPLIKN 254
Cdd:cd14099 153 YDGERKKtlcGTPNYIAPEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPFEtsdvkET---YKRI---KKNEYSFPSHLS 226
                       250       260
                ....*....|....*....|....*..
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14099 227 ISDEAKDLIRSMLQPDPTKRPSLDEIL 253
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
41-282 2.52e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 108.29  E-value: 2.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKwRAKD---VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLV--MEYAEGGS 111
Cdd:cd08221   7 VLGRGAFGEAVLYR-KTEDnslVVWKEVNlsrlSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFieMEYCNGGN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYN--VLHGAEPLPYYTAAhamsWCL-QCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTA--CDIQTHM 186
Cdd:cd08221  86 LHDkiAQQKNQLFPEEVVL----WYLyQIVSAVSHIHKA---GILHRDIKTLNIFLTKADLV-KLGDFGISkvLDSESSM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKNLPKPIESLMTR 265
Cdd:cd08221 158 AESiVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATN--PLRLAVKIVQGEYEDIDEQYSEEIIQLVHD 235
                       250
                ....*....|....*..
gi 21735562 266 CWSKDPSQRPSMEEIVK 282
Cdd:cd08221 236 CLHQDPEDRPTAEELLE 252
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
30-280 2.66e-26

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 108.28  E-value: 2.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWR--AKDVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVM 104
Cdd:cd05052   2 EIERTDITMKHKLGGGQYGEVYEGVWKkyNLTVAVKTLKEDTmEVEEFLKEAAVMKEIKHPNLVQLLGVCTRepPFYIIT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTA----C 180
Cdd:cd05052  82 EFMPYGNLLDYLRECNR-EELNAVVLLYMATQIASAMEYLEK---KNFIHRDLAARNCL-VGENHLVKVADFGLSrlmtG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeiggPAFRIMWAVH---NGTRPPLIKNLP 256
Cdd:cd05052 157 DTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYgMSPY-----PGIDLSQVYElleKGYRMERPEGCP 231
                       250       260
                ....*....|....*....|....
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05052 232 PKVYELMRACWQWNPSDRPSFAEI 255
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
30-289 2.76e-26

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 110.07  E-value: 2.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKA-------KWRAKDVAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACLN 98
Cdd:cd05102   3 EFPRDRLRLGKVLGHGAFGKVVEAsafgidkSSSCETVAVKMLKegaTASEHKALMSELKILIHIgNHLNVVNLLGACTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 ---PVCLVMEYAEGGSLYNVLHGAEP--LPY------------------------------------------------- 124
Cdd:cd05102  83 pngPLMVIVEFCKYGNLSNFLRAKREgfSPYrersprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprqevd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 125 ------YTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTACDIQTHMTN-NKGSA---- 193
Cdd:cd05102 163 dlwqspLTMEDLICYSFQVARGMEFLAS---RKCIHRDLAARNILL-SENNVVKICDFGLARDIYKDPDYvRKGSArlpl 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 194 AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeiggPAFRI----MWAVHNGTRPPLIKNLPKPIESLMTRCWS 268
Cdd:cd05102 239 KWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLgASPY-----PGVQIneefCQRLKDGTRMRAPEYATPEIYRIMLSCWH 313
                       330       340
                ....*....|....*....|.
gi 21735562 269 KDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05102 314 GDPKERPTFSDLVEILGDLLQ 334
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
40-282 3.01e-26

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 108.19  E-value: 3.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQI-------ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP----VCLVMEY 106
Cdd:cd06653   8 KLLGRGAFGEVylCYDADTGRELAVKQVpfdpdsqETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPeekkLSIFVEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT-- 184
Cdd:cd06653  88 MPGGSVKDQLKAYGAL---TENVTRRYTRQILQGVSYLHS---NMIVHRDIKGANILRDSAGNV-KLGDFGASKRIQTic 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 ----HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPA--FRImwaVHNGTRPPLIKNLPKP 258
Cdd:cd06653 161 msgtGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAaiFKI---ATQPTKPQLPDGVSDA 237
                       250       260
                ....*....|....*....|....
gi 21735562 259 IESLMTRCWSKDpSQRPSMEEIVK 282
Cdd:cd06653 238 CRDFLRQIFVEE-KRRPTAEFLLR 260
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
35-278 3.15e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 108.17  E-value: 3.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAK---DVAIKQIESESERKAFIV---ELRQLSRVNHPNIVKLYGA--CLNPVCLVMEY 106
Cdd:cd14201   7 EYSRKDLVGHGAFAVVFKGRHRKKtdwEVAIKSINKKNLSKSQILlgkEIKILKELQHENIVALYDVqeMPNSVFLVMEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLL--------VAGGTVLKICDFGT 178
Cdd:cd14201  87 CNGGDLADYLQAKGTLSEDTIRVFLQ---QIAAAMRILHS---KGIIHRDLKPQNILLsyasrkksSVSGIRIKIADFGF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDIQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd14201 161 ARYLQSNMMAATlcGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETS 240
                       250       260
                ....*....|....*....|..
gi 21735562 257 KPIESLMTRCWSKDPSQRPSME 278
Cdd:cd14201 241 PYLADLLLGLLQRNQKDRMDFE 262
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
40-282 3.18e-26

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 108.21  E-value: 3.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQI-------ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP----VCLVMEY 106
Cdd:cd06652   8 KLLGQGAFGRVylCYDADTGRELAVKQVqfdpespETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPqertLSIFMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG------TAC 180
Cdd:cd06652  88 MPGGSIKDQLKSYGAL---TENVTRKYTRQILEGVHYLHS---NMIVHRDIKGANILRDSVGNV-KLGDFGaskrlqTIC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiggpaFRIMWAVHNGTRPPLIKNLPkPIE 260
Cdd:cd06652 161 LSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAE-----FEAMAAIFKIATQPTNPQLP-AHV 234
                       250       260
                ....*....|....*....|....*.
gi 21735562 261 SLMTRCWSK----DPSQRPSMEEIVK 282
Cdd:cd06652 235 SDHCRDFLKrifvEAKLRPSADELLR 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
37-282 4.71e-26

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 107.48  E-value: 4.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIK-----QIESESERKAFiVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYA 107
Cdd:cd14071   3 DIERTIGKGNFAVVKLARHRitKTEVAIKiidksQLDEENLKKIY-REVQIMKMLNHPHIIKLYQVmeTKDMLYLVTEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVL--HG--AEPlpyytAAHAMSWclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd14071  82 SNGEIFDYLaqHGrmSEK-----EARKKFW--QILSAVEYCHKRH---IVHRDLKAENLLLDANMNI-KIADFGFSNFFK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 T--HMTNNKGSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDeigGPAFRIMWA-VHNGT-RPPLIknLPKP 258
Cdd:cd14071 151 PgeLLKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFD---GSTLQTLRDrVLSGRfRIPFF--MSTD 225
                       250       260
                ....*....|....*....|....
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14071 226 CEHLIRRMLVLDPSKRLTIEQIKK 249
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
37-301 6.04e-26

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 108.99  E-value: 6.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIKQIESESER----KAFIVELRQLSRVNHPNIVKLYGACLNP--------VCL 102
Cdd:cd07855   8 EPIETIGSGAYGVVCSAidTKSGQKVAIKKIPNAFDVvttaKRTLRELKILRHFKHDNIIAIRDILRPKvpyadfkdVYV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNlLLVAGGTVLKICDFGTA--- 179
Cdd:cd07855  88 VLDLMES-DLHHIIHSDQPL---TLEHIRYFLYQLLRGLKYIHSAN---VIHRDLKPSN-LLVNENCELKIGDFGMArgl 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 ----CDIQTHMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF-------------DEIGGPAFRIMW 241
Cdd:cd07855 160 ctspEEHKYFMTEYVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFpgknyvhqlqlilTVLGTPSQAVIN 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 242 AVHNGTRPPLIKNLPK--PIE-------------SLMTRCWSKDPSQRPSMEEivkIMTH--LMRYFPGADEPLQYP 301
Cdd:cd07855 240 AIGADRVRRYIQNLPNkqPVPwetlypkadqqalDLLSQMLRFDPSERITVAE---ALQHpfLAKYHDPDDEPDCAP 313
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
32-223 6.42e-26

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 107.80  E-value: 6.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVVCKAKWRA--KDVAIKQIESeseRKAF-------IVELRQLSRVN-HPNIVKLYGACLNPVC 101
Cdd:cd07832   1 RYKILGR---IGEGAHGIVFKAKDREtgETVALKKVAL---RKLEggipnqaLREIKALQACQgHPYVVKLRDVFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 --LVMEYAeGGSLYNVLHGAE-PLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGT 178
Cdd:cd07832  75 fvLVFEYM-LSSLSEVLRDEErPL---TEAQVKRYMRMLLKGVAYMHA---NRIMHRDLKPANLLISSTG-VLKIADFGL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 A----CDIQTHMTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVI 223
Cdd:cd07832 147 ArlfsEEDPRLYSHQVATRWYRAPELLYGSrKYDEGVDLWAVGCIFAELL 196
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
37-280 6.93e-26

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 107.00  E-value: 6.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYG---ACLNPVCLVMEY 106
Cdd:cd14163   3 QLGKTIGEGTYSKVKEAfsKKHQRKVAIKIIDKSGGPEEFIQrflprELQIVERLDHKNIIHVYEmleSADGKIYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYN-VLHGAePLPyytAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLvaGGTVLKICDFGTACDI-QT 184
Cdd:cd14163  83 AEDGDVFDcVLHGG-PLP---EHRAKALFRQLVEAIRYCHGC---GVAHRDLKCENALL--QGFTLKLTDFGFAKQLpKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNK---GSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDEIGGPafRIMWAVHNGTRPPLIKNLPKPIE 260
Cdd:cd14163 154 GRELSQtfcGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIP--KMLCQQQKGVSLPGHLGVSRTCQ 231
                       250       260
                ....*....|....*....|
gi 21735562 261 SLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14163 232 DLLKRLLEPDMVLRPSIEEV 251
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
30-278 8.10e-26

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 107.47  E-value: 8.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAK-DVAIKQIESES-ERKAFIVELRQLSRVNHPNIVKLYGACLN-PVCLVMEY 106
Cdd:cd05071   5 EIPRESLRLEVKLGQGCFGEVWMGTWNGTtRVAIKTLKPGTmSPEAFLQEAQVMKKLRHEKLVQLYAVVSEePIYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQ--- 183
Cdd:cd05071  85 MSKGSLLDFLKG-EMGKYLRLPQLVDMAAQIASGMAYVERMN---YVHRDLRAANIL-VGENLVCKVADFGLARLIEdne 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 -THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRPPLIKNLPKPIES 261
Cdd:cd05071 160 yTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKgRVPYP--GMVNREVLDQVERGYRMPCPPECPESLHD 237
                       250
                ....*....|....*..
gi 21735562 262 LMTRCWSKDPSQRPSME 278
Cdd:cd05071 238 LMCQCWRKEPEERPTFE 254
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
34-289 8.19e-26

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 107.84  E-value: 8.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVE--EVVGRGAFGVVCKAKWRAKD------VAIKQIESESERKA---FIVELRQLSRVNHPNIVKLYGACLNP-VC 101
Cdd:cd05110   5 KETELKrvKVLGSGAFGTVYKGIWVPEGetvkipVAIKILNETTGPKAnveFMDEALIMASMDHPHLVRLLGVCLSPtIQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC- 180
Cdd:cd05110  85 LVTQLMPHGCLLDYVH--EHKDNIGSQLLLNWCVQIAKGMMYL---EERRLVHRDLAARNVLVKSPNHV-KITDFGLARl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 ----DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIggPAFRIMWAVHNGTRPPLIKNL 255
Cdd:cd05110 159 legdEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGI--PTREIPDLLEKGERLPQPPIC 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05110 237 TIDVYMVMVKCWMIDADSRPKFKELAAEFSRMAR 270
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
41-282 9.50e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 106.37  E-value: 9.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVV--CKAKWRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKL-----YGACLnpVCLVMEYAEG 109
Cdd:cd08223   7 VIGKGSYGEVwlVRHKRDRKQYVIKKLNlknaSKRERKAAEQEAKLLSKLKHPNIVSYkesfeGEDGF--LYIVMGFCEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVL--HGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGgTVLKICDFGTA------CD 181
Cdd:cd08223  85 GDLYTRLkeQKGVLLE---ERQVVEWFVQIAMALQYMHE---RNILHRDLKTQNIFLTKS-NIIKVGDLGIArvlessSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD--EIGGPAFRIMwavhNGTRPPLIKNLPKPI 259
Cdd:cd08223 158 MATTLI---GTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNakDMNSLVYKIL----EGKLPPMPKQYSPEL 230
                       250       260
                ....*....|....*....|...
gi 21735562 260 ESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd08223 231 GELIKAMLHQDPEKRPSVKRILR 253
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
37-282 1.03e-25

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 107.42  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGR---GAFGVVCKAKWRAKDV--AIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06644  12 EVWEIIGElgdGAFGKVYKAKNKETGAlaAAKVIEtkSEEELEDYMVEIEILATCNHPYIVKLLGAFYwdGKLWIMIEFC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLhgAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFG-TACDIQTHM 186
Cdd:cd06644  92 PGGAVDAIM--LELDRGLTEPQIQVICRQMLEALQYLHSMK---IIHRDLKAGNVLLTLDGDI-KLADFGvSAKNVKTLQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNK--GSAAWMAPEV-----FEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNgTRPPLIKNLPK-- 257
Cdd:cd06644 166 RRDSfiGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELN--PMRVLLKIAK-SEPPTLSQPSKws 242
                       250       260
                ....*....|....*....|....*.
gi 21735562 258 -PIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06644 243 mEFRDFLKTALDKHPETRPSAAQLLE 268
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
42-280 1.11e-25

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 106.82  E-value: 1.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIE--SESERKAFIVELRQLSRVNHPNIVK----LY-GACLNpvcLVMEYAEGGSL 112
Cdd:cd14154   1 LGKGFFGQAIKVTHREtgEVMVMKELIrfDEEAQRNFLKEVKVMRSLDHPNVLKfigvLYkDKKLN---LITEYIPGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHG-AEPLPYytaAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLkICDFGTACDIQ-------- 183
Cdd:cd14154  78 KDVLKDmARPLPW---AQRVRFAKDIASGMAYLHSMN---IIHRDLNSHNCLVREDKTVV-VADFGLARLIVeerlpsgn 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 -------THMTNNK--------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKpfdeiGGPAF--RIMWAVHN- 245
Cdd:cd14154 151 mspsetlRHLKSPDrkkrytvvGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVE-----ADPDYlpRTKDFGLNv 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21735562 246 -GTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14154 226 dSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETL 261
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
34-282 1.18e-25

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 106.19  E-value: 1.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKD--VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYG----AClnPVCL 102
Cdd:cd14116   5 EDFEIGRPLGKGKFGNVYLAREKQSKfiLALKvlfkaQLEKAGVEHQLRREVEIQSHLRHPNILRLYGyfhdAT--RVYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTACDI 182
Cdd:cd14116  83 ILEYAPLGTVYREL---QKLSKFDEQRTATYITELANALSYCHS---KRVIHRDIKPENLLLGSAGE-LKIADFGWSVHA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 -QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD-EIGGPAFRIMWAVHNgTRPPLIKNLPKpie 260
Cdd:cd14116 156 pSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEaNTYQETYKRISRVEF-TFPDFVTEGAR--- 231
                       250       260
                ....*....|....*....|..
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14116 232 DLISRLLKHNPSQRPMLREVLE 253
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
35-287 1.23e-25

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 106.65  E-value: 1.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAK--WRAKDVAIKQIESESERKAFIV--ELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAE 108
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARnlHTGELAAVKIIKLEPGDDFSLIqqEIFMVKECKHCNIVAYFGSylSREKLWICMEYCG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAmswCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTN 188
Cdd:cd06646  90 GGSLQDIYHVTGPLSELQIAYV---CRETLQGLAYLHS---KGKMHRDIKGANILLTDNGDV-KLADFGVAAKITATIAK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NK---GSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIgGPAFRIMWAVHNGTRPPLIKNLPK---PI 259
Cdd:cd06646 163 RKsfiGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDL-HPMRALFLMSKSNFQPPKLKDKTKwssTF 241
                       250       260
                ....*....|....*....|....*...
gi 21735562 260 ESLMTRCWSKDPSQRPSMEeivKIMTHL 287
Cdd:cd06646 242 HNFVKISLTKNPKKRPTAE---RLLTHL 266
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
40-287 1.63e-25

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 106.59  E-value: 1.63e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGA------CLNPVCLVMEYAEGGSL 112
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFReTEIYQTVMLRHENILGFIAAdikstgSWTQLWLITEYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHgAEPLpyyTAAHAMSWCLQCSQGVAYLHS----MQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTA------CD 181
Cdd:cd14056  81 YDYLQ-RNTL---DTEEALRLAYSAASGLAHLHTeivgTQGKpAIAHRDLKSKNILVKRDGTCC-IADLGLAvrydsdTN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNK-GSAAWMAPEVFEGS----NYSE-KC-DVFSWGIILWEVITRRK----------PFDEIGG--PAFRIMWA 242
Cdd:cd14056 156 TIDIPPNPRvGTKRYMAPEVLDDSinpkSFESfKMaDIYSFGLVLWEIARRCEiggiaeeyqlPYFGMVPsdPSFEEMRK 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 243 V--HNGTRPPL---IKNLP--KPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14056 236 VvcVEKLRPPIpnrWKSDPvlRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
31-280 1.94e-25

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 106.20  E-value: 1.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVV----CKAKWRAKD---VAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACLN--P 99
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVflaeCHNLLPEQDkmlVAVKALKeaTESARQDFQREAELLTVLQHQHIVRFYGVCTEgeP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVL--HGAE----------PLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAG 167
Cdd:cd05092  82 LIMVFEYMRHGDLNRFLrsHGPDakildggegqAPGQLTLGQMLQIASQIASGMVYLASLH---FVHRDLATRNCL-VGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 168 GTVLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGP-AFRIM 240
Cdd:cd05092 158 GLVVKIGDFGMSRDIYSTDYYRVGGRTmlpirWMPPESILYRKFTTESDIWSFGVVLWEIFTYgKQPWYQLSNTeAIECI 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 241 WAVHNGTRPpliKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05092 238 TQGRELERP---RTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
30-280 2.60e-25

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 105.92  E-value: 2.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAK-------WRAKDVAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLN- 98
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGEllgpsseESAISVAIKTLKENASpktQQDFRREAELMSDLQHPNIVCLLGVCTKe 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 -PVCLVMEYAEGGSLYNVLHGAEPLPYYTAA------HAMSWC-------LQCSQGVAYLHSmqpKALIHRDLKPPNLLl 164
Cdd:cd05048  81 qPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSsdddgtASSLDQsdflhiaIQIAAGMEYLSS---HHYVHRDLAARNCL- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 165 VAGGTVLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeIGGPAFR 238
Cdd:cd05048 157 VGDGLTVKISDFGLSRDIYSSDYYRVQSKSllpvrWMPPEAILYGKFTTESDVWSFGVVLWEIFSYgLQPY--YGYSNQE 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 239 IMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05048 235 VIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
35-287 2.91e-25

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 105.48  E-value: 2.91e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHG-EVAIRLIDierdNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPphLAIITSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSWclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlkICDFG--------TAC 180
Cdd:cd14153  80 GRTLYSVVRDAKVVLDVNKTRQIAQ--EIVKGMGYLHA---KGILHKDLKSKNVFYDNGKVV--ITDFGlftisgvlQAG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSN---------YSEKCDVFSWGIILWEVITRRKPFDEigGPAFRIMWAVHNGTRPPL 251
Cdd:cd14153 153 RREDKLRIQSGWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREWPFKT--QPAEAIIWQVGSGMKPNL 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 252 IK-NLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14153 231 SQiGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
42-228 2.98e-25

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 106.06  E-value: 2.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESE------RKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLY 113
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSEldwsvvKNSFLTEVEKLSRFRHPNIVDLAGYSAQQgnYCLIYVYLPNGSLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVlKICDFGTA-----------CDI 182
Cdd:cd14159  81 DRLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDSP-SLIHGDVKSSNILLDAALNP-KLGDFGLArfsrrpkqpgmSST 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP 228
Cdd:cd14159 159 LARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
35-280 3.10e-25

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 105.70  E-value: 3.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKDV--AIKQIESESERKAF---IVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06622   2 EIEVLDELGKGNYGSVYKVLHRPTGVtmAMKEIRLELDESKFnqiIMELDILHKAVSPYIVDFYGAFFieGAVYMCMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGA-------EPLPYYTAAHAMswclqcsQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC 180
Cdd:cd06622  82 DAGSLDKLYAGGvategipEDVLRRITYAVV-------KGLKFLK--EEHNIIHRDVKPTNVLVNGNGQV-KLCDFGVSG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMT-NNKGSAAWMAPEVFEGSN------YSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLI 252
Cdd:cd06622 152 NLVASLAkTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYpPETYANIFAQLSAIVDGDPPTLP 231
                       250       260
                ....*....|....*....|....*...
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd06622 232 SGYSDDAQDFVAKCLNKIPNRRPTYAQL 259
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
30-280 3.68e-25

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 105.84  E-value: 3.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVV--CKA----KWRAKD------------VAIKQIESESERKA---FIVELRQLSRVNHPN 88
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVhlCEAegmeKFMDKDfalevsenqpvlVAVKMLRADANKNArndFLKEIKIMSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  89 IVKLYGACL--NPVCLVMEYAEGGSLYNVLHGAEP---LPYYTAAHAMSW------CLQCSQGVAYLHSMQpkaLIHRDL 157
Cdd:cd05095  81 IIRLLAVCItdDPLCMITEYMENGDLNQFLSRQQPegqLALPSNALTVSYsdlrfmAAQIASGMKYLSSLN---FVHRDL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 158 KPPNLLlVAGGTVLKICDFGTACDIQT-HMTNNKGSAA----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT--RRKPFD 230
Cdd:cd05095 158 ATRNCL-VGKNYTIKIADFGMSRNLYSgDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQPYS 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 231 EIG--------GPAFRIMWAVHNGTRPPLIknlPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05095 237 QLSdeqvientGEFFRDQGRQTYLPQPALC---PDSVYKLMLSCWRRDTKDRPSFQEI 291
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
42-288 3.87e-25

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 106.25  E-value: 3.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA------KWRAKD---VAIKQIESESERKAF---IVELRQLSRV-NHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05101  32 LGEGCFGQVVMAeavgidKDKPKEavtVAVKMLKDDATEKDLsdlVSEMEMMKMIgKHKNIINLLGACTQdgPLYVIVEY 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPY-------------YTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKI 173
Cdd:cd05101 112 ASKGNLREYLRARRPPGMeysydinrvpeeqMTFKDLVSCTYQLARGMEYLASQK---CIHRDLAARNVL-VTENNVMKI 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDIQT-----HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIggpaFRIMWA 242
Cdd:cd05101 188 ADFGLARDINNidyykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGspypgiPVEEL----FKLLKE 263
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 243 VHNGTRPpliKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05101 264 GHRMDKP---ANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
34-280 4.59e-25

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 104.99  E-value: 4.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKDV-AIKQIE----SESERKAFIVE---LRQLSrvNHPNIVKLYGACLNP----VC 101
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIyALKRVDlegaDEQTLQSYKNEielLKKLK--GSDRIIQLYDYEVTDeddyLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGgSLYNVLHGAEPLPYYTAAHAMSW--CLQCsqgVAYLHSmqpKALIHRDLKPPNLLLVAGgtVLKICDFGTA 179
Cdd:cd14131  79 MVMECGEI-DLATILKKKRPKPIDPNFIRYYWkqMLEA---VHTIHE---EGIVHSDLKPANFLLVKG--RLKLIDFGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNK-----GSAAWMAPEVFEGSNYSE----------KCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVH 244
Cdd:cd14131 150 KAIQNDTTSIVrdsqvGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIID 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21735562 245 NGTRpplIKNLPKPIESL---MTRCWSKDPSQRPSMEEI 280
Cdd:cd14131 230 PNHE---IEFPDIPNPDLidvMKRCLQRDPKKRPSIPEL 265
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
37-279 4.65e-25

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 105.44  E-value: 4.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQI---ESESERKAFIVE----LRQLSRVNHPNIVKLYGACLNP-------V 100
Cdd:cd07838   2 EEVAEIGEGAYGTVYKARDLqdGRFVALKKVrvpLSEEGIPLSTIReialLKQLESFEHPNVVRLLDVCHGPrtdrelkL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGG-SLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTA 179
Cdd:cd07838  82 TLVFEHVDQDlATYLDKCPKPGLPPETIKDLMR---QLLRGLDFLHSH---RIVHRDLKPQNILVTSDGQV-KLADFGLA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 --CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEvITRRKP--------------FDEIGGP-------- 235
Cdd:cd07838 155 riYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAE-LFNRRPlfrgsseadqlgkiFDVIGLPseeewprn 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 236 ------AFRimwavHNGTRPP--LIKNLPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd07838 234 salprsSFP-----SYTPRPFksFVPEIDEEGLDLLKKMLTFNPHKRISAFE 280
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
42-303 7.16e-25

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 105.95  E-value: 7.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD----VAIKQIESESERKAF----IVELRQLSRV-NHPNIVKLY------GACLNPVCLVMEY 106
Cdd:cd07857   8 LGQGAYGIVCSARNAETSeeetVAIKKITNVFSKKILakraLRELKLLRHFrGHKNITCLYdmdivfPGNFNELYLYEEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKICDFGTACDI---- 182
Cdd:cd07857  88 MEA-DLHQIIRSGQPL---TDAHFQSFIYQILCGLKYIHSAN---VLHRDLKPGNLLVNADCE-LKICDFGLARGFsenp 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 ---QTHMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITrRKPFDE--------------IGGPAFRIMWAVH 244
Cdd:cd07857 160 genAGFMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLG-RKPVFKgkdyvdqlnqilqvLGTPDEETLSRIG 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 245 NGTRPPLIKNLP----KPIES-----------LMTRCWSKDPSQRPSMEEivkIMTH--LMRYFPGADEPLqypCQ 303
Cdd:cd07857 239 SPKAQNYIRSLPnipkKPFESifpnanplaldLLEKLLAFDPTKRISVEE---ALEHpyLAIWHDPDDEPV---CQ 308
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-233 7.32e-25

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 104.91  E-value: 7.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEevVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd14085   3 DFFEIESE--LGRGATSVVyrCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPteISLVLELV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYN--VLHGaeplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV--AGGTVLKICDFGTA--CD 181
Cdd:cd14085  81 TGGELFDriVEKG-----YYSERDAADAVKQILEAVAYLHE---NGIVHRDLKPENLLYAtpAPDAPLKIADFGLSkiVD 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 182 IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIG 233
Cdd:cd14085 153 QQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFyDERG 205
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
41-229 7.51e-25

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 104.58  E-value: 7.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESE--SERKAF---IVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05608   8 VLGKGGFGEVSACQMRAtgKLYACKKLNKKrlKKRKGYegaMVEKRILAKVHSRFIVSLAYAfqTKTDLCLVMTIMNGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L-YNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK 190
Cdd:cd05608  88 LrYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQ---RRIIYRDLKPENVLLDDDGNV-RISDLGLAVELKDGQTKTK 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21735562 191 GSAA---WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05608 164 GYAGtpgFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPF 205
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
42-282 8.40e-25

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 103.75  E-value: 8.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNVLH 117
Cdd:cd14156   1 IGSGFFSKVYKVTHGAtgKVMVVKIYKNDVDQHKIVREISLLQKLSHPNIVRYLGICVkdEKLHPILEYVSGGCLEELLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 GAEPlpyytaahAMSW----CLQC--SQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLK--ICDFGTACDIQTHMTNN 189
Cdd:cd14156  81 REEL--------PLSWrekvELACdiSRGMVYLHS---KNIYHRDLNSKNCLIRVTPRGREavVTDFGLAREVGEMPAND 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K-------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrRKPFDEIGGP----------AFRIMwavhngtrpplI 252
Cdd:cd14156 150 PerklslvGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILA-RIPADPEVLPrtgdfgldvqAFKEM-----------V 217
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14156 218 PGCPEPFLDLAASCCRMDAFKRPSFAELLD 247
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
34-229 1.05e-24

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 104.20  E-value: 1.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQIEseserKAFIVELRQ----------LSRVNHPNIVKLYGACLNPVC 101
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGkyYALKILK-----KAKIIKLKQvehvlnekriLSEVRHPFIVNLLGSFQDDRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 L--VMEYAEGGSLYNVLHGAEPLPYYTAahaMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKICDFGTA 179
Cdd:cd05580  76 LymVMEYVPGGELFSLLRRSGRFPNDVA---KFYAAEVVLALEYLHSLD---IVYRDLKPENLLLDSDGH-IKITDFGFA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05580 149 KRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF 198
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
42-289 1.15e-24

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 105.45  E-value: 1.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKW-------RAKDVAIKQIE---SESERKAFIVELRQLSRV-NHPNIVKLYGACLN---PVCLVMEYA 107
Cdd:cd05103  15 LGRGAFGQVIEADAfgidktaTCRTVAVKMLKegaTHSEHRALMSELKILIHIgHHLNVVNLLGACTKpggPLMVIVEFC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHG--AEPLPYYTAA--------------------------------------------------------- 128
Cdd:cd05103  95 KFGNLSAYLRSkrSEFVPYKTKGarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsdveeeeagqedlykd 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 129 -----HAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTACDIQTHMTN-NKGSA----AWMAP 198
Cdd:cd05103 175 fltleDLICYSFQVAKGMEFLAS---RKCIHRDLAARNILL-SENNVVKICDFGLARDIYKDPDYvRKGDArlplKWMAP 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 199 EVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeiggPAFRI----MWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQ 273
Cdd:cd05103 251 ETIFDRVYTIQSDVWSFGVLLWEIFSLgASPY-----PGVKIdeefCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQ 325
                       330
                ....*....|....*.
gi 21735562 274 RPSMEEIVKIMTHLMR 289
Cdd:cd05103 326 RPTFSELVEHLGNLLQ 341
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
37-282 1.42e-24

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 103.10  E-value: 1.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIE-SESERKAFIV--ELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd14185   3 EIGRTIGDGNFAVVkeCRHWNENQEYAMKIIDkSKLKGKEDMIesEILIIKSLSHPNIVKLFEVyeTEKEIYLILEYVRG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAA-HAMSWClqcsQGVAYLHSmqpKALIHRDLKPPNLLL---VAGGTVLKICDFGTACDIQTH 185
Cdd:cd14185  83 GDLFDAIIESVKFTEHDAAlMIIDLC----EALVYIHS---KHIVHRDLKPENLLVqhnPDKSTTLKLADFGLAKYVTGP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-------DEIggpaFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:cd14185 156 IFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrsperdqEEL----FQIIQLGHYEFLPPYWDNISEA 231
                       250       260
                ....*....|....*....|....
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14185 232 AKDLISRLLVVDPEKRYTAKQVLQ 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
36-229 1.51e-24

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 103.08  E-value: 1.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKAKWRAK--DVAIKQIESES--ERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14190   6 IHSKEVLGGGKFGKVHTCTEKRTglKLAAKVINKQNskDKEMVLLEIQVMNQLNHRNLIQLYEAIETPneIVLFMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYN-VLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLV-AGGTVLKICDFGTA--CDIQTH 185
Cdd:cd14190  86 GELFErIVDEDYHL---TEVDAMVFVRQICEGIQFMHQMR---VLHLDLKPENILCVnRTGHQVKIIDFGLArrYNPREK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14190 160 LKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPF 203
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
42-274 1.82e-24

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 103.07  E-value: 1.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDV--AIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRtfALKCV-----KKRHIVQTRQqehifsekeiLEECNSPFIVKLYRTFKDKkyLYMLMEYC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAahamSWCLQC-SQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQthm 186
Cdd:cd05572  76 LGGELWTILRDRGLFDEYTA----RFYTACvVLAFEYLHSRG---IIYRDLKPENLLLDSNGYV-KLVDFGFAKKLG--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 tnnKGSAAW--------MAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRP---PliKNL 255
Cdd:cd05572 145 ---SGRKTWtfcgtpeyVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKIYNIILKGIDKiefP--KYI 219
                       250
                ....*....|....*....
gi 21735562 256 PKPIESLMTRCWSKDPSQR 274
Cdd:cd05572 220 DKNAKNLIKQLLRRNPEER 238
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
42-282 2.31e-24

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 102.60  E-value: 2.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK--WRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSL- 112
Cdd:cd14072   8 IGKGNFAKVKLARhvLTGREVAIKIIDktqlNPSSLQKLFREVRIMKILNHPNIVKLFEVIETekTLYLVMEYASGGEVf 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 -YNVLHGAeplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAcdiQTHMTNNK- 190
Cdd:cd14072  88 dYLVAHGR-----MKEKEARAKFRQIVSAVQYCHQ---KRIVHRDLKAENLLLDADMNI-KIADFGFS---NEFTPGNKl 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ----GSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGT-RPPLIknLPKPIESLMT 264
Cdd:cd14072 156 dtfcGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFD--GQNLKELRERVLRGKyRIPFY--MSTDCENLLK 231
                       250
                ....*....|....*...
gi 21735562 265 RCWSKDPSQRPSMEEIVK 282
Cdd:cd14072 232 KFLVLNPSKRGTLEQIMK 249
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
37-280 2.37e-24

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 102.47  E-value: 2.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYA 107
Cdd:cd14073   4 ELLETLGKGTYGKVKLAIERATGreVAIKsikkdKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENkdKIVIVMEYA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTH-- 185
Cdd:cd14073  84 SGGELYDYISERRRLPEREARRIFR---QIVSAVHYCHKNG---VVHRDLKLENILLDQNGNA-KIADFGLSNLYSKDkl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDeigGPAFRIMW-AVHNGT-RPPliknlPKPIE-- 260
Cdd:cd14073 157 LQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFD---GSDFKRLVkQISSGDyREP-----TQPSDas 228
                       250       260
                ....*....|....*....|
gi 21735562 261 SLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14073 229 GLIRWMLTVNPKRRATIEDI 248
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
32-282 2.47e-24

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 102.53  E-value: 2.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIeveevvGRGAFGVVCKA--KWRAKDVAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCL 102
Cdd:cd06607   5 DLREI------GHGSFGAVYYArnKRTSEVVAIKKMsysgkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLreHTAWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAhamSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTA--- 179
Cdd:cd06607  79 VMEYCLGSASDIVEVHKKPLQEVEIA---AICHGALQGLAYLHSHN---RIHRDVKAGNILLTEPGTV-KLADFGSAslv 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMtnnkGSAAWMAPEVF----EGsNYSEKCDVFSWGIILWEvITRRKPfdeiggPAFRI--MWAVHNGTR--PPL 251
Cdd:cd06607 152 CPANSFV----GTPYWMAPEVIlamdEG-QYDGKVDVWSLGITCIE-LAERKP------PLFNMnaMSALYHIAQndSPT 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 252 IKNLPKPIE--SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06607 220 LSSGEWSDDfrNFVDSCLQKIPQDRPSAEDLLK 252
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
35-282 2.60e-24

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 103.67  E-value: 2.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKDV--AIKQIESE---SERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06615   2 DFEKLGELGAGNGGVVTKVLHRPSGLimARKLIHLEikpAIRNQIIRELKVLHECNSPYIVGFYGAFYsdGEISICMEHM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHaMSWCLqcSQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMT 187
Cdd:cd06615  82 DGGSLDQVLKKAGRIPENILGK-ISIAV--LRGLTYLR--EKHKIMHRDVKPSNILVNSRGEI-KLCDFGVSGQLIDSMA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF------------------DEIGGPAFRIMWAVHNGTR 248
Cdd:cd06615 156 NSfVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIpppdakeleamfgrpvseGEAKESHRPVSGHPPDSPR 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 249 P-------PLIKNLPKPI----------ESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06615 236 PmaifellDYIVNEPPPKlpsgafsdefQDFVDKCLKKNPKERADLKELTK 286
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
77-282 2.84e-24

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 102.03  E-value: 2.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  77 ELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIH 154
Cdd:cd14075  51 EISSMEKLHHPNIIRLYEVveTLSKLHLVMEYASGGELYTKISTEGKLSESEAKPLFA---QIVSAVKHMHENN---IIH 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 155 RDLKPPNLLLvAGGTVLKICDFG--TACDIQTHMTNNKGSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPF-- 229
Cdd:cd14075 125 RDLKAENVFY-ASNNCVKVGDFGfsTHAKRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFra 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 230 DEIGGPAFRIMWAVHngTRPPlikNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14075 204 ETVAKLKKCILEGTY--TIPS---YVSEPCQELIRGILQPVPSDRYSIDEIKN 251
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
43-229 4.26e-24

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 102.53  E-value: 4.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKakWRAKD----VAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKlygAC-----LNPVC------L 102
Cdd:cd13989   2 GSGGFGYVTL--WKHQDtgeyVAIKKCRqelspSDKNRERWCLEVQIMKKLNHPNVVS---ARdvppeLEKLSpndlplL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLL--VAGGTVLKICDFGTAC 180
Cdd:cd13989  77 AMEYCSGGDLRKVLNQPENCCGLKESEVRTLLSDISSAISYLHE---NRIIHRDLKPENIVLqqGGGRVIYKLIDLGYAK 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 181 DI--QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd13989 154 ELdqGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
31-292 4.75e-24

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 102.40  E-value: 4.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVV----CKAKWRAKD---VAIKQIESE--SERKAFIVELRQLSRVNHPNIVKLYGACLN--P 99
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVflaeCYNLSPTKDkmlVAVKTLKDPtlAARKDFQREAELLTNLQHDHIVKFYGVCGDgdP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVL--HGAEPLPYYTA-----------AHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVA 166
Cdd:cd05094  82 LIMVFEYMKHGDLNKFLraHGPDAMILVDGqprqakgelglSQMLHIATQIASGMVYLASQH---FVHRDLATRNCL-VG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 167 GGTVLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIM 240
Cdd:cd05094 158 ANLLVKIGDFGMSRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSFGVILWEIFTYgKQPWFQLSNT--EVI 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 241 WAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFP 292
Cdd:cd05094 236 ECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
37-282 4.84e-24

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 101.23  E-value: 4.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQIES----ESERKAFIVELRQLSRVN-HPNIVKLYGAC--LNPVCLVMEYA 107
Cdd:cd14050   4 TILSKLGEGSFGEVFKVRSRedGKLYAVKRSRSrfrgEKDRKRKLEEVERHEKLGeHPNCVRFIKAWeeKGILYIQTELC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 eGGSLYNVLHGAEPLPYYTAahamsWCLQCS--QGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTH 185
Cdd:cd14050  84 -DTSLQQYCEETHSLPESEV-----WNILLDllKGLKHLHD---HGLIHLDIKPANIFLSKDG-VCKLGDFGLVVELDKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNN--KGSAAWMAPEVFEGSnYSEKCDVFSWGIILWEVITrrkpfdEIGGPAFRIMW-AVHNGTRP-----PLIKNLPK 257
Cdd:cd14050 154 DIHDaqEGDPRYMAPELLQGS-FTKAADIFSLGITILELAC------NLELPSGGDGWhQLRQGYLPeeftaGLSPELRS 226
                       250       260
                ....*....|....*....|....*
gi 21735562 258 PIESLMTrcwsKDPSQRPSMEEIVK 282
Cdd:cd14050 227 IIKLMMD----PDPERRPTAEDLLA 247
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
42-282 5.48e-24

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 101.64  E-value: 5.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIVELRQ----LSRVNHPNIVKLYGACLNP-VC-LVMEYAEGGSLY 113
Cdd:cd14069   9 LGEGAFGEVFLAVNRntEEAVAVKFVDMKRAPGDCPENIKKevciQKMLSHKNVVRFYGHRREGeFQyLFLEYASGGELF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGtVLKICDFGTA----CDIQTHMTNN 189
Cdd:cd14069  89 DKI---EPDVGMPEDVAQFYFQQLMAGLKYLHSC---GITHRDIKPENLLLDEND-NLKISDFGLAtvfrYKGKERLLNK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K-GSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGT---RPplIKNLPKPIESLMT 264
Cdd:cd14069 162 McGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKtylTP--WKKIDTAALSLLR 239
                       250
                ....*....|....*...
gi 21735562 265 RCWSKDPSQRPSMEEIVK 282
Cdd:cd14069 240 KILTENPNKRITIEDIKK 257
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
57-284 5.92e-24

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 101.97  E-value: 5.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  57 AKDVAIKQIESESERKAFiVELRQ----LSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHG-AEPLPYYTAAHAM 131
Cdd:cd14067  37 SADTMLKHLRAADAMKNF-SEFRQeasmLHSLQHPCIVYLIGISIHPLCFALELAPLGSLNTVLEEnHKGSSFMPLGHML 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 132 SW--CLQCSQGVAYLHSmqpKALIHRDLKPPNLLL----VAGGTVLKICDFGtacdIQTHMTNN-----KGSAAWMAPEV 200
Cdd:cd14067 116 TFkiAYQIAAGLAYLHK---KNIIFCDLKSDNILVwsldVQEHINIKLSDYG----ISRQSFHEgalgvEGTPGYQAPEI 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 201 FEGSNYSEKCDVFSWGIILWEVITRRKPfdEIGGPAFRIMWAVHNGTRPPLIKnlPKPI-----ESLMTRCWSKDPSQRP 275
Cdd:cd14067 189 RPRIVYDEKVDMFSYGMVLYELLSGQRP--SLGHHQLQIAKKLSKGIRPVLGQ--PEEVqffrlQALMMECWDTKPEKRP 264

                ....*....
gi 21735562 276 SMEEIVKIM 284
Cdd:cd14067 265 LACSVVEQM 273
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
42-281 6.06e-24

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 102.37  E-value: 6.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNV 115
Cdd:cd06659  29 IGEGSTGVVCIAreKHSGRQVAVKMMDlrKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLvgEELWVLMEYLQGGALTDI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK---GS 192
Cdd:cd06659 109 VSQTR----LNEEQIATVCEAVLQALAYLHS---QGVIHRDIKSDSILLTLDGRV-KLSDFGFCAQISKDVPKRKslvGT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP-FDEIGGPAFRIMwavhNGTRPPLIKNLPK--PI-ESLMTRCWS 268
Cdd:cd06659 181 PYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPyFSDSPVQAMKRL----RDSPPPKLKNSHKasPVlRDFLERMLV 256
                       250
                ....*....|...
gi 21735562 269 KDPSQRPSMEEIV 281
Cdd:cd06659 257 RDPQERATAQELL 269
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
41-282 7.03e-24

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 101.46  E-value: 7.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKA--KWRAKDVAIKQIESES------ERKAFIVELRQ-----LSRVNHPNIVKLYGACLNPVCL--VME 105
Cdd:cd06628   7 LIGSGSFGSVYLGmnASSGELMAVKQVELPSvsaenkDRKKSMLDALQreialLRELQHENIVQYLGSSSDANHLniFLE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVL--HGA--EPLpyytaahAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD 181
Cdd:cd06628  87 YVPGGSVATLLnnYGAfeESL-------VRNFVRQILKGLNYLHN---RGIIHRDIKGANILVDNKGGI-KISDFGISKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQ---THMTNNK------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeiggPAFRIMWAVH---NGTRP 249
Cdd:cd06628 156 LEansLSTKNNGarpslqGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF-----PDCTQMQAIFkigENASP 230
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 250 PLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06628 231 TIPSNISSEARDFLEKTFEIDHNKRPTADELLK 263
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
42-290 7.31e-24

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 101.56  E-value: 7.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGAC-----LNpvcLVMEYAEGGSL 112
Cdd:cd14222   1 LGKGFFGQAIKVTHKAtgKVMVMKELIrcDEETQKTFLTEVKVMRSLDHPNVLKFIGVLykdkrLN---LLTEFIEGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYytaAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVLkICDFGTACDI---------- 182
Cdd:cd14222  78 KDFLRADDPFPW---QQKVSFAKGIASGMAYLHSM---SIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIveekkkpppd 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 ------QTHMTNNK-------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVI----------TRRKPFdeigGPAFRI 239
Cdd:cd14222 151 kpttkkRTLRKNDRkkrytvvGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIgqvyadpdclPRTLDF----GLNVRL 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 240 MWAVHngtrppLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRY 290
Cdd:cd14222 227 FWEKF------VPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALSLY 271
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
41-230 8.00e-24

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 100.79  E-value: 8.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWR-AKDV-AIKQ------IESESERKAFiVELRQLSRVNHPNIVKLYGA-CLNPVC-LVMEYAEGG 110
Cdd:cd05578   7 VIGKGSFGKVCIVQKKdTKKMfAMKYmnkqkcIEKDSVRNVL-NELEILQELEHPFLVNLWYSfQDEEDMyMVVDLLLGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SL-YNVLHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT-HMTN 188
Cdd:cd05578  86 DLrYHLQQKVK----FSEETVKFYICEIVLALDYLHS---KNIIHRDIKPDNILLDEQGHV-HITDFNIATKLTDgTLAT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 189 NK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd05578 158 STsGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYE 200
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
40-289 8.59e-24

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 103.39  E-value: 8.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA-------KWRAKDVAIKQIESES---ERKAFIVELRQLSRV-NHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd05106  44 KTLGAGAFGKVVEAtafglgkEDNVLRVAVKMLKASAhtdEREALMSELKILSHLgQHKNIVNLLGACTHggPVLVITEY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVL-HGAE-----------------------------------------------PLPYYTAAHAMSWC---- 134
Cdd:cd05106 124 CCYGDLLNFLrKKAEtflnfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvemrPVSSSSSQSSDSKDeedt 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 135 ---------------LQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKICDFGTACDIqthMTNN----KGSA-- 193
Cdd:cd05106 204 edswpldlddllrfsSQVAQGMDFLAS---KNCIHRDVAARNVLL-TDGRVAKICDFGLARDI---MNDSnyvvKGNArl 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 194 --AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEI--GGPAFRIMWAVHNGTRPPLIknlPKPIESLMTRCWS 268
Cdd:cd05106 277 pvKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLgKSPYPGIlvNSKFYKMVKRGYQMSRPDFA---PPEIYSIMKMCWN 353
                       330       340
                ....*....|....*....|.
gi 21735562 269 KDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05106 354 LEPTERPTFSQISQLIQRQLG 374
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
37-229 1.24e-23

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 101.10  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACLNP--------VCL 102
Cdd:cd07840   2 EKIAQIGEGTYGQVYKARNKktGELVALKKIRMENEKEGFpitaIREIKLLQKLDHPNVVRLKEIVTSKgsakykgsIYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAE---GGSLYNvlhgaePLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTA 179
Cdd:cd07840  82 VFEYMDhdlTGLLDN------PEVKFTESQIKCYMKQLLEGLQYLHS---NGILHRDIKGSNILINNDG-VLKLADFGLA 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 180 cdiqTHMTN-------NKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07840 152 ----RPYTKennadytNRVITLWYrPPELLLGAtRYGPEVDMWSVGCILAELFTGKPIF 206
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
30-284 1.25e-23

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 101.20  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKwrAKD---------VAIKQI-ESES--ERKAFIVELRQLSRVNHPNIVKLYGACL 97
Cdd:cd05061   2 EVSREKITLLRELGQGSFGMVYEGN--ARDiikgeaetrVAVKTVnESASlrERIEFLNEASVMKGFTCHHVVRLLGVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 --NPVCLVMEYAEGGSLYNVLHGAEP-------LPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGG 168
Cdd:cd05061  80 kgQPTLVVMELMAHGDLKSYLRSLRPeaennpgRPPPTLQEMIQMAAEIADGMAYLNA---KKFVHRDLAARNCM-VAHD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 169 TVLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDEIGGPafRIMWA 242
Cdd:cd05061 156 FTVKIGDFGMTRDIYETDYYRKGGKGllpvrWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNE--QVLKF 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 243 VHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05061 234 VMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
40-282 1.28e-23

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 100.39  E-value: 1.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIE-SESERKAFIV-ELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLY 113
Cdd:cd06647  13 EKIGQGASGTVYTAIDVAtgQEVAIKQMNlQQQPKKELIInEILVMRENKNPNIVNYLDSYLvgDELWVVMEYLAGGSLT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYYTAAhamsWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDI---QTHMTNNK 190
Cdd:cd06647  93 DVVTETCMDEGQIAA----VCRECLQALEFLHSNQ---VIHRDIKSDNILLGMDGSV-KLTDFGFCAQItpeQSKRSTMV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEigGPAFRIMWAVHNGTrpPLIKN---LPKPIESLMTRC 266
Cdd:cd06647 165 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNE--NPLRALYLIATNGT--PELQNpekLSAIFRDFLNRC 240
                       250
                ....*....|....*.
gi 21735562 267 WSKDPSQRPSMEEIVK 282
Cdd:cd06647 241 LEMDVEKRGSAKELLQ 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
42-276 1.60e-23

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 100.04  E-value: 1.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR----AKDVAIKQIESESERKAFIVELRQLSRV----NHPNIVKLYGAC-LNPVCLVMEYAEGGSL 112
Cdd:cd05116   3 LGSGNFGTVKKGYYQmkkvVKTVAVKILKNEANDPALKDELLREANVmqqlDNPYIVRMIGICeAESWMLVMEMAELGPL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTH------M 186
Cdd:cd05116  83 NKFLQKNR---HVTEKNITELVHQVSMGMKYL---EESNFVHRDLAARNVLLVTQHYA-KISDFGLSKALRADenyykaQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPAFRIMwaVHNGTRPPLIKNLPKPIESLMTR 265
Cdd:cd05116 156 THGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYgQKPYKGMKGNEVTQM--IEKGERMECPAGCPPEMYDLMKL 233
                       250
                ....*....|.
gi 21735562 266 CWSKDPSQRPS 276
Cdd:cd05116 234 CWTYDVDERPG 244
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
37-281 1.85e-23

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 99.79  E-value: 1.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAK--WRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14074   6 DLEETLGRGHFAVVKLARhvFTGEKVAVKVIDktklDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQtkLYLILELGD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL--HG---AEPLpyytaahAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFG------ 177
Cdd:cd14074  86 GGDMYDYImkHEnglNEDL-------ARKYFRQIVSAISYCHKLH---VVHRDLKPENVVFFEKQGLVKLTDFGfsnkfq 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 ------TACdiqthmtnnkGSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPP 250
Cdd:cd14074 156 pgekleTSC----------GSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPA 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 21735562 251 LIKNLPKpieSLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14074 226 HVSPECK---DLIRRMLIRDPKKRASLEEIE 253
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
40-282 1.91e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 100.95  E-value: 1.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQI--ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLY 113
Cdd:cd06655  25 EKIGQGASGTVFTAIDVAtgQEVAIKQInlQKQPKKELIINEILVMKELKNPNIVNFLDSFLvgDELFVVMEYLAGGSLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAeplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDI---QTHMTNNK 190
Cdd:cd06655 105 DVVTET----CMDEAQIAAVCRECLQALEFLHANQ---VIHRDIKSDNVLLGMDGSV-KLTDFGFCAQItpeQSKRSTMV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVH-NGTrpPLIKNLPK--PI-ESLMTRC 266
Cdd:cd06655 177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALYLIAtNGT--PELQNPEKlsPIfRDFLNRC 252
                       250
                ....*....|....*.
gi 21735562 267 WSKDPSQRPSMEEIVK 282
Cdd:cd06655 253 LEMDVEKRGSAKELLQ 268
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
40-280 1.92e-23

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 99.93  E-value: 1.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA---KWRAKdVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYG---ACLNPVCLVMEYAE 108
Cdd:cd14164   6 TTIGEGSFSKVKLAtsqKYCCK-VAIKIVDRRRASPDFVQkflprELSILRRVNHPNIVQMFEcieVANGRLYIVMEAAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GgslyNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTH--- 185
Cdd:cd14164  85 T----DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMN---IVHRDLKCENILLSADDRKIKIADFGFARFVEDYpel 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMwavHNGTRPPLIKNLPKPIESLMT 264
Cdd:cd14164 158 STTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQ---QRGVLYPSGVALEEPCRALIR 234
                       250
                ....*....|....*.
gi 21735562 265 RCWSKDPSQRPSMEEI 280
Cdd:cd14164 235 TLLQFNPSTRPSIQQV 250
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
37-229 2.11e-23

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 99.71  E-value: 2.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESER-KAFIV--ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14095   3 DIGRVIGDGNFAVVkeCRDKATDKEYALKIIDKAKCKgKEHMIenEVAILRRVKHPNIVQLIEEYDTDteLYLVMELVKG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAhAMSWCLqcSQGVAYLHSMQpkaLIHRDLKPPNLLLVA---GGTVLKICDFGTACDIQTHM 186
Cdd:cd14095  83 GDLFDAITSSTKFTERDAS-RMVTDL--AQALKYLHSLS---IVHRDIKPENLLVVEhedGSKSLKLADFGLATEVKEPL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14095 157 FTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPF 199
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
37-295 2.63e-23

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 101.59  E-value: 2.63e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGACLNP--VCL 102
Cdd:cd05573   4 EVIKVIGRGAFGEVWLVRDKDTGqvYAMKIL-----RKSDMLKREQiahvraerdiLADADSPWIVRLHYAFQDEdhLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLP-----YYTAAHAMSwclqcsqgVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:cd05573  79 VMEYMPGGDLMNLLIKYDVFPeetarFYIAELVLA--------LDSLHKL---GFIHRDIKPDNILLDADGHI-KLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDI-----------QTHMTNNK---------------------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR 225
Cdd:cd05573 147 LCTKMnksgdresylnDSVNTLFQdnvlarrrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYG 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 226 RKPF--DEIGGPAFRIM-WAVH-----NGTRPPLIKNLpkpIESLMTrcwskDPSQR-PSMEEivkIMTHLmrYFPGAD 295
Cdd:cd05573 227 FPPFysDSLVETYSKIMnWKESlvfpdDPDVSPEAIDL---IRRLLC-----DPEDRlGSAEE---IKAHP--FFKGID 292
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
35-282 2.85e-23

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 99.38  E-value: 2.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQ----IESESERKAFIVELRQLSRV-NHPNIVKLYGACL--NPVCLVME 105
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGclYAVKKskkpFRGPKERARALREVEAHAALgQHPNIVRYYSSWEegGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTACDIQTH 185
Cdd:cd13997  81 LCENGSLQDALEELSPISKLSEAEVWDLLLQVALGLAFIHS---KGIVHLDIKPDNIFISNKGT-CKIGDFGLATRLETS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITrRKPFDEiGGPafriMWAVHNGTRPPLIKNLPKPIE--SL 262
Cdd:cd13997 157 GDVEEGDSRYLAPELLNENyTHLPKADIFSLGVTVYEAAT-GEPLPR-NGQ----QWQQLRQGKLPLPPGLVLSQEltRL 230
                       250       260
                ....*....|....*....|
gi 21735562 263 MTRCWSKDPSQRPSMEEIVK 282
Cdd:cd13997 231 LKVMLDPDPTRRPTADQLLA 250
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
36-282 3.35e-23

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 99.81  E-value: 3.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVvGRGAFGVVCKAKWRAKD--VAIKQIESE---SERKAFIVELRQLSRVNH-PNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd06617   4 EVIEEL-GRGAYGVVDKMRHVPTGtiMAVKRIRATvnsQEQKRLLMDLDISMRSVDcPYTVTFYGALFREgdVWICMEVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGgSLYNV--------LHGAEPLPYYTAAHAMSwclqcsqGVAYLHSMQpkALIHRDLKPPNLLLVAGGTVlKICDFGTA 179
Cdd:cd06617  83 DT-SLDKFykkvydkgLTIPEDILGKIAVSIVK-------ALEYLHSKL--SVIHRDVKPSNVLINRNGQV-KLCDFGIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHM--TNNKGSAAWMAPEVFEG----SNYSEKCDVFSWGIILWEVITRRKPFDEIGGPaFRIMWAVHNGTRPPLIK 253
Cdd:cd06617 152 GYLVDSVakTIDAGCKPYMAPERINPelnqKGYDVKSDVWSLGITMIELATGRFPYDSWKTP-FQQLKQVVEEPSPQLPA 230
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 254 NLPKP-IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06617 231 EKFSPeFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
38-280 3.42e-23

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 99.26  E-value: 3.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14079   6 LGKTLGVGSFGKVKLAEHEltGHKVAVKILNRQKIKSLDMEekirrEIQILKLFRHPHIIRLYEVIETPtdIFMVMEYVS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSL--YNVLHGAeplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG--------- 177
Cdd:cd14079  86 GGELfdYIVQKGR-----LSEDEARRFFQQIISGVEYCHR---HMVVHRDLKPENLLLDSNMNV-KIADFGlsnimrdge 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 ---TACdiqthmtnnkGSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDEIGGPA-FR-IMWAVHngtrpPL 251
Cdd:cd14079 157 flkTSC----------GSPNYAAPEVISGKLYAgPEVDVWSCGVILYALLCGSLPFDDEHIPNlFKkIKSGIY-----TI 221
                       250       260
                ....*....|....*....|....*....
gi 21735562 252 IKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14079 222 PSHLSPGARDLIKRMLVVDPLKRITIPEI 250
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
42-282 4.81e-23

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 100.11  E-value: 4.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNevVAIKKMsysgkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLkdHTAWLVMEYCLGSAS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAcDIQTHMTNNKGS 192
Cdd:cd06633 109 DLLEVHKKPLQEVEIAAITHGALQ---GLAYLHS---HNMIHRDIKAGNILLTEPGQV-KLADFGSA-SIASPANSFVGT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVF----EGsNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKN-LPKPIESLMTRCW 267
Cdd:cd06633 181 PYWMAPEVIlamdEG-QYDGKVDIWSLGITCIELAERKPPLFNMN--AMSALYHIAQNDSPTLQSNeWTDSFRGFVDYCL 257
                       250
                ....*....|....*
gi 21735562 268 SKDPSQRPSMEEIVK 282
Cdd:cd06633 258 QKIPQERPSSAELLR 272
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
52-284 4.88e-23

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 98.71  E-value: 4.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  52 KAKWRAKDVAIK--QIESESERKA--FIVELRQLSRVNHPNIVKLYGACLNPVCLVM--EYAEGGSLYNVLHGAEPLpYY 125
Cdd:cd14057  13 KGRWQGNDIVAKilKVRDVTTRISrdFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVisQYMPYGSLYNVLHEGTGV-VV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 126 TAAHAMSWCLQCSQGVAYLHSMQPkaLIHRDLKPPNLLLVAGGTVLKICDFGTACDIQthmtnNKG---SAAWMAPEVFE 202
Cdd:cd14057  92 DQSQAVKFALDIARGMAFLHTLEP--LIPRHHLNSKHVMIDEDMTARINMADVKFSFQ-----EPGkmyNPAWMAPEALQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 203 GSNYS---EKCDVFSWGIILWEVITRRKPFD-----EIGgpafriMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQR 274
Cdd:cd14057 165 KKPEDinrRSADMWSFAILLWELVTREVPFAdlsnmEIG------MKIALEGLRVTIPPGISPHMCKLMKICMNEDPGKR 238
                       250
                ....*....|
gi 21735562 275 PSMEEIVKIM 284
Cdd:cd14057 239 PKFDMIVPIL 248
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
33-289 5.23e-23

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 99.26  E-value: 5.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVE--EVVGRGAFGVVCKAKWRAKD------VAIKQIESESERKAFIV---ELRQLSRVNHPNIVKLYGACLNP-V 100
Cdd:cd05111   4 FKETELRklKVLGSGVFGTVHKGIWIPEGdsikipVAIKVIQDRSGRQSFQAvtdHMLAIGSLDHAYIVRLLGICPGAsL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNvlHGAEPLPYYTAAHAMSWCLQCSQGVAYLhsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTAC 180
Cdd:cd05111  84 QLVTQLLPLGSLLD--HVRQHRGSLGPQLLLNWCVQIAKGMYYL---EEHRMVHRNLAARNVLLKSPSQV-QVADFGVAD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -----DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRimwAVHNGTRPPLIKN- 254
Cdd:cd05111 158 llypdDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMT-------FGAEPYA---GMRLAEVPDLLEKg 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 255 --LPKP------IESLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd05111 228 erLAQPqictidVYMVMVKCWMIDENIRPTFKELANEFTRMAR 270
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-282 5.53e-23

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 99.42  E-value: 5.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKA-------KWRAKDVAIKQIESES----ERKAFIVELrqlsrVNHPNIVKLYGACLNPVC- 101
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCvqkstgqEFAAKIINTKKLSARDhqklEREARICRL-----LKHPNIVRLHDSISEEGFh 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 -LVMEYAEGGSLYNVLHGAEplpYYTAAHAmSWCL-QCSQGVAYLHSMqpkALIHRDLKPPNLLLV--AGGTVLKICDFG 177
Cdd:cd14086  76 yLVFDLVTGGELFEDIVARE---FYSEADA-SHCIqQILESVNHCHQN---GIVHRDLKPENLLLAskSKGAAVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDI---QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFR-IMWAVHNGTRP--- 249
Cdd:cd14086 149 LAIEVqgdQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFwDEDQHRLYAqIKAGAYDYPSPewd 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21735562 250 ---PLIKNLpkpIESLMTRcwskDPSQRPSMEEIVK 282
Cdd:cd14086 229 tvtPEAKDL---INQMLTV----NPAKRITAAEALK 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
37-231 6.76e-23

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 98.37  E-value: 6.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESESE-RKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd14087   4 DIKALIGRGSFSRVVRVEHRVtrQPYAIKMIETKCRgREVCESELNVLRRVRHTNIIQLIEVfeTKERVYMVMELATGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVLK--ICDFGTACDIQTH---- 185
Cdd:cd14087  84 LFDRIIAKGSFTERDATRVLQMVLD---GVKYLHGL---GITHRDLKPENLLYYHPGPDSKimITDFGLASTRKKGpncl 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd14087 158 MKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDD 203
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
29-282 6.99e-23

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 98.62  E-value: 6.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  29 EEIDYKEIeVEEVVGRGAFGVVCKA--KWRAKDVAIKQIE----SESERKAF------IVELRQLSRVNHPNIVKLYGAC 96
Cdd:cd14084   2 KELRKKYI-MSRTLGSGACGEVKLAydKSTCKKVAIKIINkrkfTIGSRREInkprniETEIEILKKLSHPCIIKIEDFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 LNP--VCLVMEYAEGGSLYN----VLHGAEPLPYYTAahamswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV--AGG 168
Cdd:cd14084  81 DAEddYYIVLELMEGGELFDrvvsNKRLKEAICKLYF-------YQMLLAVKYLHS---NGIIHRDLKPENVLLSsqEEE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 169 TVLKICDFGTACDIQ--THMTNNKGSAAWMAPEV--FEGSN-YSEKCDVFSWGIILWEVITRRKPFDE-----------I 232
Cdd:cd14084 151 CLIKITDFGLSKILGetSLMKTLCGTPTYLAPEVlrSFGTEgYTRAVDCWSLGVILFICLSGYPPFSEeytqmslkeqiL 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 233 GGpafRIMWAvhngtrPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14084 231 SG---KYTFI------PKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
37-281 8.08e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 98.12  E-value: 8.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFG---VVCKAKWRAKdVAIKQI-------ESESERKAFIVelrqLSRVNHPNIVK----------LYgac 96
Cdd:cd08219   3 NVLRVVGEGSFGralLVQHVNSDQK-YAMKEIrlpksssAVEDSRKEAVL----LAKMKHPNIVAfkesfeadghLY--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 lnpvcLVMEYAEGGSLYNVLHgAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDF 176
Cdd:cd08219  75 -----IVMEYCDGGDLMQKIK-LQRGKLFPEDTILQWFVQMCLGVQHIHE---KRVLHRDIKSKNIFLTQNGKV-KLGDF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDIQTHMT---NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTRPPLIK 253
Cdd:cd08219 145 GSARLLTSPGAyacTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQ--ANSWKNLILKVCQGSYKPLPS 222
                       250       260
                ....*....|....*....|....*...
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd08219 223 HYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
34-282 9.91e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 98.19  E-value: 9.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAK--WRAKDVAIKQIESESERKAFIV--ELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARnvNTGELAAIKVIKLEPGEDFAVVqqEIIMMKDCKHSNIVAYFGSYLrrDKLWICMEFC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHAmswCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMT 187
Cdd:cd06645  91 GGGSLQDIYHVTGPLSESQIAYV---SRETLQGLYYLHS---KGKMHRDIKGANILLTDNGHV-KLADFGVSAQITATIA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNK---GSAAWMAPEVF---EGSNYSEKCDVFSWGIILWEVITRRKPFDEIgGPAFRIMWAVHNGTRPPLIKNLPK---P 258
Cdd:cd06645 164 KRKsfiGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMFDL-HPMRALFLMTKSNFQPPKLKDKMKwsnS 242
                       250       260
                ....*....|....*....|....
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06645 243 FHHFVKMALTKNPKKRPTAEKLLQ 266
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
40-282 1.09e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 98.23  E-value: 1.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQI-------ESESERKAFIVELRQLSRVNHPNIVKLYGaCL-----NPVCLVME 105
Cdd:cd06651  13 KLLGQGAFGRVylCYDVDTGRELAAKQVqfdpespETSKEVSALECEIQLLKNLQHERIVQYYG-CLrdraeKTLTIFME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG------TA 179
Cdd:cd06651  92 YMPGGSVKDQLKAYGAL---TESVTRKYTRQILEGMSYLHS---NMIVHRDIKGANILRDSAGNV-KLGDFGaskrlqTI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKPI 259
Cdd:cd06651 165 CMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMA-AIFKIATQPTNPQLPSHISEHA 243
                       250       260
                ....*....|....*....|...
gi 21735562 260 ESLMtRCWSKDPSQRPSMEEIVK 282
Cdd:cd06651 244 RDFL-GCIFVEARHRPSAEELLR 265
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
40-284 1.12e-22

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 99.98  E-value: 1.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKW-------RAKDVAIKQIESE---SERKAFIVELRQLSRV-NHPNIVKLYGACL--NPVCLVMEY 106
Cdd:cd05104  41 KTLGAGAFGKVVEATAyglakadSAMTVAVKMLKPSahsTEREALMSELKVLSYLgNHINIVNLLGACTvgGPTLVITEY 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 -------------------------AEGGSLYNVLHGAEP------------------LP------------YYTAAHA- 130
Cdd:cd05104 121 ccygdllnflrrkrdsficpkfedlAEAALYRNLLHQREMacdslneymdmkpsvsyvVPtkadkrrgvrsgSYVDQDVt 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 131 ----------------MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGgTVLKICDFGTACDIQTHmTNN--KGS 192
Cdd:cd05104 201 seileedelaldtedlLSFSYQVAKGMEFLAS---KNCIHRDLAARNILLTHG-RITKICDFGLARDIRND-SNYvvKGN 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 A----AWMAPEVFEGSNYSEKCDVFSWGIILWEVIT------RRKPFDEiggpAFRIMwaVHNGTRPPLIKNLPKPIESL 262
Cdd:cd05104 276 ArlpvKWMAPESIFECVYTFESDVWSYGILLWEIFSlgsspyPGMPVDS----KFYKM--IKEGYRMDSPEFAPSEMYDI 349
                       330       340
                ....*....|....*....|..
gi 21735562 263 MTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd05104 350 MRSCWDADPLKRPTFKQIVQLI 371
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
42-274 1.43e-22

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 97.93  E-value: 1.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGACL------NPVCLVMEYAEGGSLYN 114
Cdd:cd14144   3 VGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFReTEIYQTVLMRHENILGFIAADIkgtgswTQLYLITDYHENGSLYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEplpyYTAAHAMSWCLQCSQGVAYLHS----MQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTAC-------DI 182
Cdd:cd14144  83 FLRGNT----LDTQSMLKLAYSAACGLAHLHTeifgTQGKpAIAHRDIKSKNILVKKNGTCC-IADLGLAVkfisetnEV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSE------KCDVFSWGIILWEvITRR-----------KPFDEI--GGPAFRIMWAV 243
Cdd:cd14144 158 DLPPNTRVGTKRYMAPEVLDESLNRNhfdaykMADMYSFGLVLWE-IARRcisggiveeyqLPYYDAvpSDPSYEDMRRV 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21735562 244 --HNGTRPPlIKN------LPKPIESLMTRCWSKDPSQR 274
Cdd:cd14144 237 vcVERRRPS-IPNrwssdeVLRTMSKLMSECWAHNPAAR 274
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
28-280 1.52e-22

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 98.04  E-value: 1.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  28 FEEIDYKEIEVeevVGRGAFGVVCKAKW------RAKDVAIKQIESES--ERKAFIVELRQLSRVNHPNIVKLYGACLNP 99
Cdd:cd05081   1 FEERHLKYISQ---LGKGNFGSVELCRYdplgdnTGALVAVKQLQHSGpdQQRDFQREIQILKALHSDFIVKYRGVSYGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 ----VCLVMEYAEGGSLYNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICD 175
Cdd:cd05081  78 grrsLRLVMEYLPSGCLRDFLQRHRAR--LDASRLLLYSSQICKGMEYLGSRR---CVHRDLAARNIL-VESEAHVKIAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTA----CDIQTHMTNNKGSAA--WMAPEVFEGSNYSEKCDVFSWGIILWEVIT----RRKPFDE---IGGP------A 236
Cdd:cd05081 152 FGLAkllpLDKDYYVVREPGQSPifWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkSCSPSAEflrMMGCerdvpaL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 237 FRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05081 232 CRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSAL 275
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
42-229 2.16e-22

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 97.68  E-value: 2.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQIESE---SERKAFIVELRQLSRVNHPNIVKlygAC---------LNPV-CLVMEY 106
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGekIAIKSCRLElsvKNKDRWCHEIQIMKKLNHPNVVK---ACdvpeemnflVNDVpLLAMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLL--VAGGTVLKICDFGTACDIQ- 183
Cdd:cd14039  78 CSGGDLRKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENK---IIHRDLKPENIVLqeINGKIVHKIIDLGYAKDLDq 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 184 -THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14039 155 gSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
42-282 2.26e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 97.79  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNV 115
Cdd:cd06657  28 IGEGSTGIVCIATVKSsgKLVAVKKMDlrKQQRRELLFNEVVIMRDYQHENVVEMYNSYLvgDELWVVMEFLEGGALTDI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK---GS 192
Cdd:cd06657 108 VTHTR----MNEEQIAAVCLAVLKALSVLHA---QGVIHRDIKSDSILLTHDGRV-KLSDFGFCAQVSKEVPRRKslvGT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNGTrPPLIKNLPK---PIESLMTRCWSK 269
Cdd:cd06657 180 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY--FNEPPLKAMKMIRDNL-PPKLKNLHKvspSLKGFLDRLLVR 256
                       250
                ....*....|...
gi 21735562 270 DPSQRPSMEEIVK 282
Cdd:cd06657 257 DPAQRATAAELLK 269
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
41-290 3.03e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 100.09  E-value: 3.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   41 VVGR----GAFgVVCKAKWRAKDVAIKQIESESERKAFIV--ELRQLSRVNHPNIVKLYG--ACLNPVCLVMEYAEGGSL 112
Cdd:PTZ00267  74 LVGRnpttAAF-VATRGSDPKEKVVAKFVMLNDERQAAYArsELHCLAACDHFGIVKHFDdfKSDDKLLLIMEYGSGGDL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  113 YNVLHG--AEPLPY--YTAAhamswcLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGtVLKICDFG--------TAC 180
Cdd:PTZ00267 153 NKQIKQrlKEHLPFqeYEVG------LLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTG-IIKLGDFGfskqysdsVSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  181 DIQTHMTnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeigGPAFR-IMWAVHNGTRPPLIKNLPKPI 259
Cdd:PTZ00267 226 DVASSFC---GTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFK---GPSQReIMQQVLYGKYDPFPCPVSSGM 299
                        250       260       270
                 ....*....|....*....|....*....|.
gi 21735562  260 ESLMTRCWSKDPSQRPSMEEIVKimTHLMRY 290
Cdd:PTZ00267 300 KALLDPLLSKNPALRPTTQQLLH--TEFLKY 328
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
42-282 3.11e-22

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 96.92  E-value: 3.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKD----VAIKQIESESeRKAFIVELRQ----LSRVNHPNIVKLYGACL----NPVCLVMEYA 107
Cdd:cd05079  12 LGEGHFGKVelCRYDPEGDNtgeqVAVKSLKPES-GGNHIADLKKeieiLRNLYHENIVKYKGICTedggNGIKLIMEFL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLynvlhgAEPLPYYTA----AHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd05079  91 PSGSL------KEYLPRNKNkinlKQQLKYAVQICKGMDYLGSRQ---YVHRDLAARNVLVESEHQV-KIGDFGLTKAIE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 TH-----MTNNKGSAA-WMAPEVFEGSNYSEKCDVFSWGIILWEVIT----RRKP---FDEIGGPAF------RIMWAVH 244
Cdd:cd05079 161 TDkeyytVKDDLDSPVfWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsESSPmtlFLKMIGPTHgqmtvtRLVRVLE 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 245 NGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05079 241 EGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIE 278
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
35-301 3.39e-22

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 96.96  E-value: 3.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAkDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHG-EVAIRLLEidgnNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPphLAIITSFCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlkICD---FGTACDIQTH 185
Cdd:cd14152  80 GRTLYSFVR--DPKTSLDINKTRQIAQEIIKGMGYLHA---KGIVHKDLKSKNVFYDNGKVV--ITDfglFGISGVVQEG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNN--KGSAAW---MAPEVFE----GSN-----YSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNG---TR 248
Cdd:cd14152 153 RRENelKLPHDWlcyLAPEIVRemtpGKDedclpFSKAADVYAFGTIWYELQARDWPL--KNQPAEALIWQIGSGegmKQ 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 249 PPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLmryfPGADEPLQYP 301
Cdd:cd14152 231 VLTTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL----PKLNRRLSHP 279
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
28-280 3.40e-22

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 97.01  E-value: 3.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  28 FEEidyKEIEVEEVVGRGAFGVVCKAKW------RAKDVAIKQIESESER--KAFIVELRQLSRVNHPNIVKLYGACL-- 97
Cdd:cd14205   1 FEE---RHLKFLQQLGKGNFGSVEMCRYdplqdnTGEVVAVKKLQHSTEEhlRDFEREIEILKSLQHDNIVKYKGVCYsa 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 --NPVCLVMEYAEGGSLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICD 175
Cdd:cd14205  78 grRNLRLIMEYLPYGSLRDYLQKHKE--RIDHIKLLQYTSQICKGMEYLGT---KRYIHRDLATRNIL-VENENRVKIGD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTA----CDIQTHMTNNKGSAA--WMAPEVFEGSNYSEKCDVFSWGIILWEVIT----RRKP---FDEIGGP------- 235
Cdd:cd14205 152 FGLTkvlpQDKEYYKVKEPGESPifWYAPESLTESKFSVASDVWSFGVVLYELFTyiekSKSPpaeFMRMIGNdkqgqmi 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21735562 236 AFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14205 232 VFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
31-292 3.60e-22

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 97.03  E-value: 3.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVV----CKAKWRAKD---VAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NP 99
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVflaeCYNLCPEQDkilVAVKTLKdaSDNARKDFHREAELLTNLQHEHIVKFYGVCVegDP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVL--HG--------AEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGT 169
Cdd:cd05093  82 LIMVFEYMKHGDLNKFLraHGpdavlmaeGNRPAELTQSQMLHIAQQIAAGMVYLASQH---FVHRDLATRNCL-VGENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 170 VLKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAV 243
Cdd:cd05093 158 LVKIGDFGMSRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNN--EVIECI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 21735562 244 HNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFP 292
Cdd:cd05093 236 TQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASP 284
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
37-280 3.94e-22

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 95.99  E-value: 3.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGV--VCKAKWRAKDVAIKQIES----ESERKAFIVELRQLsrvNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14662   3 ELVKDIGSGNFGVarLMRNKETKELVAVKYIERglkiDENVQREIINHRSL---RHPNIIRFKEVVLTPthLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLvaGGTV---LKICDFGTACDIQTH 185
Cdd:cd14662  80 GGELFERICNAG---RFSEDEARYFFQQLISGVSYCHSMQ---ICHRDLKLENTLL--DGSPaprLKICDFGYSKSSVLH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 mTNNK---GSAAWMAPEVFEGSNYSEK-CDVFSWGIILWEVITRRKPFDEIGGPA-FR--------IMWAVHNGTRppli 252
Cdd:cd14662 152 -SQPKstvGTPAYIAPEVLSRKEYDGKvADVWSCGVTLYVMLVGAYPFEDPDDPKnFRktiqrimsVQYKIPDYVR---- 226
                       250       260
                ....*....|....*....|....*...
gi 21735562 253 knLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14662 227 --VSQDCRHLLSRIFVANPAKRITIPEI 252
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
32-282 4.45e-22

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 96.63  E-value: 4.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEevVGRGAFGVVCKAKWRAKDV--AIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd06643   5 DFWEIVGE--LGDGAFGKVYKAQNKETGIlaAAKVIDtkSEEELEDYMVEIDILASCDHPNIVKLLDAFYyeNNLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAE-PLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFG-TACDIQ 183
Cdd:cd06643  83 FCAGGAVDAVMLELErPL---TEPQIRVVCKQTLEALVYLHENK---IIHRDLKAGNILFTLDGDI-KLADFGvSAKNTR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNNK--GSAAWMAPEVF--EGSN---YSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNgTRPPlikNLP 256
Cdd:cd06643 156 TLQRRDSfiGTPYWMAPEVVmcETSKdrpYDYKADVWSLGVTLIEMAQIEPPHHELN--PMRVLLKIAK-SEPP---TLA 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 257 KP------IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06643 230 QPsrwspeFKDFLRKCLEKNVDARWTTSQLLQ 261
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
63-280 4.96e-22

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 95.50  E-value: 4.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  63 KQIeSESERkafivELRQLSRVNHPNIVKLYGACLNP--------VCLVMEYAEGGSLYNVLHGAEPLPYYTAAHamsWC 134
Cdd:cd14012  40 KQI-QLLEK-----ELESLKKLRHPNLVSYLAFSIERrgrsdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARR---WT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 135 LQCSQGVAYLHSmqpKALIHRDLKPPNLLLVA--GGTVLKICDFG---TACDI--QTHMTNNKgSAAWMAPEVFEGSN-Y 206
Cdd:cd14012 111 LQLLEALEYLHR---NGVVHKSLHAGNVLLDRdaGTGIVKLTDYSlgkTLLDMcsRGSLDEFK-QTYWLPPELAQGSKsP 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 207 SEKCDVFSWGIILWEVITRRKPFDEIGGPafrimwavhNGTRPPLikNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14012 187 TRKTDVWDLGLLFLQMLFGLDVLEKYTSP---------NPVLVSL--DLSASLQDFLSKCLSLDPKKRPTALEL 249
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
61-281 5.77e-22

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 96.31  E-value: 5.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  61 AIKQIESE---SERKAFIVELRQ----LSRVNHPNIVKLYGACLNP---VCLVMEYAeGGSLYNVLH-----GAEPLPyy 125
Cdd:cd14001  32 AVKKINSKcdkGQRSLYQERLKEeakiLKSLNHPNIVGFRAFTKSEdgsLCLAMEYG-GKSLNDLIEeryeaGLGPFP-- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 126 tAAHAMSWCLQCSQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNK-------GSAAWMAP 198
Cdd:cd14001 109 -AATILKVALSIARALEYLH--NEKKILHGDIKSGNVLIKGDFESVKLCDFGVSLPLTENLEVDSdpkaqyvGTEPWKAK 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 199 EV-FEGSNYSEKCDVFSWGIILWEVITRRKP---------------FDEiggpAFRIMWAVHN--GTRPP-----LIKNL 255
Cdd:cd14001 186 EAlEEGGVITDKADIFAYGLVLWEMMTLSVPhlnlldiedddedesFDE----DEEDEEAYYGtlGTRPAlnlgeLDDSY 261
                       250       260
                ....*....|....*....|....*.
gi 21735562 256 PKPIEsLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14001 262 QKVIE-LFYACTQEDPKDRPSAAHIV 286
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
42-280 6.27e-22

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 95.62  E-value: 6.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVcKAKWRAK---DVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLY---GACLNPVCLVMEYAEGG 110
Cdd:cd14165   9 LGEGSYAKV-KSAYSERlkcNVAIKIIDKKKAPDDFVEkflprELEILARLNHKSIIKTYeifETSDGKVYIVMELGVQG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEPLPYYTaAHAMSWclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFG----TACDIQTHM 186
Cdd:cd14165  88 DLLEFIKLRGALPEDV-ARKMFH--QLSSAIKYCHELD---IVHRDLKCENLLLDKDFNI-KLTDFGfskrCLRDENGRI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNK---GSAAWMAPEVFEGSNYSEKC-DVFSWGIILWEVITRRKPFDEiggPAFRIMWAVHNGTRP--PLIKNLPKPIE 260
Cdd:cd14165 161 VLSKtfcGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDD---SNVKKMLKIQKEHRVrfPRSKNLTSECK 237
                       250       260
                ....*....|....*....|
gi 21735562 261 SLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14165 238 DLIYRLLQPDVSQRLCIDEV 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
42-280 6.31e-22

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 95.44  E-value: 6.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGV--VCKAKWRAKDVAIKQIES----ESERKAFIVELRQLsrvNHPNIVKLYGACLNP--VCLVMEYAEGGSLY 113
Cdd:cd14665   8 IGSGNFGVarLMRDKQTKELVAVKYIERgekiDENVQREIINHRSL---RHPNIVRFKEVILTPthLAIVMEYAAGGELF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLvAGGTV--LKICDFG--TACDIQTHMTNN 189
Cdd:cd14665  85 ERICNAG---RFSEDEARFFFQQLISGVSYCHSMQ---ICHRDLKLENTLL-DGSPAprLKICDFGysKSSVLHSQPKST 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEK-CDVFSWGIILWEVITRRKPFDEIGGPA------FRIMWAVHngTRPPLIKNLPKpIESL 262
Cdd:cd14665 158 VGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEPRnfrktiQRILSVQY--SIPDYVHISPE-CRHL 234
                       250
                ....*....|....*...
gi 21735562 263 MTRCWSKDPSQRPSMEEI 280
Cdd:cd14665 235 ISRIFVADPATRITIPEI 252
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
37-276 6.82e-22

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 95.41  E-value: 6.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESeseRKAF----IVELRQLSRVN------HPNIVKLYGACL--NPVCL 102
Cdd:cd14133   2 EVLEVLGKGTFGQVVKCYDLLtgEEVALKIIKN---NKDYldqsLDEIRLLELLNkkdkadKYHIVRLKDVFYfkNHLCI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAeGGSLYNvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTV-LKICDFGTACD 181
Cdd:cd14133  79 VFELL-SQNLYE-FLKQNKFQYLSLPRIRKIAQQILEALVFLHSL---GLIHCDLKPENILLASYSRCqIKIIDFGSSCF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE-------------IGGPAFRIMWAvHNGTR 248
Cdd:cd14133 154 LTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGasevdqlariigtIGIPPAHMLDQ-GKADD 232
                       250       260
                ....*....|....*....|....*...
gi 21735562 249 PPLIKnlpkpiesLMTRCWSKDPSQRPS 276
Cdd:cd14133 233 ELFVD--------FLKKLLEIDPKERPT 252
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
50-284 6.86e-22

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 95.70  E-value: 6.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  50 VCKAKWRAKDVAIKQIE------SESERKafivELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLYNVLHGAE- 120
Cdd:cd14045  23 TQTGIYDGRTVAIKKIAkksftlSKRIRK----EVKQVRELDHPNLCKFIGGCIEvpNVAIITEYCPKGSLNDVLLNEDi 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 121 PLPYytaAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGS------AA 194
Cdd:cd14045  99 PLNW---GFRFSFATDIARGMAYLHQHK---IYHGRLKSSNCV-IDDRWVCKIADYGLTTYRKEDGSENASGyqqrlmQV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 195 WMAPEvFEGSNYSEKC---DVFSWGIILWEVITRRKPFDEIGGPafrimwaVHNGTRPPLIK--------NLPKPIE--S 261
Cdd:cd14045 172 YLPPE-NHSNTDTEPTqatDVYSYAIILLEIATRNDPVPEDDYS-------LDEAWCPPLPElisgktenSCPCPADyvE 243
                       250       260
                ....*....|....*....|...
gi 21735562 262 LMTRCWSKDPSQRPSMEEIVKIM 284
Cdd:cd14045 244 LIRRCRKNNPAQRPTFEQIKKTL 266
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
42-282 7.29e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 96.26  E-value: 7.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQIE--SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNV 115
Cdd:cd06658  30 IGEGSTGIVCIAteKHTGKQVAVKKMDlrKQQRRELLFNEVVIMRDYHHENVVDMYNSYLvgDELWVVMEFLEGGALTDI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK---GS 192
Cdd:cd06658 110 VTHTR----MNEEQIATVCLSVLRALSYLHN---QGVIHRDIKSDSILLTSDGRI-KLSDFGFCAQVSKEVPKRKslvGT 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNgTRPPLIKNLPK---PIESLMTRCWSK 269
Cdd:cd06658 182 PYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY--FNEPPLQAMRRIRD-NLPPRVKDSHKvssVLRGFLDLMLVR 258
                       250
                ....*....|...
gi 21735562 270 DPSQRPSMEEIVK 282
Cdd:cd06658 259 EPSQRATAQELLQ 271
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
40-282 7.51e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 96.33  E-value: 7.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQ--IESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLY 113
Cdd:cd06654  26 EKIGQGASGTVYTAMDVAtgQEVAIRQmnLQQQPKKELIINEILVMRENKNPNIVNYLDSYLvgDELWVVMEYLAGGSLT 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAeplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDI---QTHMTNNK 190
Cdd:cd06654 106 DVVTET----CMDEGQIAAVCRECLQALEFLHSNQ---VIHRDIKSDNILLGMDGSV-KLTDFGFCAQItpeQSKRSTMV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNGTRPPL--IKNLPKPIESLMTRCWS 268
Cdd:cd06654 178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLE 255
                       250
                ....*....|....
gi 21735562 269 KDPSQRPSMEEIVK 282
Cdd:cd06654 256 MDVEKRGSAKELLQ 269
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
42-291 7.54e-22

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 95.41  E-value: 7.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGAC-----LNpvcLVMEYAEGGSL 112
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKElirfDEETQRTFLKEVKVMRCLEHPNVLKFIGVLykdkrLN---FITEYIKGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLkICDFGTA------CDIQTHM 186
Cdd:cd14221  78 RGIIKSMDS--HYPWSQRVSFAKDIASGMAYLHSMN---IIHRDLNSHNCLVRENKSVV-VADFGLArlmvdeKTQPEGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNK-----------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK------PFDEIGGPAFRIMWAVHNgtrP 249
Cdd:cd14221 152 RSLKkpdrkkrytvvGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNadpdylPRTMDFGLNVRGFLDRYC---P 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 250 PlikNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYF 291
Cdd:cd14221 229 P---NCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL 267
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
37-231 8.43e-22

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 95.13  E-value: 8.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLNPVC--LVMEYAEG 109
Cdd:cd14083   6 EFKEVLGTGAFSEVVLAEDKAtgKLVAIKCIDKKAlkgKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHlyLVMELVTG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYN--VLHGAeplpyYT---AAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLV--AGGTVLKICDFG-TACD 181
Cdd:cd14083  86 GELFDriVEKGS-----YTekdASHLIR---QVLEAVDYLHS---LGIVHRDLKPENLLYYspDEDSKIMISDFGlSKME 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 182 IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DE 231
Cdd:cd14083 155 DSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFyDE 205
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
40-281 1.03e-21

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 94.76  E-value: 1.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVE-------------LRQLSRVNHPNIVKLYGACLNPVC--L 102
Cdd:cd14004   6 KEMGEGAYGQVnlAIYKSKGKEVVIKFIFKERILVDTWVRdrklgtvpleihiLDTLNKRSHPNIVKLLDFFEDDEFyyL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VME-YAEGGSLYNVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAcd 181
Cdd:cd14004  86 VMEkHGSGMDLFDFI---ERKPNMDEKEAKYIFRQVADAVKHLHD---QGIVHRDIKDENVILDGNGTI-KLIDFGSA-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 iqTHMTNNK-----GSAAWMAPEVFEGSNYSEK-CDVFSWGIILWEVITRRKPF---DEIGGPAFRIMWAVHngtrppli 252
Cdd:cd14004 157 --AYIKSGPfdtfvGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFyniEEILEADLRIPYAVS-------- 226
                       250       260
                ....*....|....*....|....*....
gi 21735562 253 knlpKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14004 227 ----EDLIDLISRMLNRDVGDRPTIEELL 251
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
40-282 1.05e-21

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 95.94  E-value: 1.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQ--IESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLY 113
Cdd:cd06656  25 EKIGQGASGTVYTAIDIAtgQEVAIKQmnLQQQPKKELIINEILVMRENKNPNIVNYLDSYLvgDELWVVMEYLAGGSLT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAeplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDI---QTHMTNNK 190
Cdd:cd06656 105 DVVTET----CMDEGQIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLGMDGSV-KLTDFGFCAQItpeQSKRSTMV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGPAFRIMWAVHNGTRPPL--IKNLPKPIESLMTRCWS 268
Cdd:cd06656 177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLE 254
                       250
                ....*....|....
gi 21735562 269 KDPSQRPSMEEIVK 282
Cdd:cd06656 255 MDVDRRGSAKELLQ 268
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
40-297 1.06e-21

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 96.60  E-value: 1.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKA--KWRAKDVAIKQIeSESERKAF----IVELRQLSRVNHPNIVKLYG-------ACLNPVCLVMEY 106
Cdd:cd07849  11 SYIGEGAYGMVCSAvhKPTGQKVAIKKI-SPFEHQTYclrtLREIKILLRFKHENIIGILDiqrpptfESFKDVYIVQEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGgSLYNVLHgAEPLPYytaAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKICDFGTA-CDIQTH 185
Cdd:cd07849  90 MET-DLYKLIK-TQHLSN---DHIQYFLYQILRGLKYIHSAN---VLHRDLKPSNLLLNTNCD-LKICDFGLArIADPEH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 -----MTNNKGSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF-------------DEIGGPAFRIMWAVHNG 246
Cdd:cd07849 161 dhtgfLTEYVATRWYRAPEIMLNSKgYTKAIDIWSVGCILAEMLSNRPLFpgkdylhqlnlilGILGTPSQEDLNCIISL 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 247 TRPPLIKNLP----KPIESLMTRCWSK-----------DPSQRPSMEEivkIMTH--LMRYFPGADEP 297
Cdd:cd07849 241 KARNYIKSLPfkpkVPWNKLFPNADPKaldlldkmltfNPHKRITVEE---ALAHpyLEQYHDPSDEP 305
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
35-285 1.39e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 94.88  E-value: 1.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRA---KDVAIKQI--------ESESERKAFIVELrqLSRVN-------HPNIVKLYGAC 96
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSngqTLLALKEInmtnpafgRTEQERDKSVGDI--ISEVNiikeqlrHPNIVRYYKTF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 L--NPVCLVMEYAEG---GSLYNVLHgaEPLPYYTAAHAMSWCLQCSQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVL 171
Cdd:cd08528  79 LenDRLYIVMELIEGaplGEHFSSLK--EKNEHFTEDRIWNIFVQMVLALRYLH--KEKQIVHRDLKPNNIMLGEDDKVT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 172 kICDFGTACDIQ---THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIMWAVHNg 246
Cdd:cd08528 155 -ITDFGLAKQKGpesSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFysTNMLTLATKIVEAEYE- 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 247 trpPLIKNL-PKPIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd08528 233 ---PLPEGMySDDITFVIRSCLTPDPEARPDIVEVSSMIS 269
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
40-288 1.40e-21

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 94.91  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD-----VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACLN---------PVc 101
Cdd:cd05035   5 KILGEGEFGSVMEAQLKQDDgsqlkVAVKTMKvdihTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTasdlnkppsPM- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVL------HGAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkICD 175
Cdd:cd05035  84 VILPFMKHGDLHSYLlysrlgGLPEKLPLQTLLKFM---VDIAKGMEYLSN---RNFIHRDLAARNCMLDENMTVC-VAD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTACDI-------QTHMTnnKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIGGPafRIMWAVHNGT 247
Cdd:cd05035 157 FGLSRKIysgdyyrQGRIS--KMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRgQTPYPGVENH--EIYDYLRNGN 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21735562 248 RPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05035 233 RLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
61-281 1.44e-21

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 95.06  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  61 AIKQI---ESESERKAfIVELRQLSRVNHPNIVKLYGACLNP-------VCLVMEYAEGGSLYNVL-----HGaEPLPyy 125
Cdd:cd13986  29 ALKKIlchSKEDVKEA-MREIENYRLFNHPNILRLLDSQIVKeaggkkeVYLLLPYYKRGSLQDEIerrlvKG-TFFP-- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 126 tAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLkICDFGTACDIQTHMTNNK------------GSA 193
Cdd:cd13986 105 -EDRILHIFLGICRGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPI-LMDLGSMNPARIEIEGRRealalqdwaaehCTM 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 194 AWMAPEVFE---GSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNG-TRPPLIKNLPKPIESLMTRCWSK 269
Cdd:cd13986 183 PYRAPELFDvksHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLALAVLSGnYSFPDNSRYSEELHQLVKSMLVV 262
                       250
                ....*....|..
gi 21735562 270 DPSQRPSMEEIV 281
Cdd:cd13986 263 NPAERPSIDDLL 274
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-276 1.85e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 94.88  E-value: 1.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  23 SQVLN-FEEIDYkeieveevVGRGAFGVVCKA--KWRAKDVAIKQI--ESESERKAFIV--ELRQLSRVNHPNIVKLYGA 95
Cdd:cd14049   2 SRYLNeFEEIAR--------LGKGGYGKVYKVrnKLDGQYYAIKKIliKKVTKRDCMKVlrEVKVLAGLQHPNIVGYHTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  96 CLNPVCLV----MEYAEGgSLYNVL-----HGAE------PLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPP 160
Cdd:cd14049  74 WMEHVQLMlyiqMQLCEL-SLWDWIvernkRPCEeefksaPYTPVDVDVTTKILQQLLEGVTYIHSM---GIVHRDLKPR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 161 NLLLVAGGTVLKICDFGTACDIQ---------------THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVItr 225
Cdd:cd14049 150 NIFLHGSDIHVRIGDFGLACPDIlqdgndsttmsrlngLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF-- 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 226 rKPFdEIGGPAFRIMWAVHNGTRP-PLIKNLPKPIESLMTRCwSKDPSQRPS 276
Cdd:cd14049 228 -QPF-GTEMERAEVLTQLRNGQIPkSLCKRWPVQAKYIKLLT-STEPSERPS 276
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
37-282 2.04e-21

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 94.69  E-value: 2.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIK------QIESESERKAFIveLRQLSrvNHPNIVKLYGACL-------NPVC 101
Cdd:cd06638  21 EIIETIGKGTYGKVFKVlnKKNGSKAAVKildpihDIDEEIEAEYNI--LKALS--DHPNVVKFYGMYYkkdvkngDQLW 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHG--------AEPLPYYTAAHAMswclqcsQGVAYLHSMQPkalIHRDLKPPNLLLVAGGTVlKI 173
Cdd:cd06638  97 LVLELCNGGSVTDLVKGflkrgermEEPIIAYILHEAL-------MGLQHLHVNKT---IHRDVKGNNILLTTEGGV-KL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDI-QTHMTNNK--GSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPFDEIggpafRIMWAVHN 245
Cdd:cd06638 166 VDFGVSAQLtSTRLRRNTsvGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADL-----HPMRALFK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 246 GTR-PPLIKNLPK----PIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06638 241 IPRnPPPTLHQPElwsnEFNDFIRKCLTKDYEKRPTVSDLLQ 282
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
40-292 2.14e-21

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 94.30  E-value: 2.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD----VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACL---------NPVcL 102
Cdd:cd05075   6 KTLGEGEFGSVMEGQLNQDDsvlkVAVKTMKiaicTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLqntesegypSPV-V 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLH----GAEP--LPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkICDF 176
Cdd:cd05075  85 ILPFMKHGDLHSFLLysrlGDCPvyLPTQMLVKFMT---DIASGMEYLSS---KNFIHRDLAARNCMLNENMNVC-VADF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMWAVHNGTRpp 250
Cdd:cd05075 158 GLSKKIYNGDYYRQGRISkmpvkWIAIESLADRVYTTKSDVWSFGVTMWEIATRgQTPYP--GVENSEIYDYLRQGNR-- 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 251 liknLPKPIE------SLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFP 292
Cdd:cd05075 234 ----LKQPPDcldglyELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
37-280 2.18e-21

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 93.87  E-value: 2.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA-KDVAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14161   6 EFLETLGKGTYGRVKKARDSSgRLVAIKsirkdRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSskIVIVMEYAS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT--HM 186
Cdd:cd14161  86 RGDLYDYISERQRLSELEARHFFR---QIVSAVHYCHA---NGIVHRDLKLENILLDANGNI-KIADFGLSNLYNQdkFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDeigGPAFRIMWA-VHNGT-RPPliknlPKPIESLM 263
Cdd:cd14161 159 QTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFD---GHDYKILVKqISSGAyREP-----TKPSDACG 230
                       250
                ....*....|....*....
gi 21735562 264 TRCW--SKDPSQRPSMEEI 280
Cdd:cd14161 231 LIRWllMVNPERRATLEDV 249
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
30-229 2.22e-21

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 95.52  E-value: 2.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVvGRGAFGVVCKAKWRA--KDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGaCLNPVC-- 101
Cdd:cd07858   2 EVDTKYVPIKPI-GRGAYGIVCSAKNSEtnEKVAIKKIanafDNRIDAKRTLREIKLLRHLDHENVIAIKD-IMPPPHre 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 ------LVMEYAEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAgGTVLKICD 175
Cdd:cd07858  80 afndvyIVYELMDT-DLHQIIRSSQTL---SDDHCQYFLYQLLRGLKYIHSAN---VLHRDLKPSNLLLNA-NCDLKICD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 176 FG---TACDIQTHMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07858 152 FGlarTTSEKGDFMTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIFAELLGRKPLF 209
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
40-287 3.09e-21

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 94.05  E-value: 3.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGA------CLNPVCLVMEYAEGGSL 112
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFReAEIYQTVMLRHENILGFIAAdnkdngTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLhGAEPLPYYTAAHAmswCLQCSQGVAYLH----SMQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTAC------- 180
Cdd:cd14143  81 FDYL-NRYTVTVEGMIKL---ALSIASGLAHLHmeivGTQGKpAIAHRDLKSKNILVKKNGTCC-IADLGLAVrhdsatd 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSNY-----SEKC-DVFSWGIILWEvITRR-----------KPFDEI--GGPAFRIMW 241
Cdd:cd14143 156 TIDIAPNHRVGTKRYMAPEVLDDTINmkhfeSFKRaDIYALGLVFWE-IARRcsiggihedyqLPYYDLvpSDPSIEEMR 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 242 AV--HNGTRPPlIKNLPKPIESL------MTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14143 235 KVvcEQKLRPN-IPNRWQSCEALrvmakiMRECWYANGAARLTALRIKKTLSQL 287
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
37-229 3.11e-21

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 94.66  E-value: 3.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA----KDVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYGACLNP----VCLV 103
Cdd:cd07842   3 EIEGCIGRGTYGRVYKAKRKNgkdgKEYAIKKFKGDKEQYTGISqsacrEIALLRELKHENVVSLVEVFLEHadksVYLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGgSLYNVLH-----GAEPLPYYTAAHAMsWclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGT---VLKICD 175
Cdd:cd07842  83 FDYAEH-DLWQIIKfhrqaKRVSIPPSMVKSLL-W--QILNGIHYLHS---NWVLHRDLKPANILVMGEGPergVVKIGD 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 176 FGTA--CD--IQTHMTNNKGSAA-WM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07842 156 LGLArlFNapLKPLADLDPVVVTiWYrAPELLLGArHYTKAIDIWAIGCIFAELLTLEPIF 216
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
41-288 3.71e-21

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 95.86  E-value: 3.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKW----RAK---DVAIKQIE---SESERKAFIVELRQLSRVN-HPNIVKLYGACLN--PVCLVMEYA 107
Cdd:cd05105  44 ILGSGAFGKVVEGTAyglsRSQpvmKVAVKMLKptaRSSEKQALMSELKIMTHLGpHLNIVNLLGACTKsgPIYIITEYC 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLH---------------------GAEPLPYYTAAHA------------------------------------ 130
Cdd:cd05105 124 FYGDLVNYLHknrdnflsrhpekpkkdldifGINPADESTRSYVilsfenkgdymdmkqadttqyvpmleikeaskysdi 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 131 ------------------------------------MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLvAGGTVLKIC 174
Cdd:cd05105 204 qrsnydrpasykgsndsevknllsddgseglttldlLSFTYQVARGMEFLAS---KNCVHRDLAARNVLL-AQGKIVKIC 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 175 DFGTACDIQtHMTN--NKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITrrkpfdeIGGPAFRIMWA------ 242
Cdd:cd05105 280 DFGLARDIM-HDSNyvSKGSTflpvKWMAPESIFDNLYTTLSDVWSYGILLWEIFS-------LGGTPYPGMIVdstfyn 351
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 243 -VHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05105 352 kIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
32-286 3.74e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 94.74  E-value: 3.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEEV--VGRGAFGVVCKAKWRAKD--VAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLN--PVCL 102
Cdd:cd06650   1 ELKDDDFEKIseLGAGNGGVVFKVSHKPSGlvMARKLIHLEIKpaiRNQIIRELQVLHECNSPYIVGFYGAFYSdgEISI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYTAAHAmswCLQCSQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI 182
Cdd:cd06650  81 CMEHMDGGSLDQVLKKAGRIPEQILGKV---SIAVIKGLTYLR--EKHKIMHRDVKPSNILVNSRGEI-KLCDFGVSGQL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-----------------------DEIGGPAFR 238
Cdd:cd06650 155 IDSMANSfVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakelelmfgcqvegdaaetPPRPRTPGR 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 239 IMWAVHNGTRPPL--------IKNLPKP----------IESLMTRCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd06650 235 PLSSYGMDSRPPMaifelldyIVNEPPPklpsgvfsleFQDFVNKCLIKNPAERADLKQ---LMVH 297
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
27-229 3.76e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 93.72  E-value: 3.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  27 NFEEIdykeieveEVVGRGAFGVVCKAKWR--AKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGAC--LN 98
Cdd:cd07860   1 NFQKV--------EKIGEGTYGVVYKARNKltGEVVALKKIrldtETEGVPSTAIREISLLKELNHPNIVKLLDVIhtEN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 PVCLVMEYAEGgSLYNVLHGAePLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd07860  73 KLYLVFEFLHQ-DLKKFMDAS-ALTGIPLPLIKSYLFQLLQGLAFCHSHR---VLHRDLKPQNLLINTEGAI-KLADFGL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 179 A----CDIQTHmTNNKGSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07860 147 ArafgVPVRTY-THEVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALF 201
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
37-290 3.88e-21

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 93.32  E-value: 3.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVEL-----RQLSRvnHPNIVKLYGACLN---------PV 100
Cdd:cd13975   3 KLGRELGRGQYGVVyaCDSWGGHFPCALKSVVPPDDKHWNDLALefhytRSLPK--HERIVSLHGSVIDysygggssiAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGgSLYNVLHGAEPLPyytaaHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaC 180
Cdd:cd13975  81 LLIMERLHR-DLYTGIKAGLSLE-----ERLQIALDVVEGIRFLHS---QGLVHRDIKLKNVLLDKKNRA-KITDLGF-C 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQTHMTNN-KGSAAWMAPEVFEGsNYSEKCDVFSWGIILWEVITRRKPFDEiggpAFR------IMW-AVHNGTRPPLI 252
Cdd:cd13975 150 KPEAMMSGSiVGTPIHMAPELFSG-KYDNSVDVYAFGILFWYLCAGHVKLPE----AFEqcaskdHLWnNVRKGVRPERL 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRY 290
Cdd:cd13975 225 PVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMDR 262
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
35-287 3.96e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 93.55  E-value: 3.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAK--WRAKDVAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATclLDRKPVALKKVQifemmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIedNELNIVLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYN-VLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT 184
Cdd:cd08228  83 LADAGDLSQmIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHS---RRVMHRDIKPANVFITATGVV-KLGDLGLGRFFSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIK-NLPKPIE 260
Cdd:cd08228 159 KTTAAHslvGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPTeHYSEKLR 238
                       250       260
                ....*....|....*....|....*..
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd08228 239 ELVSMCIYPDPDQRPDIGYVHQIAKQM 265
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
42-281 5.95e-21

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 93.25  E-value: 5.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE------SESERKAFIVELRQLSRVNHPNIVKLYGA---------ClnpVCLVMEY 106
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCElqdrklTKAEQQRFKEEAEMLKGLQHPNIVRFYDSwesvlkgkkC---IVLVTEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHM 186
Cdd:cd14031  95 MTSGTLKTYL---KRFKVMKPKVLRSWCRQILKGLQFLHTRTP-PIIHRDLKCDNIFITGPTGSVKIGDLGLATLMRTSF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNK-GSAAWMAPEVFEgSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKP-IESLMT 264
Cdd:cd14031 171 AKSViGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRKVTSGIKPASFNKVTDPeVKEIIE 248
                       250
                ....*....|....*..
gi 21735562 265 RCWSKDPSQRPSMEEIV 281
Cdd:cd14031 249 GCIRQNKSERLSIKDLL 265
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
43-229 6.13e-21

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 92.33  E-value: 6.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYNVLh 117
Cdd:cd14006   2 GRGRFGVVkrCIEKATGREFAAKFIPKRDKKKEAVLrEISILNQLQHPRIIQLHEAYESPteLVLILELCSGGELLDRL- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 gAEPLPYyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTV-LKICDFGTACDI--QTHMTNNKGSAA 194
Cdd:cd14006  81 -AERGSL-SEEEVRTYMRQLLEGLQYLHNHH---ILHLDLKPENILLADRPSPqIKIIDFGLARKLnpGEELKEIFGTPE 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21735562 195 WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14006 156 FVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPF 190
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
42-284 6.15e-21

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 93.96  E-value: 6.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK--WRAKDVAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd06635  33 IGHGSFGAVYFARdvRTSEVVAIKKMsysgkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLreHTAWLVMEYCLGSAS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAcDIQTHMTNNKGS 192
Cdd:cd06635 113 DLLEVHKKPLQEIEIAAITHGALQ---GLAYLHS---HNMIHRDIKAGNILLTEPGQV-KLADFGSA-SIASPANSFVGT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEV---FEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKN-LPKPIESLMTRCWS 268
Cdd:cd06635 185 PYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMN--AMSALYHIAQNESPTLQSNeWSDYFRNFVDSCLQ 262
                       250
                ....*....|....*.
gi 21735562 269 KDPSQRPSMEEIVKIM 284
Cdd:cd06635 263 KIPQDRPTSEELLKHM 278
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
33-229 8.78e-21

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 92.86  E-value: 8.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEieVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESE---SERKAFI-VELRQLSRvNHPNIVKL--YGACLNPVCLVM 104
Cdd:cd14090   3 YKL--TGELLGEGAYASVqtCINLYTGKEYAVKIIEKHpghSRSRVFReVETLHQCQ-GHPNILQLieYFEDDERFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDFGTACDI 182
Cdd:cd14090  80 EKMRGGPL---LSHIEKRVHFTEQEASLVVRDIASALDFLHD---KGIAHRDLKPENILCESMDKVspVKICDFDLGSGI 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21735562 183 QTHMTNNK-----------GSAAWMAPEV-----FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14090 154 KLSSTSMTpvttpelltpvGSAEYMAPEVvdafvGEALSYDKRCDLWSLGVILYIMLCGYPPF 216
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
40-274 9.26e-21

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 92.83  E-value: 9.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD------VAIKqIESESERKAFIVELRQLS--RVNHPNIVKLYGACLNPV------CLVME 105
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQNAsgqyetVAVK-IFPYEEYASWKNEKDIFTdaSLKHENILQFLTAEERGVgldrqyWLITA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNvlhgaeplpyYTAAHAMSW---CLQCS---QGVAYLHS-----MQPKALI-HRDLKPPNLLLVAGGTVLkI 173
Cdd:cd14055  80 YHENGSLQD----------YLTRHILSWedlCKMAGslaRGLAHLHSdrtpcGRPKIPIaHRDLKSSNILVKNDGTCV-L 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTAC--DIQT---HMTNNK--GSAAWMAPEVFEGS-NYSE-----KCDVFSWGIILWEVITR----------RKPF- 229
Cdd:cd14055 149 ADFGLALrlDPSLsvdELANSGqvGTARYMAPEALESRvNLEDlesfkQIDVYSMALVLWEMASRceasgevkpyELPFg 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21735562 230 DEIGG-PAFRIM----------------WAVHNGTRppliknlpkPIESLMTRCWSKDPSQR 274
Cdd:cd14055 229 SKVRErPCVESMkdlvlrdrgrpeipdsWLTHQGMC---------VLCDTITECWDHDPEAR 281
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
37-229 1.07e-20

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 93.45  E-value: 1.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGACLNPVCL-- 102
Cdd:cd05599   4 EPLKVIGRGAFGEVrlVRKKDTGHVYAMKKL-----RKSEMLEKEQvahvraerdiLAEADNPWVVKLYYSFQDEENLyl 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLP-----YYTAahamswclQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:cd05599  79 IMEFLPGGDMMTLLMKKDTLTeeetrFYIA--------ETVLAIESIHKL---GYIHRDIKPDNLLLDARGHI-KLSDFG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 178 --TACDIqTHMT-NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05599 147 lcTGLKK-SHLAySTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPF 200
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
37-229 1.15e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 92.02  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESER-KAFIVE--LRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14184   4 KIGKVIGDGNFAVVkeCVERSTGKEFALKIIDKAKCCgKEHLIEneVSILRRVKHPNIIMLIEEMDTPaeLYLVMELVKG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPlpyYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVA---GGTVLKICDFGTACDIQTHM 186
Cdd:cd14184  84 GDLFDAITSSTK---YTERDASAMVYNLASALKYLHGL---CIVHRDIKPENLLVCEypdGTKSLKLGDFGLATVVEGPL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14184 158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF 200
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
41-276 1.39e-20

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 92.29  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKD-----VAIK----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLN-------PVCLV- 103
Cdd:cd05074  16 MLGKGEFGSVREAQLKSEDgsfqkVAVKmlkaDIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRsrakgrlPIPMVi 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLH----GAEP--LPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkICDFG 177
Cdd:cd05074  96 LPFMKHGDLHTFLLmsriGEEPftLPLQTLVRFM---IDIASGMEYLSS---KNFIHRDLAARNCMLNENMTVC-VADFG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEI-GGPAFRIMWAVHNGTRPP 250
Cdd:cd05074 169 LSKKIYSGDYYRQGCASklpvkWLALESLADNVYTTHSDVWAFGVTMWEIMTRgQTPYAGVeNSEIYNYLIKGNRLKQPP 248
                       250       260
                ....*....|....*....|....*.
gi 21735562 251 likNLPKPIESLMTRCWSKDPSQRPS 276
Cdd:cd05074 249 ---DCLEDVYELMCQCWSPEPKCRPS 271
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-240 1.50e-20

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 93.21  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  20 EAPSQVLNFEEIDYKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQI-------ESESerkAFIVELRQ-LSRVNHPNI 89
Cdd:cd05596  12 EKPVNEITKLRMNAEDFDVIKVIGRGAFGEVqlVRHKSTKKVYAMKLLskfemikRSDS---AFFWEERDiMAHANSEWI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  90 VKLYGACLNP--VCLVMEYAEGGSLYNVLHGAEplpyYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAG 167
Cdd:cd05596  89 VQLHYAFQDDkyLYMVMDYMPGGDLVNLMSNYD----VPEKWARFYTAEVVLALDAIHSM---GFVHRDVKPDNMLLDAS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 168 GTvLKICDFGTaC-----DIQTHMTNNKGSAAWMAPEVFEGSN----YSEKCDVFSWGIILWEVITRRKPF--DEIGGPA 236
Cdd:cd05596 162 GH-LKLADFGT-CmkmdkDGLVRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFyaDSLVGTY 239

                ....
gi 21735562 237 FRIM 240
Cdd:cd05596 240 GKIM 243
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
30-282 1.57e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 92.44  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKDV--AIKQI---ESESERKAFIVELRQLSRVNH-PNIVKLYGACLN--PVC 101
Cdd:cd06618  11 KADLNDLENLGEIGSGTCGQVYKMRHKKTGHvmAVKQMrrsGNKEENKRILMDLDVVLKSHDcPYIVKCYGYFITdsDVF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEG--GSLYNVLHGaePLPYYTAAHaMSWCLqcsqgVAYLHSMQPK-ALIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd06618  91 ICMELMSTclDKLLKRIQG--PIPEDILGK-MTVSI-----VKALHYLKEKhGVIHRDVKPSNILLDESGNV-KLCDFGI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 A---CDIQTHmTNNKGSAAWMAPEVFE---GSNYSEKCDVFSWGIILWEVITRRKPFDEIGGpAFRIMWAVHNGTRP--P 250
Cdd:cd06618 162 SgrlVDSKAK-TRSAGCAAYMAPERIDppdNPKYDIRADVWSLGISLVELATGQFPYRNCKT-EFEVLTKILNEEPPslP 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 251 LIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06618 240 PNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQ 271
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
42-229 1.59e-20

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 91.13  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIK--QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLYN- 114
Cdd:cd14103   1 LGRGKFGTVYRCVEKAtgKELAAKfiKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPreMVLVMEYVAGGELFEr 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVA-GGTVLKICDFGTAcdiQTHMTNNK--- 190
Cdd:cd14103  81 VVDDDFELTERDCILFMR---QICEGVQYMHKQG---ILHLDLKPENILCVSrTGNQIKIIDFGLA---RKYDPDKKlkv 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21735562 191 --GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14103 152 lfGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPF 192
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
42-236 2.00e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 91.95  E-value: 2.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR--AKDVAIKQIESESERKAF-------IVELRQLSRVNHPNIVKLYGACLN-------PVCLVME 105
Cdd:cd07863   8 IGVGAYGTVYKARDPhsGHFVALKSVRVQTNEDGLplstvreVALLKRLEAFDHPNIVRLMDVCATsrtdretKVTLVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGgSLYNVLHGAEP--LPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd07863  88 HVDQ-DLRTYLDKVPPpgLPAETIKDLMR---QFLRGLDFLHA---NCIVHRDLKPENILVTSGGQV-KLADFGLARIYS 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 184 THM--TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVItRRKP--------------FDEIGGPA 236
Cdd:cd07863 160 CQMalTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF-RRKPlfcgnseadqlgkiFDLIGLPP 227
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
35-282 2.01e-20

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 91.93  E-value: 2.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESE----SErkafivELRQLSRV-NHPNIVKLYGACL--NPVCLVME 105
Cdd:cd14091   1 EYEIKEEIGKGSYSVCkrCIHKATGKEYAVKIIDKSkrdpSE------EIEILLRYgQHPNIITLRDVYDdgNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLV-AGGT--VLKICDFGTAcdi 182
Cdd:cd14091  75 LLRGGELLDRILRQKFFSEREASAVM---KTLTKTVEYLHSQG---VVHRDLKPSNILYAdESGDpeSLRICDFGFA--- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 qTHMTNNKG-------SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGP---AFRIMWAVHNGtRPPLI 252
Cdd:cd14091 146 -KQLRAENGllmtpcyTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF--ASGPndtPEVILARIGSG-KIDLS 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 253 ----KNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14091 222 ggnwDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQ 255
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
42-229 2.02e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 91.43  E-value: 2.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA-------KDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSL 112
Cdd:cd05577   1 LGRGGFGEVCACQVKAtgkmyacKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKdkLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 -YNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI--QTHMTNN 189
Cdd:cd05577  81 kYHIYNVGTRG--FSEARAIFYAAEIICGLEHLHN---RFIVYRDLKPENILLDDHGHV-RISDLGLAVEFkgGKKIKGR 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21735562 190 KGSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05577 155 VGTHGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPF 195
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
34-287 2.11e-20

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 92.12  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGACLNP------VCLVMEY 106
Cdd:cd14142   5 RQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFReTEIYNTVLLRHENILGFIASDMTSrnsctqLWLITHY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEplpyyTAAHAMSW-CLQCSQGVAYLHS----MQPKALI-HRDLKPPNLLLVAGGTVLkICDFGTAC 180
Cdd:cd14142  85 HENGSLYDYLQRTT-----LDHQEMLRlALSAASGLVHLHTeifgTQGKPAIaHRDLKSKNILVKSNGQCC-IADLGLAV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -----DIQTHMTNNK--GSAAWMAPEVFEGS-NYS-----EKCDVFSWGIILWEVITR----------RKPFDEIGG--P 235
Cdd:cd14142 159 thsqeTNQLDVGNNPrvGTKRYMAPEVLDETiNTDcfesyKRVDIYAFGLVLWEVARRcvsggiveeyKPPFYDVVPsdP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21735562 236 AFRIMW--AVHNGTRP---------PLIKNLPKpiesLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14142 239 SFEDMRkvVCVDQQRPnipnrwssdPTLTAMAK----LMKECWYQNPSARLTALRIKKTLLKI 297
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
42-229 3.68e-20

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 91.18  E-value: 3.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVckAKWRAKD----VAIKQIESE---SERKAFIVELRQLSRVNHPNIV----------KLYGACLnPVcLVM 104
Cdd:cd14038   2 LGTGGFGNV--LRWINQEtgeqVAIKQCRQElspKNRERWCLEIQIMKRLNHPNVVaardvpeglqKLAPNDL-PL-LAM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVL--KICDFGTA--C 180
Cdd:cd14038  78 EYCQGGDLRKYLNQFENCCGLREGAILTLLSDISSALRYLHENR---IIHRDLKPENIVLQQGEQRLihKIIDLGYAkeL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21735562 181 DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14038 155 DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
30-297 4.25e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 90.89  E-value: 4.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKDV--AIKQIES---ESERKAFIVELRQLSRVNH-PNIVKLYGACLNP-VCL 102
Cdd:cd06616   2 EFTAEDLKDLGEIGRGAFGTVNKMLHKPSGTimAVKRIRStvdEKEQKRLLMDLDVVMRSSDcPYIVKFYGALFREgDCW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 V-MEYAEGG--SLYNVLHGAEP--LPYYTAAH-AMSwclqcsqGVAYLHSMQPK-ALIHRDLKPPNLLLVAGGTVlKICD 175
Cdd:cd06616  82 IcMELMDISldKFYKYVYEVLDsvIPEEILGKiAVA-------TVKALNYLKEElKIIHRDVKPSNILLDRNGNI-KLCD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTACDIQTHM--TNNKGSAAWMAPEVFEGSN----YSEKCDVFSWGIILWEVITRRKPFDEIgGPAFRIMWAVHNGTrP 249
Cdd:cd06616 154 FGISGQLVDSIakTRDAGCRPYMAPERIDPSAsrdgYDVRSDVWSLGITLYEVATGKFPYPKW-NSVFDQLTQVVKGD-P 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 250 PLIKNLPK-----PIESLMTRCWSKDPSQRPSMEEIVKimTHLMRYFPGADEP 297
Cdd:cd06616 232 PILSNSEErefspSFVNFVNLCLIKDESKRPKYKELLK--HPFIKMYEERNVD 282
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
42-288 4.96e-20

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 92.38  E-value: 4.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA-------KWRAKDVAIKQIES---ESERKAFIVELRQLSRVN-HPNIVKLYGACLN--PVCLVMEYAE 108
Cdd:cd05107  45 LGSGAFGRVVEAtahglshSQSTMKVAVKMLKStarSSEKQALMSELKIMSHLGpHLNIVNLLGACTKggPIYIITEYCR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLH----------------------GA----------------------------------------------- 119
Cdd:cd05107 125 YGDLVDYLHrnkhtflqyyldknrddgslisGGstplsqrkshvslgsesdggymdmskdesadyvpmqdmkgtvkyadi 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLPYYTA--------------------AHAMSW------CLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKI 173
Cdd:cd05107 205 ESSNYESPydqylpsapertrrdtlineSPALSYmdlvgfSYQVANGMEFLAS---KNCVHRDLAARNVLICEGKLV-KI 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTACDIQtHMTN--NKGSA----AWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDEIggPAFRIMW-AVHN 245
Cdd:cd05107 281 CDFGLARDIM-RDSNyiSKGSTflplKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLgGTPYPEL--PMNEQFYnAIKR 357
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 21735562 246 GTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLM 288
Cdd:cd05107 358 GYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
40-239 5.86e-20

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 90.43  E-value: 5.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAF----IVELRQLSRVNHPNIVKLY-----GACLNpvcLVMEYAE 108
Cdd:cd07835   5 EKIGEGTYGVVYKARDKLtgEIVALKKIRLETEDEGVpstaIREISLLKELNHPNIVRLLdvvhsENKLY---LVFEFLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GgSLYNVLHGAePLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTA------CDI 182
Cdd:cd07835  82 L-DLKKYMDSS-PLTGLDPPLIKSYLYQLLQGIAFCHSHR---VLHRDLKPQNLLIDTEG-ALKLADFGLArafgvpVRT 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 183 QTH--MTnnkgsaAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF------DEIggpaFRI 239
Cdd:cd07835 156 YTHevVT------LWYrAPEILLGSkHYSTPVDIWSVGCIFAEMVTRRPLFpgdseiDQL----FRI 212
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
42-276 8.65e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 90.09  E-value: 8.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA---KWRAKDVAIKQIESESERKAF-------IVELRQLSRVNHPNIVKLYGACL-------NPVCLVM 104
Cdd:cd07862   9 IGEGAYGKVFKArdlKNGGRFVALKRVRVQTGEEGMplstireVAVLRHLETFEHPNVVRLFDVCTvsrtdreTKLTLVF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEP-LPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTA--CD 181
Cdd:cd07862  89 EHVDQDLTTYLDKVPEPgVPTETIKDMM---FQLLRGLDFLHSHR---VVHRDLKPQNILVTSSGQI-KLADFGLAriYS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVItRRKP--------------FDEIGGPAFRiMWAVHNG- 246
Cdd:cd07862 162 FQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF-RRKPlfrgssdvdqlgkiLDVIGLPGEE-DWPRDVAl 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21735562 247 ------TRP--PLIKNLPKPIE---SLMTRCWSKDPSQRPS 276
Cdd:cd07862 240 prqafhSKSaqPIEKFVTDIDElgkDLLLKCLTFNPAKRIS 280
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
32-229 8.91e-20

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 89.20  E-value: 8.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIV--ELRQLSRVNHPNIVKLYGA--CLNPVCLVME 105
Cdd:cd14193   2 SYYNVNKEEILGGGRFGQVhkCEEKSSGLKLAAKIIKARSQKEKEEVknEIEVMNQLNHANLIQLYDAfeSRNDIVLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYN-VLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGT-VLKICDFGTACDIQ 183
Cdd:cd14193  82 YVDGGELFDrIIDENYNL---TELDTILFIKQICEGIQYMHQMY---ILHLDLKPENILCVSREAnQVKIIDFGLARRYK 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 184 TH--MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14193 156 PRekLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
42-282 1.10e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 88.91  E-value: 1.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIESEsERKAFIVELRqlSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNVLH 117
Cdd:cd13995  12 IPRGAFGKVYLAQDTKtkKRMACKLIPVE-QFKPSDVEIQ--ACFRHENIAELYGALLweETVHLFMEAGEGGSVLEKLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 GAEPLPYYTaahaMSWCLQ-CSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkiCDFGtacdIQTHMTNN------- 189
Cdd:cd13995  89 SCGPMREFE----IIWVTKhVLKGLDFLHS---KNIIHHDIKPSNIVFMSTKAVL--VDFG----LSVQMTEDvyvpkdl 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP----FDEIGGPAFriMWAVHNGTrPPLiKNLPKPIESLMTR 265
Cdd:cd13995 156 RGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPwvrrYPRSAYPSY--LYIIHKQA-PPL-EDIAQDCSPAMRE 231
                       250       260
                ....*....|....*....|.
gi 21735562 266 ----CWSKDPSQRPSMEEIVK 282
Cdd:cd13995 232 lleaALERNPNHRSSAAELLK 252
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
34-230 1.37e-19

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 88.76  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKW--RAKDVAIKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYGAC--LNPVCLVM 104
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSlhTGLEVAIKMIDKKAMQKAGMVqrvrnEVEIHCQLKHPSILELYNYFedSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVL-HGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAcdIQ 183
Cdd:cd14186  81 EMCHNGEMSRYLkNRKKPFTEDEARHFMH---QIVTGMLYLHS---HGILHRDLTLSNLLLTRNMNI-KIADFGLA--TQ 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 184 THMTNNK-----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd14186 152 LKMPHEKhftmcGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD 203
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
29-280 1.50e-19

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 89.31  E-value: 1.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  29 EEIDYKEIEVEEVVGRGAFGVVCKAKW-------RAKDVAIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACL- 97
Cdd:cd05091   1 KEINLSAVRFMEELGEDRFGKVYKGHLfgtapgeQTQAVAIKTLKDKAEgplREEFRHEAMLRSRLQHPNIVCLLGVVTk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 -NPVCLVMEYAEGGSLYNVLHGAEP-------------LPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLL 163
Cdd:cd05091  81 eQPMSMIFSYCSHGDLHEFLVMRSPhsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHH---VVHKDLATRNVL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 164 LVAGGTVlKICDFGT-----ACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeIGGPAF 237
Cdd:cd05091 158 VFDKLNV-KISDLGLfrevyAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYgLQPY--CGYSNQ 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 238 RIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05091 235 DVIEMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
35-282 1.86e-19

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 88.38  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKD--VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVME 105
Cdd:cd14117   7 DFDIGRPLGKGKFGNVYLAREKQSKfiVALKvlfksQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRkrIYLILE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTAcdIQTH 185
Cdd:cd14117  87 YAPRGELYKELQKHGRFDEQRTATFME---ELADALHYCHE---KKVIHRDIKPENLLMGYKGE-LKIADFGWS--VHAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiggpafrimwAVHNGTRPPLIK-------NL 255
Cdd:cd14117 158 SLRRRtmcGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFES----------ASHTETYRRIVKvdlkfppFL 227
                       250       260
                ....*....|....*....|....*..
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14117 228 SDGSRDLISKLLRYHPSERLPLKGVME 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
35-229 2.00e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 89.49  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   35 EIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIeseseRKAFIVELRQ----------LSRVNHPNIVKLYGACL--NPV 100
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVriAKHKGTGEYYAIKCL-----KKREILKMKQvqhvaqeksiLMELSHPFIVNMMCSFQdeNRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  101 CLVMEYAEGGSLYNVLHGAEPLPYYTAAHamsWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTAC 180
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKAGRFPNDVAKF---YHAELVLAFEYLHS---KDIIYRDLKPENLLLDNKGHV-KVTDFGFAK 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 21735562  181 DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PTZ00263 167 KVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
34-282 2.02e-19

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 88.16  E-value: 2.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEI-EVEEVVGRGAFG--VVCKAKWRAKDVAIKQIES---ESERKAFIVELRQLSRVNHPNIVKLYG--ACLNPVCLVME 105
Cdd:cd14167   2 RDIyDFREVLGTGAFSevVLAEEKRTQKLVAIKCIAKkalEGKETSIENEIAVLHKIKHPNIVALDDiyESGGHLYLIMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYN--VLHGaeplpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVA--GGTVLKICDFGTAC- 180
Cdd:cd14167  82 LVSGGELFDriVEKG-----FYTERDASKLIFQILDAVKYLHDM---GIVHRDLKPENLLYYSldEDSKIMISDFGLSKi 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -DIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:cd14167 154 eGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDAKLFEQILKAEYEFDSPYWDDISDS 233
                       250       260
                ....*....|....*....|....
gi 21735562 259 IESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14167 234 AKDFIQHLMEKDPEKRFTCEQALQ 257
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
39-280 2.24e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 89.28  E-value: 2.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVV--CKAKWRAKDVAIKQIeseSERKAFIVELRQLSRV-NHPNIVKLYGACLNP--VCLVMEYAEGGSLy 113
Cdd:cd14092  11 EEALGDGSFSVCrkCVHKKTGQEFAVKIV---SRRLDTSREVQLLRLCqGHPNIVKLHEVFQDElhTYLVMELLRGGEL- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 nvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGG--TVLKICDFGTAC---DIQTHMTN 188
Cdd:cd14092  87 --LERIRKKKRFTESEASRIMRQLVSAVSFMHS---KGVVHRDLKPENLLFTDEDddAEIKIVDFGFARlkpENQPLKTP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKgSAAWMAPEVFEGSN----YSEKCDVFSWGIILWEVITRRKPFDEIGG--PAFRIMWAVHNGT---RPPLIKNLPKPI 259
Cdd:cd14092 162 CF-TLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRneSAAEIMKRIKSGDfsfDGEEWKNVSSEA 240
                       250       260
                ....*....|....*....|.
gi 21735562 260 ESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14092 241 KSLIQGLLTVDPSKRLTMSEL 261
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
37-279 2.52e-19

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 88.41  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQIESESER-KAFIVE--LRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14169   6 ELKEKLGEGAFSEVVLAQERgsQRLVALKCIPKKALRgKEAMVEneIAVLRRINHENIVSLEDIYESPthLYLAMELVTG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVL--HGaeplpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAG--GTVLKICDFG-TACDIQT 184
Cdd:cd14169  86 GELFDRIieRG-----SYTEKDASQLIGQVLQAVKYLHQL---GIVHRDLKPENLLYATPfeDSKIMISDFGlSKIEAQG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLM 263
Cdd:cd14169 158 MLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFyDENDSELFNQILKAEYEFDSPYWDDISESAKDFI 237
                       250
                ....*....|....*.
gi 21735562 264 TRCWSKDPSQRPSMEE 279
Cdd:cd14169 238 RHLLERDPEKRFTCEQ 253
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
42-228 2.97e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 89.34  E-value: 2.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDV--AIKQIESESE---RKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSLYN 114
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLimARKLIHLEIKpaiRNQIIRELQVLHECNSPYIVGFYGAFYSdgEISICMEHMDGGSLDQ 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEPLPYYTAAHAMSWCLqcsQGVAYLHsmQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNN-KGSA 193
Cdd:cd06649  93 VLKEAKRIPEEILGKVSIAVL---RGLAYLR--EKHQIMHRDVKPSNILVNSRGEI-KLCDFGVSGQLIDSMANSfVGTR 166
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21735562 194 AWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKP 228
Cdd:cd06649 167 SYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
35-309 3.34e-19

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 89.80  E-value: 3.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVckakWRAKD------VAIKQIES-----ESERKAFiVELRQLSRVNHPNIVKL-------YGAC 96
Cdd:cd07853   1 DVEPDRPIGYGAFGVV----WSVTDprdgkrVALKKMPNvfqnlVSCKRVF-RELKMLCFFKHDNVLSAldilqppHIDP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 LNPVCLVMEYAEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDF 176
Cdd:cd07853  76 FEEIYVVTELMQS-DLHKIIVSPQPL---SSDHVKVFLYQILRGLKYLHSAG---ILHRDIKPGNLL-VNSNCVLKICDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTA----CDIQTHMTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF-------------DEIGGPAFR 238
Cdd:cd07853 148 GLArveePDESKHMTQEVVTQYYRAPEILMGSrHYTSAVDIWSVGCIFAELLGRRILFqaqspiqqldlitDLLGTPSLE 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 239 IMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSqrpsmEEIVKIMTHLMRYFP----GADEPLQYPcqYSDEGQ 309
Cdd:cd07853 228 AMRSACEGARAHILRGPHKPPSLPVLYTLSSQAT-----HEAVHLLCRMLVFDPdkriSAADALAHP--YLDEGR 295
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
42-281 3.58e-19

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 88.18  E-value: 3.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE------SESERKAFIVELRQLSRVNHPNIVKLYGACLNP------VCLVMEYAEG 109
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCElqdrklSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTvkgkkcIVLVTELMTS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTaahAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNN 189
Cdd:cd14030 113 GTLKTYLKRFKVMKIKV---LRSWCRQILKGLQFLHTRTP-PIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKS 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K-GSAAWMAPEVFEgSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKP-IESLMTRCW 267
Cdd:cd14030 189 ViGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRRVTSGVKPASFDKVAIPeVKEIIEGCI 266
                       250
                ....*....|....
gi 21735562 268 SKDPSQRPSMEEIV 281
Cdd:cd14030 267 RQNKDERYAIKDLL 280
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
42-230 3.72e-19

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 87.54  E-value: 3.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA--KDVAIKQIeseseRKAFIVELRQLSRV-----------NHPNIVKLYGACLNP--VCLVMEY 106
Cdd:cd05611   4 ISKGAFGSVYLAKKRStgDYFAIKVL-----KKSDMIAKNQVTNVkaeraimmiqgESPYVAKLYYSFQSKdyLYLVMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG--TACDIQT 184
Cdd:cd05611  79 LNGGDCASLIKTLGGLP---EDWAKQYIAEVVLGVEDLHQ---RGIIHRDIKPENLLIDQTGH-LKLTDFGlsRNGLEKR 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 185 HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd05611 152 HNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH 197
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
31-292 3.85e-19

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 88.07  E-value: 3.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  31 IDYKEIEVEEVVGRGAFGVVCKAKWRAKD-----VAIKQIE----SESERKAFIVELRQLSRVNHPNIVKLYGACL---- 97
Cdd:cd14204   4 IDRNLLSLGKVLGEGEFGSVMEGELQQPDgtnhkVAVKTMKldnfSQREIEEFLSEAACMKDFNHPNVIRLLGVCLevgs 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 ----NPVcLVMEYAEGGSLYNVL----HGAEP--LPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAG 167
Cdd:cd14204  84 qripKPM-VILPFMKYGDLHSFLlrsrLGSGPqhVPLQTLLKFM---IDIALGMEYLSSRN---FLHRDLAARNCMLRDD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 168 GTVLkICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFDeiGGPAFRIMW 241
Cdd:cd14204 157 MTVC-VADFGLSKKIYSGDYYRQGRIAkmpvkWIAVESLADRVYTVKSDVWAFGVTMWEIATRgMTPYP--GVQNHEIYD 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 242 AVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFP 292
Cdd:cd14204 234 YLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
37-224 3.86e-19

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 88.78  E-value: 3.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESE-RKAFIVELRQLSRVNH------PNIVKLYGACL--NPVCLVME 105
Cdd:cd14134  15 KILRLLGEGTFGKVleCWDRKRKRYVAVKIIRNVEKyREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDyrGHMCIVFE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 -YaeGGSLYNVL--HGAEPlpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAG--------------- 167
Cdd:cd14134  95 lL--GPSLYDFLkkNNYGP---FPLEHVQHIAKQLLEAVAFLHDLK---LTHTDLKPENILLVDSdyvkvynpkkkrqir 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 168 ---GTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14134 167 vpkSTDIKLIDFGSATFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYT 226
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
77-280 3.95e-19

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 87.80  E-value: 3.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  77 ELRQLSRVNHPNIVKLYGACLNPV----CLVMEYAEGGSLYNVLhGAEPLPYYTAAHAMSWCLQcsqGVAYLHSmqpKAL 152
Cdd:cd14118  64 EIAILKKLDHPNVVKLVEVLDDPNednlYMVFELVDKGAVMEVP-TDNPLSEETARSYFRDIVL---GIEYLHY---QKI 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 153 IHRDLKPPNLLLVAGGTVlKICDFGTACD---IQTHMTNNKGSAAWMAPEVFEGS--NYSEKC-DVFSWGIILWEVITRR 226
Cdd:cd14118 137 IHRDIKPSNLLLGDDGHV-KIADFGVSNEfegDDALLSSTAGTPAFMAPEALSESrkKFSGKAlDIWAMGVTLYCFVFGR 215
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 227 KPF-DEiggpafRIMwAVHNGTRPPLIKNLPKPI-----ESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14118 216 CPFeDD------HIL-GLHEKIKTDPVVFPDDPVvseqlKDLILRMLDKNPSERITLPEI 268
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
40-321 3.98e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 88.52  E-value: 3.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFG--VVCKAKWRAKDVAIKQIESE-----SERKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGG 110
Cdd:cd05595   1 KLLGKGTFGkvILVREKATGRYYAMKILRKEviiakDEVAHTVTESRVLQNTRHPFLTALKYAfqTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK 190
Cdd:cd05595  81 ELFFHLSRER---VFTEDRARFYGAEIVSALEYLHS---RDVVYRDIKLENLMLDKDGHI-KITDFGLCKEGITDGATMK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMwaVHNGTRPPliKNLPKPIESLMTRC 266
Cdd:cd05595 154 tfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDHERLFELI--LMEEIRFP--RTLSPEAKSLLAGL 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 267 WSKDPSQR--PSMEEIVKIMTHlmRYFPGA--DEPLQYPCQYSDEGQSNSATSTGSFMD 321
Cdd:cd05595 230 LKKDPKQRlgGGPSDAKEVMEH--RFFLSInwQDVVQKKLLPPFKPQVTSEVDTRYFDD 286
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
41-229 4.30e-19

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 88.04  E-value: 4.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAK-------WRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05607   9 VLGKGGFGEVCAVQvkntgqmYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAfeTKTHLCLVMSLMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L-YNVLHGAEP------LPYYTAahamswclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ- 183
Cdd:cd05607  89 LkYHIYNVGERgiemerVIFYSA--------QITCGILHLHSLK---IVYRDMKPENVLLDDNGNC-RLSDLGLAVEVKe 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 184 -THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05607 157 gKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF 203
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
37-229 4.38e-19

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 87.36  E-value: 4.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESER-KAFIV--ELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd14183   9 KVGRTIGDGNFAVVkeCVERSTGREYALKIINKSKCRgKEHMIqnEVSILRRVKHPNIVLLIEEmdMPTELYLVMELVKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPlpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVA---GGTVLKICDFGTACDIQTHM 186
Cdd:cd14183  89 GDLFDAITSTNK---YTERDASGMLYNLASAIKYLHSLN---IVHRDIKPENLLVYEhqdGSKSLKLGDFGLATVVDGPL 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14183 163 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF 205
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
35-281 4.44e-19

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 87.57  E-value: 4.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAK--WRAKDVAIKQIES--ESERKAFIVE---LRQLSrvNHPNIVKLYGAC----------L 97
Cdd:cd14036   1 KLRIKRVIAEGGFAFVYEAQdvGTGKEYALKRLLSneEEKNKAIIQEinfMKKLS--GHPNIVQFCSAAsigkeesdqgQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVCLVMEYAEGGsLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:cd14036  79 AEYLLLTELCKGQ-LVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSP-PIIHRDLKIENLLIGNQGQI-KLCDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIqTHMTNNKGSA----------------AWMAPEVFEG-SNY--SEKCDVFSWGIILWEVITRRKPFDEigGPAFR 238
Cdd:cd14036 156 SATTE-AHYPDYSWSAqkrslvedeitrnttpMYRTPEMIDLySNYpiGEKQDIWALGCILYLLCFRKHPFED--GAKLR 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 239 IMWAvhNGTRPPLIKNLpKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14036 233 IINA--KYTIPPNDTQY-TVFHDLIRSTLKVNPEERLSITEIV 272
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
39-229 4.58e-19

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 87.41  E-value: 4.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVVCKA--KWRAKDVAIKQIE----SESERKAFIVELRQLSRV-NHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14106  13 STPLGRGKFAVVRKCihKETGKEYAAKFLRkrrrGQDCRNEILHEIAVLELCkDCPRVVNLHEVYETRseLILILELAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVA----GGtvLKICDFGTACDIQT- 184
Cdd:cd14106  93 GELQTLLDEEECLTEADVRRLMR---QILEGVQYLHE---RNIVHLDLKPQNILLTSefplGD--IKLCDFGISRVIGEg 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 185 -HMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14106 165 eEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPF 210
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
33-229 4.74e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 87.32  E-value: 4.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIK--QIESESERKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEY 106
Cdd:cd14192   3 YYAVCPHEVLGGGRFGQVhkCTELSTGLTLAAKiiKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAfeSKTNLTLIMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLhgAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV-AGGTVLKICDFGTACDIQTH 185
Cdd:cd14192  83 VDGGELFDRI--TDESYQLTELDAILFTRQICEGVHYLHQ---HYILHLDLKPENILCVnSTGNQIKIIDFGLARRYKPR 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 186 --MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14192 158 ekLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPF 203
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
39-282 5.11e-19

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 87.33  E-value: 5.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFG-VVCKAKWRAKDVAIKQIESESerkaFIVELRQLSRV----NHPNIVK----------LYGA---ClnpV 100
Cdd:cd13982   6 PKVLGYGSEGtIVFRGTFDGRPVAVKRLLPEF----FDFADREVQLLresdEHPNVIRyfctekdrqfLYIAlelC---A 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclqcsqGVAYLHSMQpkaLIHRDLKPPNLLLV---AGGTV-LKICDF 176
Cdd:cd13982  79 ASLQDLVESPRESKLFLRPGLEPVRLLRQIAS-------GLAHLHSLN---IVHRDLKPQNILIStpnAHGNVrAMISDF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTA--CDIQTH----MTNNKGSAAWMAPEVFEGS---NYSEKCDVFSWGIILWEVITRRK-PFDE-------IGGPAFRI 239
Cdd:cd13982 149 GLCkkLDVGRSsfsrRSGVAGTSGWIAPEMLSGStkrRQTRAVDIFSLGCVFYYVLSGGShPFGDklereanILKGKYSL 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21735562 240 MWAVHNGTRPPLIKNLpkpIEslmtRCWSKDPSQRPSMEEIVK 282
Cdd:cd13982 229 DKLLSLGEHGPEAQDL---IE----RMIDFDPEKRPSAEEVLN 264
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
48-289 5.43e-19

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 87.08  E-value: 5.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  48 GVVCKAKWrakdVAIKQIESESE---RKAFIVELRQLSRVNHPNiVKLYGACL---NPVCLVMEYAEGGSLYNVLHGAEp 121
Cdd:cd14043  18 GVAYEGDW----VWLKKFPGGSHtelRPSTKNVFSKLRELRHEN-VNLFLGLFvdcGILAIVSEHCSRGSLEDLLRNDD- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 122 lpyytaaHAMSWCLQCS------QGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTH----MTNNKG 191
Cdd:cd14043  92 -------MKLDWMFKSSllldliKGMRYLHH---RGIVHGRLKSRNCV-VDGRFVLKITDYGYNEILEAQnlplPEPAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 192 SAAWMAPEVFEGSNYSEKC----DVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNgtRPPLIKNL----PKPIE--S 261
Cdd:cd14043 161 ELLWTAPELLRDPRLERRGtfpgDVFSFAIIMQEVIVRGAPYCMLGLSPEEIIEKVRS--PPPLCRPSvsmdQAPLEciQ 238
                       250       260
                ....*....|....*....|....*...
gi 21735562 262 LMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14043 239 LMKQCWSEAPERRPTFDQIFDQFKSINK 266
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
42-229 5.73e-19

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 87.22  E-value: 5.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA-------KWrakdvAIKQIESE----SERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd14097   9 LGQGSFGVVIEAthketqtKW-----AIKKINREkagsSAVKLLEREVDILKHVNHAHIIHLEEVFETPkrMYLVMELCE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEplpyYTAAHAMSWCLQC-SQGVAYLHSmqpKALIHRDLKPPNLLLV------AGGTVLKICDFGTACD 181
Cdd:cd14097  84 DGELKELLLRKG----FFSENETRHIIQSlASAVAYLHK---NDIVHRDLKLENILVKssiidnNDKLNIKVTDFGLSVQ 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 182 IQ----THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14097 157 KYglgeDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPF 208
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
42-282 6.17e-19

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 87.77  E-value: 6.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK--WRAKDVAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSL 112
Cdd:cd06634  23 IGHGSFGAVYFARdvRNNEVVAIKKMsysgkQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLreHTAWLVMEYCLGSAS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTAcDIQTHMTNNKGS 192
Cdd:cd06634 103 DLLEVHKKPLQEVEIAAITHGALQ---GLAYLHSHN---MIHRDVKAGNILLTEPGLV-KLGDFGSA-SIMAPANSFVGT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEV---FEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPPLIKN-LPKPIESLMTRCWS 268
Cdd:cd06634 175 PYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMN--AMSALYHIAQNESPALQSGhWSEYFRNFVDSCLQ 252
                       250
                ....*....|....
gi 21735562 269 KDPSQRPSMEEIVK 282
Cdd:cd06634 253 KIPQDRPTSDVLLK 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
42-229 6.38e-19

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 87.49  E-value: 6.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA---KWRAKDVAIKQIESE---------SERKAFIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYA 107
Cdd:cd14096   9 IGEGAFSNVYKAvplRNTGKPVAIKVVRKAdlssdnlkgSSRANILKEVQIMKRLSHPNIVKLLDFQESDEyyYIVLELA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLL----------------------- 164
Cdd:cd14096  89 DGGEIFHQI---VRLTYFSEDLSRHVITQVASAVKYLHEI---GVVHRDIKPENLLFepipfipsivklrkadddetkvd 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 165 -------VAGGTV--LKICDFGTACDIQTHMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14096 163 egefipgVGGGGIgiVKLADFGLSKQVWDSNTKTPcGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
37-231 6.55e-19

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 86.67  E-value: 6.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd14078   6 ELHETIGSGGFAKVKLATHILtgEKVAIKIMDKKAlgdDLPRVKTEIEALKNLSHQHICRLYHVIETDnkIFMVLEYCPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTACD----IQTH 185
Cdd:cd14078  86 GELFDYIVAKDRLSEDEARVFFR---QIVSAVAYVHS---QGYAHRDLKPENLLLDEDQN-LKLIDFGLCAKpkggMDHH 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNY-SEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd14078 159 LETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDD 205
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
33-279 8.16e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 86.64  E-value: 8.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQI----------ESESERKAFIVE---LRQLSRvnHPNIVKLYGACL 97
Cdd:cd14093   2 YAKYEPKEILGRGVSSTVrrCIEKETGQEFAVKIIditgekssenEAEELREATRREieiLRQVSG--HPNIIELHDVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NP--VCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICD 175
Cdd:cd14093  80 SPtfIFLVFELCRKGELFDYLTEVVTLSEKKTRRIM---RQLFEAVEFLHS---LNIVHRDLKPENILLDDNLNV-KISD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTACDIQ--THMTNNKGSAAWMAPEVFEGS------NYSEKCDVFSWGIILWEVItrrkpfdeIGGPAF---------- 237
Cdd:cd14093 153 FGFATRLDegEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLL--------AGCPPFwhrkqmvmlr 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21735562 238 RIMWAVHNGTRPPL--IKNLPKpieSLMTRCWSKDPSQRPSMEE 279
Cdd:cd14093 225 NIMEGKYEFGSPEWddISDTAK---DLISKLLVVDPKKRLTAEE 265
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
33-268 8.97e-19

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 86.13  E-value: 8.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESE-RKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVM--EYA 107
Cdd:cd14110   2 EKTYAFQTEINRGRFSVVrqCEEKRSGQMLAAKIIPYKPEdKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLieELC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDI---QT 184
Cdd:cd14110  82 SGPEL---LYNLAERNSYSEAEVTDYLWQILSAVDYLHS---RRILHLDLRSEN-MIITEKNLLKIVDLGNAQPFnqgKV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGS-AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGpafrimWAVHNGTRPPLIKnlpkpieslM 263
Cdd:cd14110 155 LMTDKKGDyVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLN------WERDRNIRKGKVQ---------L 219

                ....*
gi 21735562 264 TRCWS 268
Cdd:cd14110 220 SRCYA 224
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
34-281 9.44e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 86.86  E-value: 9.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEY 106
Cdd:cd06619   1 QDIQYQEILGHGNGGTVYKAyhLLTRRILAVKVIPldiTVELQKQIMSELEILYKCDSPYIIGFYGAFFveNRISICTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYYTAAHAMswclqcsQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGtacdIQTHM 186
Cdd:cd06619  81 MDGGSLDVYRKIPEHVLGRIAVAVV-------KGLTYLWSLK---ILHRDVKPSNMLVNTRGQV-KLCDFG----VSTQL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNN-----KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGG------PAFRIMWAVHNGtrPPL--IK 253
Cdd:cd06619 146 VNSiaktyVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKnqgslmPLQLLQCIVDED--PPVlpVG 223
                       250       260
                ....*....|....*....|....*...
gi 21735562 254 NLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd06619 224 QFSEKFVHFITQCMRKQPKERPAPENLM 251
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
37-290 1.24e-18

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 86.58  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA--KWRAKDVAIKQIES----ESERKAFIVELRQLSrvNHPNIVKLYGACLNP-------VCLV 103
Cdd:cd06639  25 DIIETIGKGTYGKVYKVtnKKDGSLAAVKILDPisdvDEEIEAEYNILRSLP--NHPNVVKFYGMFYKAdqyvggqLWLV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGA--------EPLPYYTAAHAMswclqcsQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICD 175
Cdd:cd06639 103 LELCNGGSVTELVKGLlkcgqrldEAMISYILYGAL-------LGLQHLHNNR---IIHRDVKGNNILLTTEGGV-KLVD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTACDI-QTHMTNNK--GSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPFDEIgGPAFRIMWAVHNgt 247
Cdd:cd06639 172 FGVSAQLtSARLRRNTsvGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPLFDM-HPVKALFKIPRN-- 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 248 RPPLIKNLPKPIES---LMTRCWSKDPSQRPSmeeivkiMTHLMRY 290
Cdd:cd06639 249 PPPTLLNPEKWCRGfshFISQCLIKDFEKRPS-------VTHLLEH 287
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
37-279 1.26e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 86.23  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVA---IKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd14194   8 DTGEELGSGQFAVVkkCREKSTGLQYAakfIKKRRTKSSRRGVSRedierEVSILKEIQHPNVITLHEVYENKtdVILIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLV---AGGTVLKICDFGTA-- 179
Cdd:cd14194  88 ELVAGGELFDFLAEKESL---TEEEATEFLKQILNGVYYLHSLQ---IAHFDLKPENIMLLdrnVPKPRIKIIDFGLAhk 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:cd14194 162 IDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlGDTKQETLANVSAVNYEFEDEYFSNTSAL 241
                       250       260
                ....*....|....*....|.
gi 21735562 259 IESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14194 242 AKDFIRRLLVKDPKKRMTIQD 262
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
37-279 1.40e-18

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 87.14  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP-------VCLV 103
Cdd:cd07859   3 KIQEVIGKGSYGVVCSAIDThtGEKVAIKKIndvfEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPsrrefkdIYVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAgGTVLKICDFGTAcdiQ 183
Cdd:cd07859  83 FELMES-DLHQVIKANDDL---TPEHHQFFLYQLLRALKYIHTAN---VFHRDLKPKNILANA-DCKLKICDFGLA---R 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNNKGSAAWM---------APEVFEG--SNYSEKCDVFSWGIILWEVITRRKPF-------------DEIGGPAFRI 239
Cdd:cd07859 152 VAFNDTPTAIFWTdyvatrwyrAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFpgknvvhqldlitDLLGTPSPET 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 240 MWAVHN-GTRPPLI---KNLPKPIES-----------LMTRCWSKDPSQRPSMEE 279
Cdd:cd07859 232 ISRVRNeKARRYLSsmrKKQPVPFSQkfpnadplalrLLERLLAFDPKDRPTAEE 286
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
43-229 1.42e-18

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 86.22  E-value: 1.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKA----KWRAKDVAIKQIESE--SERKAFIVE--LRQLS---RVNHPNIVKLYGAC---LNPVCLVMEYAE 108
Cdd:cd13990   9 GKGGFSEVYKAfdlvEQRYVACKIHQLNKDwsEEKKQNYIKhaLREYEihkSLDHPRIVKLYDVFeidTDSFCTVLEYCD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSMQPKaLIHRDLKPPNLLLVAGGT--VLKICDFGTaCDI--QT 184
Cdd:cd13990  89 GNDLDFYLKQHKSIP---EREARSIIMQVVSALKYLNEIKPP-IIHYDLKPGNILLHSGNVsgEIKITDFGL-SKImdDE 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 185 HMTNNK--------GSAAWMAPEVF----EGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd13990 164 SYNSDGmeltsqgaGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQMLYGRKPF 220
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
42-281 1.62e-18

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 85.44  E-value: 1.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE------SESERKAFIVELRQLSRVNHPNIVKLYGACLNPV----C--LVMEYAEG 109
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCElqtrklSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVrghkCiiLVTELMTS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAHamsWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNN 189
Cdd:cd14033  89 GTLKTYLKRFREMKLKLLQR---WSRQILKGLHFLHSRCP-PILHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K-GSAAWMAPEVFEgSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKP-IESLMTRCW 267
Cdd:cd14033 165 ViGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSECQNAA-QIYRKVTSGIKPDSFYKVKVPeLKEIIEGCI 242
                       250
                ....*....|....
gi 21735562 268 SKDPSQRPSMEEIV 281
Cdd:cd14033 243 RTDKDERFTIQDLL 256
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
42-286 1.99e-18

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 85.51  E-value: 1.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIE------SESERKAFIVELRQLSRVNHPNIVKLY------GACLNPVCLVMEYAEG 109
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCElqdrklTKVERQRFKEEAEMLKGLQHPNIVRFYdfwescAKGKRCIVLVTELMTS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLhgaEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNN 189
Cdd:cd14032  89 GTLKTYL---KRFKVMKPKVLRSWCRQILKGLLFLHTRTP-PIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K-GSAAWMAPEVFEgSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAfRIMWAVHNGTRPPLIKNLPKP-IESLMTRCW 267
Cdd:cd14032 165 ViGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAA-QIYRKVTCGIKPASFEKVTDPeIKEIIGECI 242
                       250
                ....*....|....*....
gi 21735562 268 SKDPSQRpsmEEIVKIMTH 286
Cdd:cd14032 243 CKNKEER---YEIKDLLSH 258
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
42-225 2.05e-18

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 86.46  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA---KWRAKdVAIKQIESESERKAFIV--ELRQLSRVN--HPNIVKL---------------YGA---- 95
Cdd:cd13977   8 VGRGSYGVVYEAvvrRTGAR-VAVKKIRCNAPENVELAlrEFWALSSIQrqHPNVIQLeecvlqrdglaqrmsHGSsksd 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  96 --------------CLNPVC-----LVMEYAEGGSLYNVLHGAEPlpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRD 156
Cdd:cd13977  87 lylllvetslkgerCFDPRSacylwFVMEFCDGGDMNEYLLSRRP----DRQTNTSFMLQLSSALAFLHRNQ---IVHRD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 157 LKPPNLLLV--AGGTVLKICDFG-------TACDIQTHMTNNK-------GSAAWMAPEVFEGsNYSEKCDVFSWGIILW 220
Cdd:cd13977 160 LKPDNILIShkRGEPILKVADFGlskvcsgSGLNPEEPANVNKhflssacGSDFYMAPEVWEG-HYTAKADIFALGIIIW 238

                ....*
gi 21735562 221 EVITR 225
Cdd:cd13977 239 AMVER 243
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
43-231 2.29e-18

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 85.26  E-value: 2.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGACLNPVCLVMeYAEGGSLYNVLHGA 119
Cdd:cd14111  12 ARGRFGVIrrCRENATGKNFPAKIVPYQAEEKQGVLqEYEILKSLHHERIMALHEAYITPRYLVL-IAEFCSGKELLHSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 120 EPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTA----------CDIQThmtnn 189
Cdd:cd14111  91 IDRFRYSEDDVVGYLVQILQGLEYLHG---RRVLHLDIKPDNIM-VTNLNAIKIVDFGSAqsfnplslrqLGRRT----- 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21735562 190 kGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd14111 162 -GTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFED 202
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
37-229 2.60e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 85.01  E-value: 2.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVA---IKQIESESERKAFIV-----ELRQLSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd14196   8 DIGEELGSGQFAIVkkCREKSTGLEYAakfIKKRQSRASRRGVSReeierEVSILRQVLHPNIITLHDVYENRtdVVLIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVL---KICDFGTACD 181
Cdd:cd14196  88 ELVSGGELFDFLAQKESL---SEEEATSFIKQILDGVNYLHT---KKIAHFDLKPENIMLLDKNIPIphiKLIDFGLAHE 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQ--THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14196 162 IEdgVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
37-282 2.60e-18

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 85.19  E-value: 2.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWR--AKDVAIKQI-------ESESERKAFIVELRQLSRV----------NHPNIVKLYGACL 97
Cdd:cd14077   4 EFVKTIGAGSMGKVKLAKHIrtGEKCAIKIIprasnagLKKEREKRLEKEISRDIRTireaalssllNHPHICRLRDFLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVC--LVMEYAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICD 175
Cdd:cd14077  84 TPNHyyMLFEYVDGGQLLDYIISHGKL---KEKQARKFARQIASALDYLHR---NSIVHRDLKIENILISKSGNI-KIID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 176 FGTA--CDIQTHMTNNKGSAAWMAPEVFEGSNYS-EKCDVFSWGIILWEVITRRKPFDEIGGPAF--RIMWAVHNgtrpp 250
Cdd:cd14077 157 FGLSnlYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALhaKIKKGKVE----- 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 251 LIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14077 232 YPSYLSSECKSLISRMLVVDPKKRATLEQVLN 263
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
38-276 3.08e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.00  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   38 VEEVVGRGAFGVVCKAKWRAKD--VAIKQIE----SESERKAFIVELRQLSRVNHPNIVK-----LYGACLNP-----VC 101
Cdd:PTZ00283  36 ISRVLGSGATGTVLCAKRVSDGepFAVKVVDmegmSEADKNRAQAEVCCLLNCDFFSIVKchedfAKKDPRNPenvlmIA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  102 LVMEYAEGGSLY----NVLHGAEPLPYYTAAhamswcLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:PTZ00283 116 LVLDYANAGDLRqeikSRAKTNRTFREHEAG------LLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLV-KLGDFG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  178 TacdiqTHMTNNK----------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGT 247
Cdd:PTZ00283 189 F-----SKMYAATvsddvgrtfcGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFD--GENMEEVMHKTLAGR 261
                        250       260
                 ....*....|....*....|....*....
gi 21735562  248 RPPLIKNLPKPIESLMTRCWSKDPSQRPS 276
Cdd:PTZ00283 262 YDPLPPSISPEMQEIVTALLSSDPKRRPS 290
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
38-282 3.27e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 85.46  E-value: 3.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVELrqLSRV-NHPNIVKLYGACLN--PVCLVMEYAEGGSL 112
Cdd:cd14175   5 VKETIGVGSYSVCkrCVHKATNMEYAVKVIDKSKRDPSEEIEI--LLRYgQHPNIITLKDVYDDgkHVYLVTELMRGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV---AGGTVLKICDFGTACDIQTH---- 185
Cdd:cd14175  83 LDKILRQK---FFSEREASSVLHTICKTVEYLHS---QGVVHRDLKPSNILYVdesGNPESLRICDFGFAKQLRAEngll 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKgSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF------------DEIGGPAFRImwavhNGTRPPLIK 253
Cdd:cd14175 157 MTPCY-TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangpsdtpeeilTRIGSGKFTL-----SGGNWNTVS 230
                       250       260
                ....*....|....*....|....*....
gi 21735562 254 NLPKPIESLMTRCwskDPSQRPSMEEIVK 282
Cdd:cd14175 231 DAAKDLVSKMLHV---DPHQRLTAKQVLQ 256
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
30-280 3.66e-18

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 85.06  E-value: 3.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCKAKW------RAKDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACLN-- 98
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGHLylpgmdHAQLVAIKTLKdynNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQeq 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 PVCLVMEYAEGGSLYNVLHGAEP------------LPYYTAAHA--MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLl 164
Cdd:cd05090  81 PVCMLFEFMNQGDLHEFLIMRSPhsdvgcssdedgTVKSSLDHGdfLHIAIQIAAGMEYLSS---HFFVHKDLAARNIL- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 165 VAGGTVLKICDFGTACDIQT---HMTNNKG--SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITR-RKPFdeIGGPAFR 238
Cdd:cd05090 157 VGEQLHVKISDLGLSREIYSsdyYRVQNKSllPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFgLQPY--YGFSNQE 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21735562 239 IMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd05090 235 VIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
41-286 4.33e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 85.34  E-value: 4.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKD--VAIK-----QIESESERKAFIVELRQLSRVN-HPNIVKLYgACL---NPVCLVMEYAEG 109
Cdd:cd05570   2 VLGKGSFGKVMLAERKKTDelYAIKvlkkeVIIEDDDVECTMTEKRVLALANrHPFLTGLH-ACFqteDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaCdiQTHMTNN 189
Cdd:cd05570  81 GDL---MFHIQRARRFTEERARFYAAEICLALQFLHE---RGIIYRDLKLDNVLLDAEGHI-KIADFGM-C--KEGIWGG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-----DEIggpaFR-IMwavhngTRPPLI-KNLP 256
Cdd:cd05570 151 NttstfcGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFegddeDEL----FEaIL------NDEVLYpRWLS 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 257 KPIESLMTRCWSKDPSQR----PSMEEivKIMTH 286
Cdd:cd05570 221 REAVSILKGLLTKDPARRlgcgPKGEA--DIKAH 252
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
25-224 4.46e-18

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 85.83  E-value: 4.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  25 VLNFEEIDyKEIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQIESeseRKAFI----VELRQLSRVNHP------NIVKL 92
Cdd:cd14226   5 VKNGEKWM-DRYEIDSLIGKGSFGQVVKAydHVEQEWVAIKIIKN---KKAFLnqaqIEVRLLELMNKHdtenkyYIVRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  93 YGACL--NPVCLVME---YaeggSLYNVL-----HGAEPLPYYTAAHamswclQCSQGVAYLhSMQPKALIHRDLKPPNL 162
Cdd:cd14226  81 KRHFMfrNHLCLVFEllsY----NLYDLLrntnfRGVSLNLTRKFAQ------QLCTALLFL-STPELSIIHCDLKPENI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21735562 163 LLV-AGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14226 150 LLCnPKRSAIKIIDFGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHT 212
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
42-225 5.21e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 85.11  E-value: 5.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR--AKDVAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACLNPVC----------LVME 105
Cdd:cd07865  20 IGQGTFGEVFKARHRktGQIVALKKVLMENEKEGFpitaLREIKILQLLKHENVVNLIEICRTKATpynrykgsiyLVFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAE---GGSLYNvlhgaePLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTA--- 179
Cdd:cd07865 100 FCEhdlAGLLSN------KNVKFTLSEIKKVMKMLLNGLYYIHRNK---ILHRDMKAANILITKDG-VLKLADFGLAraf 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 180 ----CDIQTHMTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITR 225
Cdd:cd07865 170 slakNSQPNRYTNRVVTLWYRPPELLLGErDYGPPIDMWGAGCIMAEMWTR 220
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
40-285 5.32e-18

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 84.43  E-value: 5.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWR-----AKDVAIKQIE---SESERKAFIVELRQLSRVNHPNIVKLYGACL---NPVCLVMEYAE 108
Cdd:cd05043  12 DLLQEGTFGRIFHGILRdekgkEEEVLVKTVKdhaSEIQVTMLLQESSLLYGLSHQNLLPILHVCIedgEKPMVLYPYMN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL----HGAEPLPYYTAAHAM-SWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDI- 182
Cdd:cd05043  92 WGNLKLFLqqcrLSEANNPQALSTQQLvHMALQIACGMSYLHR---RGVIHKDIAARNCVIDDELQV-KITDNALSRDLf 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 --QTHM--TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK-PFDEIGgpAFRIMWAVHNGTRPPLIKNLPK 257
Cdd:cd05043 168 pmDYHClgDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQtPYVEID--PFEMAAYLKDGYRLAQPINCPD 245
                       250       260
                ....*....|....*....|....*...
gi 21735562 258 PIESLMTRCWSKDPSQRPSMEEIVKIMT 285
Cdd:cd05043 246 ELFAVMACCWALDPEERPSFQQLVQCLT 273
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
41-229 5.67e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 85.43  E-value: 5.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWR--AKDVAIK-----------QIES-ESERKAFIVelrqLSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd05589   6 VLGRGHFGKVLLAEYKptGELFAIKalkkgdiiardEVESlMCEKRIFET----VNSARHPFLVNLFACFQTPehVCFVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHG---AEPLPYYTAAhamswCLQCsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFG---- 177
Cdd:cd05589  82 EYAAGGDLMMHIHEdvfSEPRAVFYAA-----CVVL--GLQFLHE---HKIVYRDLKLDNLLLDTEGYV-KIADFGlcke 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 178 ---------TACdiqthmtnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05589 151 gmgfgdrtsTFC----------GTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
32-229 5.70e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 84.39  E-value: 5.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACL--NPVCLV 103
Cdd:cd07861   1 DYTKIEK---IGEGTYGVVYKGRNKKtgQIVAMKKIRLESEEEGVpstaIREISLLKELQHPNIVCLEDVLMqeNRLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGgSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFG--TACD 181
Cdd:cd07861  78 FEFLSM-DLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHS---RRVLHRDLKPQNLLIDNKG-VIKLADFGlaRAFG 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07861 153 IPVRVYTHEVVTLWYrAPEVLLGSpRYSTPVDIWSIGTIFAEMATKKPLF 202
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
35-231 6.01e-18

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 84.00  E-value: 6.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWR--AKDVAIKQIE-------SESERKAfivELRQLSRVNHPNIVKLYGACLNP--VCLV 103
Cdd:cd14082   4 QIFPDEVLGSGQFGIVYGGKHRktGRDVAIKVIDklrfptkQESQLRN---EVAILQQLSHPGVVNLECMFETPerVFVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVL-HGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDFGTAC 180
Cdd:cd14082  81 MEKLHGDMLEMILsSEKGRLPERITKFLVT---QILVALRYLHS---KNIVHCDLKPENVLLASAEPFpqVKLCDFGFAR 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 181 DI--QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd14082 155 IIgeKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNE 207
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
34-231 7.28e-18

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 85.05  E-value: 7.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAK-DV----AIKQIESES-ERKAFIVELRQ-LSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATgDIyamkVLKKSETLAqEEVSFFEEERDiMAKANSPWITKLQYAFQdsENLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLpyYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT 184
Cdd:cd05601  81 EYHPGGDLLSLLSRYDDI--FEESMARFYLAELVLAIHSLHSM---GYVHRDIKPENILIDRTGHI-KLADFGSAAKLSS 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 185 HMTNNK----GSAAWMAPEVFE------GSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd05601 155 DKTVTSkmpvGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTE 211
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
37-230 7.30e-18

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 84.38  E-value: 7.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESerkafIVELRQ----------LSRVNHPNIVKLYGA--CLNPVCL 102
Cdd:cd14209   4 DRIKTLGTGSFGRVmlVRHKETGNYYAMKILDKQK-----VVKLKQvehtlnekriLQAINFPFLVKLEYSfkDNSNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPYYtaaHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDI 182
Cdd:cd14209  79 VMEYVPGGEMFSHLRRIGRFSEP---HARFYAAQIVLAFEYLHSLD---LIYRDLKPENLLIDQQG-YIKVTDFGFAKRV 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd14209 152 KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF 199
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
42-235 7.53e-18

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 84.85  E-value: 7.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQIESESERKAFIVELRQ---LSRVNHPNIVKLYGA-----CLNPVcLVMEYAEGGS 111
Cdd:cd13988   1 LGQGATANVFRGrhKKTGDLYAVKVFNNLSFMRPLDVQMREfevLKKLNHKNIVKLFAIeeeltTRHKV-LVMELCPCGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHgaEPLPYYTAAHamSWCLQCSQGV-AYLHSMQPKALIHRDLKPPNLLLVA---GGTVLKICDFGTACDIQ--TH 185
Cdd:cd13988  80 LYTVLE--EPSNAYGLPE--SEFLIVLRDVvAGMNHLRENGIVHRDIKPGNIMRVIgedGQSVYKLTDFGAARELEddEQ 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 186 MTNNKGSAAWMAPEVFE--------GSNYSEKCDVFSWGIILWEVITRRKPFDEIGGP 235
Cdd:cd13988 156 FVSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGP 213
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
30-281 8.85e-18

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 83.93  E-value: 8.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEIEVEEVVGRGAFGVVCK--AKWRAKD-----VAIKQI-ESES--ERKAFIVELRQLSRVNHPNIVKLYGACLN- 98
Cdd:cd05062   2 EVAREKITMSRELGQGSFGMVYEgiAKGVVKDepetrVAIKTVnEAASmrERIEFLNEASVMKEFNCHHVVRLLGVVSQg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 -PVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHA-------MSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTV 170
Cdd:cd05062  82 qPTLVIMELMTRGDLKSYLRSLRPEMENNPVQAppslkkmIQMAGEIADGMAYLNANK---FVHRDLAARNCMVAEDFTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 171 lKICDFGTACDIQTHMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVIT-RRKPFDeiGGPAFRIMWAVH 244
Cdd:cd05062 159 -KIGDFGMTRDIYETDYYRKGGKGllpvrWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQ--GMSNEQVLRFVM 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 245 NGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd05062 236 EGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 272
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
42-287 9.12e-18

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 83.94  E-value: 9.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGACLN------PVCLVMEYAEGGSLYN 114
Cdd:cd14220   3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFReTEIYQTVLMRHENILGFIAADIKgtgswtQLYLITDYHENGSLYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEplpyYTAAHAMSWCLQCSQGVAYLHS----MQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTAC-------DI 182
Cdd:cd14220  83 FLKCTT----LDTRALLKLAYSAACGLCHLHTeiygTQGKpAIAHRDLKSKNILIKKNGTCC-IADLGLAVkfnsdtnEV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGS---NYSEK---CDVFSWGIILWEVITR----------RKPFDEI--GGPAFRIMWAV- 243
Cdd:cd14220 158 DVPLNTRVGTKRYMAPEVLDESlnkNHFQAyimADIYSFGLIIWEMARRcvtggiveeyQLPYYDMvpSDPSYEDMREVv 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 244 -HNGTRPPLIKNLP-----KPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14220 238 cVKRLRPTVSNRWNsdeclRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
36-282 9.16e-18

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 83.87  E-value: 9.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  36 IEVEEVVGRGAFGVVCKAKWRA-------KDVAIKQIESESERKAFIVELRQLSrvNHPNIVKLYGACLNP-------VC 101
Cdd:cd14037   5 VTIEKYLAEGGFAHVYLVKTSNggnraalKRVYVNDEHDLNVCKREIEIMKRLS--GHKNIVGYIDSSANRsgngvyeVL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNV--------LHGAEPLPYYTaahamswclQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTvLKI 173
Cdd:cd14037  83 LLMEYCKGGGVIDLmnqrlqtgLTESEILKIFC---------DVCEAVAAMHYLKP-PLIHRDLKVENVLISDSGN-YKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFGTAC-----------------DIQTHMTnnkgsAAWMAPE---VFEGSNYSEKCDVFSWGIILWEVITRRKPFDEiG 233
Cdd:cd14037 152 CDFGSATtkilppqtkqgvtyveeDIKKYTT-----LQYRAPEmidLYRGKPITEKSDIWALGCLLYKLCFYTTPFEE-S 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 234 GPAfrimwAVHNG--TRPPLIKNLPKpIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14037 226 GQL-----AILNGnfTFPDNSRYSKR-LHKLIRYMLEEDPEKRPNIYQVSY 270
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
40-301 9.63e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 83.68  E-value: 9.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLS---RVNHPNIVKLYGA--CLNPVCLVMEYAEGG-S 111
Cdd:cd07836   6 EKLGEGTYATVYKGRNRTTGeiVALKEIHLDAEEGTPSTAIREISlmkELKHENIVRLHDVihTENKLMLVFEYMDKDlK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAE-PLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG--TACDIQTHMTN 188
Cdd:cd07836  86 KYMDTHGVRgALD---PNTVKSFTYQLLKGIAFCHE---NRVLHRDLKPQNLLINKRGE-LKLADFGlaRAFGIPVNTFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF------DEIgGPAFRIMWAVHNGTRPPlIKNLPKpIE 260
Cdd:cd07836 159 NEVVTLWYrAPDVLLGSrTYSTSIDIWSVGCIMAEMITGRPLFpgtnneDQL-LKIFRIMGTPTESTWPG-ISQLPE-YK 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 261 SLMTRCWSKDPSQ-RPSMEEI-VKIMTHLMRYFP----GADEPLQYP 301
Cdd:cd07836 236 PTFPRYPPQDLQQlFPHADPLgIDLLHRLLQLNPelriSAHDALQHP 282
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
30-277 1.02e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 84.32  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  30 EIDYKEieveEVVGRGAFGVV--CKAKWRAKDVAIK----QIESESERKAFIVELRQlsrvNHPNIVKLYGACLNPV--C 101
Cdd:cd14179   7 ELDLKD----KPLGEGSFSICrkCLHKKTNQEYAVKivskRMEANTQREIAALKLCE----GHPNIVKLHEVYHDQLhtF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMqpkALIHRDLKPPNLLLV--AGGTVLKICDFGTA 179
Cdd:cd14179  79 LVMELLKGGELLERIKKKQHFSETEASHIMR---KLVSAVSHMHDV---GVVHRDLKPENLLFTdeSDNSEIKIIDFGFA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 cdiQTHMTNNKG------SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIG-----GPAFRIMWAVHNGT- 247
Cdd:cd14179 153 ---RLKPPDNQPlktpcfTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDksltcTSAEEIMKKIKQGDf 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 21735562 248 --RPPLIKNLPKPIESLMTRCWSKDPSQRPSM 277
Cdd:cd14179 230 sfEGEAWKNVSQEAKDLIQGLLTVDPNKRIKM 261
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
37-279 1.10e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 84.53  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVckakWRAKD------VAIKQI-----ESESERKAF--IVELRQLSrvNHPNIVKLY----GACLNP 99
Cdd:cd07852  10 EILKKLGKGAYGIV----WKAIDkktgevVALKKIfdafrNATDAQRTFreIMFLQELN--DHPNIIKLLnvirAENDKD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGgSLYNVLHGA--EPLpyytaaHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:cd07852  84 IYLVFEYMET-DLHAVIRANilEDI------HKQYIMYQLLKALKYLHSGG---VIHRDLKPSNILLNSDCRV-KLADFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQThMTNNKGSAA--------WM-APEVFEGSN-YSEKCDVFSWGIILWEVITRR-------------KPFDEIGG 234
Cdd:cd07852 153 LARSLSQ-LEEDDENPVltdyvatrWYrAPEILLGSTrYTKGVDMWSVGCILGEMLLGKplfpgtstlnqleKIIEVIGR 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 235 P------------AFRIMWAVHNGTRPPLIKNLPK-PIES--LMTRCWSKDPSQRPSMEE 279
Cdd:cd07852 232 PsaediesiqspfAATMLESLPPSRPKSLDELFPKaSPDAldLLKKLLVFNPNKRLTAEE 291
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
38-287 1.31e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 83.54  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVVCKAKWRAKD--VAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAE 108
Cdd:cd08229  28 IEKKIGRGQFSEVYRATCLLDGvpVALKKVQifdlmDAKARADCIKEIDLLKQLNHPNVIKYYASFIedNELNIVLELAD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL-HGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGtVLKICDFGTACDIQTHMT 187
Cdd:cd08229 108 AGDLSRMIkHFKKQKRLIPEKTVWKYFVQLCSALEHMHS---RRVMHRDIKPANVFITATG-VVKLGDLGLGRFFSSKTT 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKN-LPKPIESLM 263
Cdd:cd08229 184 AAHslvGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDhYSEELRQLV 263
                       250       260
                ....*....|....*....|....
gi 21735562 264 TRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd08229 264 NMCINPDPEKRPDITYVYDVAKRM 287
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
76-287 1.42e-17

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 83.01  E-value: 1.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  76 VELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGGSLYNVLHGAEPLPYYTAahaMSWCLQCS------QGVAYLHSm 147
Cdd:cd14044  52 IELNKLLQIDYYNLTKFYGTVKldTMIFGVIEYCERGSLRDVLNDKISYPDGTF---MDWEFKISvmydiaKGMSYLHS- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 148 qPKALIHRDLKPPNLLlVAGGTVLKICDFGtaCDiqTHMTNNKGsaAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRK 227
Cdd:cd14044 128 -SKTEVHGRLKSTNCV-VDSRMVVKITDFG--CN--SILPPSKD--LWTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKE 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 228 PF-----DEIGGPAFRIMWAvhNGT---RPPLikNLPKPIE------SLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14044 200 TFytaacSDRKEKIYRVQNP--KGMkpfRPDL--NLESAGErerevyGLVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
42-286 1.62e-17

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 83.91  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAkwRAKDV----AIKqieseSERKAFIVELRQLSRV----------NHPNIVKLYGACLNPVCL--VME 105
Cdd:cd05598   9 IGVGAFGEVSLV--RKKDTnalyAMK-----TLRKKDVLKRNQVAHVkaerdilaeaDNEWVVKLYYSFQDKENLyfVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGA----EPLP-YYTAAhamswcLQCSqgVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTAC 180
Cdd:cd05598  82 YIPGGDLMSLLIKKgifeEDLArFYIAE------LVCA--IESVHKM---GFIHRDIKPDNILIDRDGHI-KLTDFGLCT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 DIQ-THmtNNK--------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIM-WavHNGTR 248
Cdd:cd05598 150 GFRwTH--DSKyylahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFlaQTPAETQLKVInW--RTTLK 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21735562 249 PPLIKNLPKPIESLMTRcWSKDPSQRPSMEEIVKIMTH 286
Cdd:cd05598 226 IPHEANLSPEAKDLILR-LCCDAEDRLGRNGADEIKAH 262
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
32-226 2.09e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 83.13  E-value: 2.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYkeiEVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAF-IVELRQ---LSRVNHPNIVKLygaclnpVCLVME 105
Cdd:cd07866   9 DY---EILGKLGEGTFGEVYKARQIKtgRVVALKKILMHNEKDGFpITALREikiLKKLKHPNVVPL-------IDMAVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEG-----GSLYNVlhgaepLPY---------------YTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV 165
Cdd:cd07866  79 RPDKskrkrGSVYMV------TPYmdhdlsgllenpsvkLTESQIKCYMLQLLEGINYLHE---NHILHRDIKAANILID 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 166 AGGtVLKICDFGTACDIQTHMTNNKGSAA-------------WM-APEVFEG-SNYSEKCDVFSWGIILWEVITRR 226
Cdd:cd07866 150 NQG-ILKIADFGLARPYDGPPPNPKGGGGggtrkytnlvvtrWYrPPELLLGeRRYTTAVDIWGIGCVFAEMFTRR 224
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
40-276 2.16e-17

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 82.77  E-value: 2.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIK------QIESESERKAFivelrQLSRVNHPNIVKLYGACLNPVCLVMEYAeggsLY 113
Cdd:cd14140   1 EIKARGRFGCVWKAQLMNEYVAVKifpiqdKQSWQSEREIF-----STPGMKHENLLQFIAAEKRGSNLEMELW----LI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLHGAEPLPYYTAAHAMSWCLQC------SQGVAYLHSMQPK--------ALIHRDLKPPNLLLVAGGTVLkICDFGTA 179
Cdd:cd14140  72 TAFHDKGSLTDYLKGNIVSWNELChiaetmARGLSYLHEDVPRckgeghkpAIAHRDFKSKNVLLKNDLTAV-LADFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQ-------THmtNNKGSAAWMAPEVFEGS-NYSE----KCDVFSWGIILWEVITRRK-----------PF-DEIGG- 234
Cdd:cd14140 151 VRFEpgkppgdTH--GQVGTRRYMAPEVLEGAiNFQRdsflRIDMYAMGLVLWELVSRCKaadgpvdeymlPFeEEIGQh 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 235 ----------------PAFRIMWAVHNGtrpplIKNLPKPIEslmtRCWSKDPSQRPS 276
Cdd:cd14140 229 psledlqevvvhkkmrPVFKDHWLKHPG-----LAQLCVTIE----ECWDHDAEARLS 277
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
41-231 2.18e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 82.76  E-value: 2.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESE--SERKAFIVELRQ---LSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05630   7 VLGKGGFGEVCACQVRAtgKMYACKKLEKKriKKRKGEAMALNEkqiLEKVNSRFVVSLAYAyeTKDALCLVLTLMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L-YNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMT--N 188
Cdd:cd05630  87 LkFHIYHMGQA--GFPEARAVFYAAEICCGLEDLHR---ERIVYRDLKPENILLDDHGHI-RISDLGLAVHVPEGQTikG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 189 NKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd05630 161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQ 203
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
40-307 2.30e-17

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 83.50  E-value: 2.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGaCLNP---------VCLVM 104
Cdd:cd07851  21 SPVGSGAYGQVCSAFDTKTGrkVAIKKLsrpfQSAIHAKRTYRELRLLKHMKHENVIGLLD-VFTPassledfqdVYLVT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAeGGSLYNVLhGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQT 184
Cdd:cd07851 100 HLM-GADLNNIV-KCQKL---SDDHIQFLVYQILRGLKYIHSA---GIIHRDLKPSN-LAVNEDCELKILDFGLARHTDD 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 185 HMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF------DEIGgpafRIMWAVhnGTRPP------- 250
Cdd:cd07851 171 EMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFpgsdhiDQLK----RIMNLV--GTPDEellkkis 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 251 ------LIKNLPK--------------PIE-SLMTRCWSKDPSQRPSMEEivkIMTH--LMRYFPGADEPLQYPCQYSDE 307
Cdd:cd07851 245 sesarnYIQSLPQmpkkdfkevfsganPLAiDLLEKMLVLDPDKRITAAE---ALAHpyLAEYHDPEDEPVAPPYDQSFE 321
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
39-229 2.53e-17

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 82.77  E-value: 2.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVV--CKAKWRAKDVAIKQIESES--ERKAFIVELRQLSRVN-HPNIVKLYGACLNPVC--LVMEYAEGGS 111
Cdd:cd14174   7 DELLGEGAYAKVqgCVSLQNGKEYAVKIIEKNAghSRSRVFREVETLYQCQgNKNILELIEFFEDDTRfyLVFEKLRGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 lynVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDF--------GTACD 181
Cdd:cd14174  87 ---ILAHIQKRKHFNEREASRVVRDIASALDFLHT---KGIAHRDLKPENILCESPDKVspVKICDFdlgsgvklNSACT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 182 IQT--HMTNNKGSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14174 161 PITtpELTTPCGSAEYMAPEVVEvftdeATFYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
41-229 2.75e-17

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 82.40  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESESERK-----AFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05605   7 VLGKGGFGEVCACQVRAtgKMYACKKLEKKRIKKrkgeaMALNEKQILEKVNSRFVVSLAYAyeTKDALCLVLTIMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPlPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMT--NN 189
Cdd:cd05605  87 LKFHIYNMGN-PGFEEERAVFYAAEITCGLEHLHS---ERIVYRDLKPENILLDDHGHV-RISDLGLAVEIPEGETirGR 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21735562 190 KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05605 162 VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPF 201
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
37-229 3.73e-17

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 82.17  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACLNPVC--LVMEYAE 108
Cdd:PLN00009   5 EKVEKIGEGTYGVVYKARDRVTNetIALKKIRLEQEDEGVpstaIREISLLKEMQHGNIVRLQDVVHSEKRlyLVFEYLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  109 ggslYNVLHGAEPLPYYTAAHAM--SWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTA----CDI 182
Cdd:PLN00009  85 ----LDLKKHMDSSPDFAKNPRLikTYLYQILRGIAYCHSHR---VLHRDLKPQNLLIDRRTNALKLADFGLArafgIPV 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 21735562  183 QTHmTNNKGSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PLN00009 158 RTF-THEVVTLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLF 204
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
37-279 3.85e-17

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 81.47  E-value: 3.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKDV--AIKQIESESERKAFIVELRQ-LSRVNHPNIVKL--YGACLNPVCLVMEYAEGGS 111
Cdd:cd14107   5 EVKEEIGRGTFGFVKRVTHKGNGEccAAKFIPLRSSTRARAFQERDiLARLSHRRLTCLldQFETRKTLILILELCSSEE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTV-LKICDFGTACDIQT--HMTN 188
Cdd:cd14107  85 LLDRLFLKGVV---TEAEVKLYIQQVLEGIGYLHGMN---ILHLDIKPDNILMVSPTREdIKICDFGFAQEITPseHQFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeiGGPAFR-IMWAVHNGT---RPPLIKNLPKPIESLMT 264
Cdd:cd14107 159 KYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPF---AGENDRaTLLNVAEGVvswDTPEITHLSEDAKDFIK 235
                       250
                ....*....|....*
gi 21735562 265 RCWSKDPSQRPSMEE 279
Cdd:cd14107 236 RVLQPDPEKRPSASE 250
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
42-282 4.05e-17

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 81.76  E-value: 4.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVcKAKWRA--------KDVAIKQIES-----ESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEY 106
Cdd:cd14076   9 LGEGEFGKV-KLGWPLpkanhrsgVQVAIKLIRRdtqqeNCQTSKIMREINILKGLTHPNIVRLLDVLKTKkyIGIVLEF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkICDFGTAC----DI 182
Cdd:cd14076  88 VSGGELFDYILARRRLKDSVACRLFA---QLISGVAYLHK---KGVVHRDLKLENLLLDKNRNLV-ITDFGFANtfdhFN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKGSAAWMAPE-VFEGSNYS-EKCDVFSWGIILWEVITRRKPFDE-----IGGPAFRIMWAVHNG--TRPPLIK 253
Cdd:cd14076 161 GDLMSTSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDdphnpNGDNVPRLYRYICNTplIFPEYVT 240
                       250       260
                ....*....|....*....|....*....
gi 21735562 254 NLPKpieSLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14076 241 PKAR---DLLRRILVPNPRKRIRLSAIMR 266
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
37-279 4.36e-17

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 82.20  E-value: 4.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIE------------SESERKAFIVELRQlsrvnHPNIVKLYGACLNPVCL 102
Cdd:cd14094   6 ELCEVIGKGPFSVVrrCIHRETGQQFAVKIVDvakftsspglstEDLKREASICHMLK-----HPHIVELLETYSSDGML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VM--EYAEGGSL-YNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDFG 177
Cdd:cd14094  81 YMvfEFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHD---NNIIHRDVKPHCVLLASKENSapVKLGGFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQ--THMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKN 254
Cdd:cd14094 158 VAIQLGesGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH 237
                       250       260
                ....*....|....*....|....*
gi 21735562 255 LPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14094 238 ISESAKDLVRRMLMLDPAERITVYE 262
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
40-282 5.48e-17

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 81.18  E-value: 5.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFG--VVCKAKWRAKDVAIKQIESE--SERKafiVELRQLSRvNHPNIVKL---YGACLNPV-CL--VMEYAEG 109
Cdd:cd14089   7 QVLGLGINGkvLECFHKKTGEKFALKVLRDNpkARRE---VELHWRAS-GCPHIVRIidvYENTYQGRkCLlvVMECMEG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVL--HGAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGG--TVLKICDFGTACDIQTH 185
Cdd:cd14089  83 GELFSRIqeRADSAFTEREAAEIMR---QIGSAVAHLHSMN---IAHRDLKPENLLYSSKGpnAILKLTDFGFAKETTTK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 --MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF------RIM----------WAVHNGT 247
Cdd:cd14089 157 ksLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmkkRIRngqyefpnpeWSNVSEE 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 248 RPPLIKNLpkpiesLMTrcwskDPSQRPSMEEIVK 282
Cdd:cd14089 237 AKDLIRGL------LKT-----DPSERLTIEEVMN 260
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-282 6.23e-17

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 81.58  E-value: 6.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIESE--SERKAFIVELRQLSRVNHPNIVKL---YGACLNpVCLVMEYAEGGSL 112
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRStgKLYALKCIKKSplSRDSSLENEIAVLKRIKHENIVTLediYESTTH-YYLVMQLVSGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YN-VLHGAeplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVA--GGTVLKICDFGTAcDIQTH--MT 187
Cdd:cd14166  88 FDrILERG----VYTEKDASRVINQVLSAVKYLHE---NGIVHRDLKPENLLYLTpdENSKIMITDFGLS-KMEQNgiMS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRC 266
Cdd:cd14166 160 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFyEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHL 239
                       250
                ....*....|....*.
gi 21735562 267 WSKDPSQRPSMEEIVK 282
Cdd:cd14166 240 LEKNPSKRYTCEKALS 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
37-279 6.73e-17

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 81.20  E-value: 6.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIE----SESERKAFIVELRQ----LSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd14195   8 EMGEELGSGQFAIVrkCREKGTGKEYAAKFIKkrrlSSSRRGVSREEIERevniLREIQHPNIITLHDIFENKtdVVLIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV---LKICDFGTACD 181
Cdd:cd14195  88 ELVSGGELFDFLAEKESL---TEEEATQFLKQILDGVHYLHS---KRIAHFDLKPENIMLLDKNVPnprIKLIDFGIAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQ--THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLPKP 258
Cdd:cd14195 162 IEagNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlGETKQETLTNISAVNYDFDEEYFSNTSEL 241
                       250       260
                ....*....|....*....|.
gi 21735562 259 IESLMTRCWSKDPSQRPSMEE 279
Cdd:cd14195 242 AKDFIRRLLVKDPKKRMTIAQ 262
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-282 6.86e-17

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 81.63  E-value: 6.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEI-EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLV 103
Cdd:cd14168   7 DIKKIfEFKEVLGTGAFSEVVLAEERAtgKLFAVKCIPKKAlkgKESSIENEIAVLRKIKHENIVALEDIYESPnhLYLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYN--VLHGaeplpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVA--GGTVLKICDFGTA 179
Cdd:cd14168  87 MQLVSGGELFDriVEKG-----FYTEKDASTLIRQVLDAVYYLHRM---GIVHRDLKPENLLYFSqdEESKIMISDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTH--MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNGTRPPLIKNLP 256
Cdd:cd14168 159 KMEGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKADYEFDSPYWDDIS 238
                       250       260
                ....*....|....*....|....*.
gi 21735562 257 KPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14168 239 DSAKDFIRNLMEKDPNKRYTCEQALR 264
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
34-292 8.70e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 83.16  E-value: 8.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   34 KEIEVEEVVGRGAFGVVCKAKW--RAKDVAIKQIESESERKAfiVELRQLSRVNHPNIVKL----YGACLNP------VC 101
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICidTSEKVAIKKVLQDPQYKN--RELLIMKNLNHINIIFLkdyyYTECFKKneknifLN 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  102 LVMEYaeggsLYNVLHgaEPLPYYTAA-HAMSWCL------QCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKIC 174
Cdd:PTZ00036 144 VVMEF-----IPQTVH--KYMKHYARNnHALPLFLvklysyQLCRALAYIHS---KFICHRDLKPQNLLIDPNTHTLKLC 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  175 DFGTAcdiqTHMTNNKGSAAWM------APEVFEGS-NYSEKCDVFSWGIILWEVItrrkpfdeIGGPAFRIMWAVHNGT 247
Cdd:PTZ00036 214 DFGSA----KNLLAGQRSVSYIcsrfyrAPELMLGAtNYTTHIDLWSLGCIIAEMI--------LGYPIFSGQSSVDQLV 281
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21735562  248 RppLIKNLPKPIESLMTR------------CWSKD-----PSQRPsmEEIVKIMTHLMRYFP 292
Cdd:PTZ00036 282 R--IIQVLGTPTEDQLKEmnpnyadikfpdVKPKDlkkvfPKGTP--DDAINFISQFLKYEP 339
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
42-223 8.78e-17

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 81.85  E-value: 8.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK--WRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLNP---VCLVMEYaEGGSL 112
Cdd:cd07856  18 VGMGAFGLVCSARdqLTGQNVAVKKImkpfSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPledIYFVTEL-LGTDL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHgAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGS 192
Cdd:cd07856  97 HRLLT-SRPLEKQFIQYFL---YQILRGLKYVHS---AGVIHRDLKPSNIL-VNENCDLKICDFGLARIQDPQMTGYVST 168
                       170       180       190
                ....*....|....*....|....*....|..
gi 21735562 193 AAWMAPEV-FEGSNYSEKCDVFSWGIILWEVI 223
Cdd:cd07856 169 RYYRAPEImLTWQKYDVEVDIWSAGCIFAEML 200
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
37-280 9.07e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 80.36  E-value: 9.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKwRAKD---VAIKQIESESERK-----------AFIVELRQLSRVNHPNIVKLYGACLNP--V 100
Cdd:cd14005   3 EVGDLLGKGGFGTVYSGV-RIRDglpVAVKFVPKSRVTEwamingpvpvpLEIALLLKASKPGVPGVIRLLDWYERPdgF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGG-SLYNVLHGAEPLPYYTAAHAMSwclqcsQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTA 179
Cdd:cd14005  82 LLIMERPEPCqDLFDFITERGALSENLARIIFR------QVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFGCG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 CDIQTHM-TNNKGSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRKPF--DEiggpaFRIMWAVHngTRPplikNL 255
Cdd:cd14005 156 ALLKDSVyTDFDGTRVYSPPEWIrHGRYHGRPATVWSLGILLYDMLCGDIPFenDE-----QILRGNVL--FRP----RL 224
                       250       260
                ....*....|....*....|....*
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14005 225 SKECCDLISRCLQFDPSKRPSLEQI 249
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
35-222 9.75e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 80.81  E-value: 9.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEY 106
Cdd:cd07848   2 KFEVLGVVGEGAYGVVlkCRHKETKEIVAIKKFkdseENEEVKETTLRELKMLRTLKQENIVELKEAFRRrgKLYLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGgslyNVLHGAEPLPYYTAAHAM-SWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQ-- 183
Cdd:cd07848  82 VEK----NMLELLEEMPNGVPPEKVrSYIYQLIKAIHWCHKND---IVHRDIKPENLL-ISHNDVLKLCDFGFARNLSeg 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21735562 184 --THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEV 222
Cdd:cd07848 154 snANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGEL 194
pknD PRK13184
serine/threonine-protein kinase PknD;
42-229 1.05e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 84.05  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   42 VGRGAFG-------VVCKAKwrakdVAIKQI-----ESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYA 107
Cdd:PRK13184  10 IGKGGMGevylaydPVCSRR-----VALKKIredlsENPLLKKRFLREAKIAADLIHPGIVPVYSICSdgDPVYYTMPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  108 EGGSLYNVLHG-------AEPLPYYTAAHA-MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLkICDFGTA 179
Cdd:PRK13184  85 EGYTLKSLLKSvwqkeslSKELAEKTSVGAfLSIFHKICATIEYVHS---KGVLHRDLKPDNILLGLFGEVV-ILDWGAA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562  180 ----------CDIQTHMTNNK-----------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PRK13184 161 ifkkleeedlLDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
41-223 1.11e-16

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 81.69  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKA--KWRAKDVAIKQIE-----SESERKAFiVELRQLSRVNHPNIVKLYGAC--------LNPVCLVME 105
Cdd:cd07850   7 PIGSGAQGIVCAAydTVTGQNVAIKKLSrpfqnVTHAKRAY-RELVLMKLVNHKNIIGLLNVFtpqksleeFQDVYLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGgSLYNVLHgaEPLPYYTaahaMSWCL-QCSQGVAYLHSmqpKALIHRDLKPPNLLlVAGGTVLKICDFGTA--CDI 182
Cdd:cd07850  86 LMDA-NLCQVIQ--MDLDHER----MSYLLyQMLCGIKHLHS---AGIIHRDLKPSNIV-VKSDCTLKILDFGLArtAGT 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21735562 183 QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVI 223
Cdd:cd07850 155 SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMI 195
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
37-282 1.31e-16

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 81.05  E-value: 1.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA---KwRAKDVAIKQIESeseRKAF----IVELRQLSRVNH------PNIVKLYGACL--NPVC 101
Cdd:cd14210  16 EVLSVLGKGSFGQVVKCldhK-TGQLVAIKIIRN---KKRFhqqaLVEVKILKHLNDndpddkHNIVRYKDSFIfrGHLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAeGGSLYNVL--HGAEPLPYYTAAhamSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGG-TVLKICDFGT 178
Cdd:cd14210  92 IVFELL-SINLYELLksNNFQGLSLSLIR---KFAKQILQALQFLHKLN---IIHCDLKPENILLKQPSkSSIKVIDFGS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 AC--------DIQthmtnnkgSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT-------------------------- 224
Cdd:cd14210 165 SCfegekvytYIQ--------SRFYRAPEVILGLPYDTAIDMWSLGCILAELYTgyplfpgeneeeqlacimevlgvppk 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21735562 225 --------RRKPFDEIGGPafRIMWAVHNGTRPPLIKNL-------PKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14210 237 slidkasrRKKFFDSNGKP--RPTTNSKGKKRRPGSKSLaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQ 307
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
21-276 1.62e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 81.41  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   21 APSQVLNFEEIDYKEIeveevVGRGAFGVVCKAKWR--AKDVAIKQI---ESESERKAFIVELRQLSRVNHPNIVKLYGA 95
Cdd:PLN00034  66 APSAAKSLSELERVNR-----IGSGAGGTVYKVIHRptGRLYALKVIygnHEDTVRRQICREIEILRDVNHPNVVKCHDM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   96 CLN--PVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSwclqcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKI 173
Cdd:PLN00034 141 FDHngEIQVLLEFMDGGSLEGTHIADEQFLADVARQILS-------GIAYLHR---RHIVHRDIKPSNLLINSAKNV-KI 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  174 CDFGTACDIQTHM---TNNKGSAAWMAPE-----VFEGSNYSEKCDVFSWGIILWEVITRRKPFDeIG--GPAFRIMWAV 243
Cdd:PLN00034 210 ADFGVSRILAQTMdpcNSSVGTIAYMSPErintdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFG-VGrqGDWASLMCAI 288
                        250       260       270
                 ....*....|....*....|....*....|...
gi 21735562  244 HNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPS 276
Cdd:PLN00034 289 CMSQPPEAPATASREFRHFISCCLQREPAKRWS 321
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
37-281 1.72e-16

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 80.16  E-value: 1.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA---KDVAIKQIE------SESERKAFIVE-LRQLSRVNHPNIVKL-----YGACLNpvc 101
Cdd:cd14052   3 ANVELIGSGEFSQVYKVSERVptgKVYAVKKLKpnyagaKDRLRRLEEVSiLRELTLDGHDNIVQLidsweYHGHLY--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSL-----YNVLHGA-EPlpyytaahAMSW--CLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKI 173
Cdd:cd14052  80 IQTELCENGSLdvflsELGLLGRlDE--------FRVWkiLVELSLGLRFIHDHH---FVHLDLKPANVLITFEGT-LKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFG--TACDIQThMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT--------------RRKPFDEIGG--- 234
Cdd:cd14052 148 GDFGmaTVWPLIR-GIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvlpdngdawqklRSGDLSDAPRlss 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 21735562 235 --PAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14052 227 tdLHSASSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVL 275
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
37-229 1.85e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 80.06  E-value: 1.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKDV--AIKQIESESERKAFIVELrQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSL 112
Cdd:cd14178   6 EIKEDIGIGSYSVCKRCVHKATSTeyAVKIIDKSKRDPSEEIEI-LLRYGQHPNIITLKDVYDDGkfVYLVMELMRGGEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV---AGGTVLKICDFGTACDIQTH---- 185
Cdd:cd14178  85 LDRILRQK---CFSEREASAVLCTITKTVEYLHS---QGVVHRDLKPSNILYMdesGNPESIRICDFGFAKQLRAEngll 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 186 MTNNKgSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14178 159 MTPCY-TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
42-229 1.95e-16

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 80.98  E-value: 1.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWR--AKDVAIKQIESESER--KAFIVELRQLSRVNHPNIVKLYGAC----------------LNPVC 101
Cdd:cd07854  13 LGCGSNGLVFSAVDSdcDKRVAVKKIVLTDPQsvKHALREIKIIRRLDHDNIVKVYEVLgpsgsdltedvgslteLNSVY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGgSLYNVL-HGaePLPyytAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLKICDFGTAC 180
Cdd:cd07854  93 IVQEYMET-DLANVLeQG--PLS---EEHARLFMYQLLRGLKYIHSAN---VLHRDLKPANVFINTEDLVLKIGDFGLAR 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 181 DIQTH------MTNNKGSAAWMAPE-VFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07854 164 IVDPHyshkgyLSEGLVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLF 219
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
37-229 2.16e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 80.83  E-value: 2.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVELrQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSL 112
Cdd:cd14176  22 EVKEDIGVGSYSVCkrCIHKATNMEFAVKIIDKSKRDPTEEIEI-LLRYGQHPNIITLKDVYDDgkYVYVVTELMKGGEL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV---AGGTVLKICDFGTACDIQTH---M 186
Cdd:cd14176 101 LDKILRQK---FFSEREASAVLFTITKTVEYLHA---QGVVHRDLKPSNILYVdesGNPESIRICDFGFAKQLRAEnglL 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14176 175 MTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF 217
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
30-229 2.21e-16

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 80.79  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   30 EIDYKEIEVEEVVGRGAFGVVCKAKWRAKD---VAIKQIES-----ESERKAFIVELRQLSRVNHPNIVKLYGACLNP-- 99
Cdd:PTZ00426  26 KMKYEDFNFIRTLGTGSFGRVILATYKNEDfppVAIKRFEKskiikQKQVDHVFSERKILNYINHPFCVNLYGSFKDEsy 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  100 VCLVMEYAEGGSLYNVLHGAEPLPYYTAahamswCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGtVLKICDFGTA 179
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNKRFPNDVG------CFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDG-FIKMTDFGFA 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 21735562  180 CDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PTZ00426 179 KVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
42-229 2.33e-16

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 79.79  E-value: 2.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRA-------KDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL--VMEYAEGGSL 112
Cdd:cd05612   9 IGTGTFGRVHLVRDRIsehyyalKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLymLMEYVPGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPlpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFGTACDIQTHMTNNKGS 192
Cdd:cd05612  89 FSYLRNSGR---FSNSTGLFYASEIVCALEYLHS---KEIVYRDLKPENILLDKEGH-IKLTDFGFAKKLRDRTWTLCGT 161
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05612 162 PEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPF 198
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
37-229 2.34e-16

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 79.45  E-value: 2.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIES-------------ESERKAFIvelrqLSRVNHPNIVKLYGACLN--P 99
Cdd:cd14105   8 DIGEELGSGQFAVVkkCREKSTGLEYAAKFIKKrrskasrrgvsreDIEREVSI-----LRQVLHPNIITLHDVFENktD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 VCLVMEYAEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTV---LKICDF 176
Cdd:cd14105  83 VVLILELVAGGELFDFLAEKESL---SEEEATEFLKQILDGVNYLHTKN---IAHFDLKPENIMLLDKNVPiprIKLIDF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 177 GTACDIQ--THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14105 157 GLAHKIEdgNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
37-282 2.40e-16

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 79.67  E-value: 2.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKW--RAKDVAIKQIE-SESERKAFIVELRQLSRVNH-PNIVKLYGACL--------NPVCLVM 104
Cdd:cd06636  19 ELVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDvTEDEEEEIKLEINMLKKYSHhRNIATYYGAFIkksppghdDQLWLVM 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGaeplpyyTAAHAMS--W----CLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd06636  99 EFCGAGSVTDLVKN-------TKGNALKedWiayiCREILRGLAHLHAHK---VIHRDIKGQNVLLTENAEV-KLVDFGV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDIQTHMTNNK---GSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTRPP 250
Cdd:cd06636 168 SAQLDRTVGRRNtfiGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMH--PMRALFLIPRNPPPK 245
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 251 L-IKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06636 246 LkSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLK 278
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
39-229 2.80e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 79.69  E-value: 2.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  39 EEVVGRGAFGVV--CKAKWRAKDVAIKQIESES--ERKAFIVELRQLSRVN-HPNIVKL--YGACLNPVCLVMEYAEGGS 111
Cdd:cd14173   7 EEVLGEGAYARVqtCINLITNKEYAVKIIEKRPghSRSRVFREVEMLYQCQgHRNVLELieFFEEEDKFYLVFEKMRGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDFGTACDIQTH---- 185
Cdd:cd14173  87 ILSHIHRRR---HFNELEASVVVQDIASALDFLHN---KGIAHRDLKPENILCEHPNQVspVKICDFDLGSGIKLNsdcs 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 186 ------MTNNKGSAAWMAPEVFEGSN-----YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14173 161 pistpeLLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
34-240 2.93e-16

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 80.81  E-value: 2.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIES----ESERKAFIVELRQ-LSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVqlVRHKASQKVYAMKLLSKfemiKRSDSAFFWEERDiMAFANSPWVVQLFCAFQDDkyLYMVM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEpLP-----YYTAAHAMSwclqcsqgVAYLHSMqpkALIHRDLKPPNLLLVAGGTvLKICDFGTA 179
Cdd:cd05621 132 EYMPGGDLVNLMSNYD-VPekwakFYTAEVVLA--------LDAIHSM---GLIHRDVKPDNMLLDKYGH-LKLADFGTC 198
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 180 CDIQ----THMTNNKGSAAWMAPEVFEGSN----YSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIM 240
Cdd:cd05621 199 MKMDetgmVHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFyaDSLVGTYSKIM 269
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
81-282 4.14e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 78.29  E-value: 4.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  81 LSRVNHPNIVKLYGACL-NPVCLVMEYAEGGSLYNVLHGAEPLPyytaahAMSWCLQCSQGVAY-LHSMQPKALIHRDLK 158
Cdd:cd05037  56 MSQISHKHLVKLYGVCVaDENIMVQEYVRYGPLDKYLRRMGNNV------PLSWKLQVAKQLASaLHYLEDKKLIHGNVR 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 159 PPNLLLV---AGGTVL--KICDFGTA-CDIQTHMTNNKgsAAWMAPEVFEG--SNYSEKCDVFSWGIILWEVITR-RKPF 229
Cdd:cd05037 130 GRNILLAregLDGYPPfiKLSDPGVPiTVLSREERVDR--IPWIAPECLRNlqANLTIAADKWSFGTTLWEICSGgEEPL 207
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 230 DEIGGPAFRIMWAVHNGTRPPLIknlpKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05037 208 SALSSQEKLQFYEDQHQLPAPDC----AELAELIMQCWTYEPTKRPSFRAILR 256
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
40-286 4.16e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 79.71  E-value: 4.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQIeseseRKAFIV----------ELRQLSRVNHPNIVKLYGACLNP--VCLVME 105
Cdd:cd05571   1 KVLGKGTFGKVilCREKATGELYAIKIL-----KKEVIIakdevahtltENRVLQNTRHPFLTSLKYSFQTNdrLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHG----AEPLPYYTAAHAMSwclqcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaC- 180
Cdd:cd05571  76 YVNGGELFFHLSRervfSEDRTRFYGAEIVL-------ALGYLHS---QGIVYRDLKLENLLLDKDGHI-KITDFGL-Ck 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 -DIQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF--------------DEIGGPafrimwav 243
Cdd:cd05571 144 eEISYGATTKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynrdhevlfelilmEEVRFP-------- 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21735562 244 hngtrppliKNLPKPIESLMTRCWSKDPSQR--PSMEEIVKIMTH 286
Cdd:cd05571 216 ---------STLSPEAKSLLAGLLKKDPKKRlgGGPRDAKEIMEH 251
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
41-274 4.53e-16

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 79.54  E-value: 4.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWR--AKDVAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGS 111
Cdd:cd05585   1 VIGKGSFGKVMQVRKKdtSRIYALKTIRkahivSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPekLYLVLAFINGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEPLP-----YYTAAHAMSwcLQCsqgvayLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTaCDI---Q 183
Cdd:cd05585  81 LFHHLQREGRFDlsrarFYTAELLCA--LEC------LHKFN---VIYRDLKPENILLDYTGHI-ALCDFGL-CKLnmkD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 THMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMwavhngTRPPLI--KNLPKPI 259
Cdd:cd05585 148 DDKTNTfCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFyDENTNEMYRKI------LQEPLRfpDGFDRDA 221
                       250
                ....*....|....*
gi 21735562 260 ESLMTRCWSKDPSQR 274
Cdd:cd05585 222 KDLLIGLLNRDPTKR 236
PHA02988 PHA02988
hypothetical protein; Provisional
52-280 5.67e-16

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 78.63  E-value: 5.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   52 KAKWRAKDVAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPV------CLVMEYAEGGSLYNVLHGAE 120
Cdd:PHA02988  38 KGIFNNKEVIIRtfkkfHKGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIVddlprlSLILEYCTRGYLREVLDKEK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  121 PLPYYTAAHAMswcLQCSQGVAYLHSMQPKAliHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEV 200
Cdd:PHA02988 118 DLSFKTKLDMA---IDCCKGLYNLYKYTNKP--YKNLTSVSFL-VTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKM 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  201 FEG--SNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRpPLIKNLPKPIESLMTRCWSKDPSQRPSME 278
Cdd:PHA02988 192 LNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKEIYDLIINKNNSL-KLPLDCPLEIKCIVEACTSHDSIKRPNIK 270

                 ..
gi 21735562  279 EI 280
Cdd:PHA02988 271 EI 272
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
37-282 7.47e-16

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 78.23  E-value: 7.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQ-IESESE---RKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAE 108
Cdd:cd07846   4 ENLGLVGEGSYGMVmkCRHKETGQIVAIKKfLESEDDkmvKKIAMREIKMLKQLRHENLVNLIEVFRRKkrWYLVFEFVD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDI---QTH 185
Cdd:cd07846  84 HTVLDDLEKYPNGLDESRVRKYL---FQILRGIDFCHSHN---IIHRDIKPENILVSQSG-VVKLCDFGFARTLaapGEV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAAWMAPEVFEG-SNYSEKCDVFSWGIILWEVITRRK--PFDEIGGPAFRIMWAVHN----------------G 246
Cdd:cd07846 157 YTDYVATRWYRAPELLVGdTKYGKAVDVWAVGCLVTEMLTGEPlfPGDSDIDQLYHIIKCLGNliprhqelfqknplfaG 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 247 TRPPLIKNlPKPIE-----------SLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd07846 237 VRLPEVKE-VEPLErrypklsgvviDLAKKCLHIDPDKRPSCSELLH 282
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
41-230 7.82e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 78.60  E-value: 7.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFG-VVCKAKWRAKDV----AIKQIESES----ERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd05582   2 VLGQGSFGkVFLVRKITGPDAgtlyAMKVLKKATlkvrDRVRTKMERDILADVNHPFIVKLHYAFQTEgkLYLILDFLRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYN-----VLHGAEPLPYYTAAHAMswclqcsqGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFG---TACD 181
Cdd:cd05582  82 GDLFTrlskeVMFTEEDVKFYLAELAL--------ALDHLHSL---GIIYRDLKPENILLDEDGHI-KLTDFGlskESID 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21735562 182 IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd05582 150 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQ 198
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
27-274 8.11e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 78.89  E-value: 8.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  27 NFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGACLNP 99
Cdd:cd05615   3 NLDRVRLTDFNFLMVLGKGSFGKVMLAERKGSDelYAIKILKkdvviQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 V---CLVMEYAEGGSLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDF 176
Cdd:cd05615  83 VdrlYFVMEYVNGGDL---MYHIQQVGKFKEPQAVFYAAEISVGLFFLHK---KGIIYRDLKLDNVMLDSEGHI-KIADF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTAcdiQTHMTNNK------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD-EIGGPAFRIMWAvHNGTRP 249
Cdd:cd05615 156 GMC---KEHMVEGVttrtfcGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDgEDEDELFQSIME-HNVSYP 231
                       250       260
                ....*....|....*....|....*
gi 21735562 250 pliKNLPKPIESLMTRCWSKDPSQR 274
Cdd:cd05615 232 ---KSLSKEAVSICKGLMTKHPAKR 253
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
16-293 9.44e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 78.92  E-value: 9.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  16 GEMIEAPSQVLNFEEIDYK----EIEVEEVVGRGAFG--VVCKAKWRAKDVAIKQIESE-----SERKAFIVELRQLSRV 84
Cdd:cd05594   3 SDNSGAEEMEVSLTKPKHKvtmnDFEYLKLLGKGTFGkvILVKEKATGRYYAMKILKKEvivakDEVAHTLTENRVLQNS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  85 NHPNIVKLYGA--CLNPVCLVMEYAEGGSLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqPKALIHRDLKPPNL 162
Cdd:cd05594  83 RHPFLTALKYSfqTHDRLCFVMEYANGGELFFHLSRER---VFSEDRARFYGAEIVSALDYLHS--EKNVVYRDLKLENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 163 LLVAGGTVlKICDFGTACD-IQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFR 238
Cdd:cd05594 158 MLDKDGHI-KITDFGLCKEgIKDGATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDHEKLFE 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 239 IMwaVHNGTRPPliKNLPKPIESLMTRCWSKDPSQR--PSMEEIVKIMTHlmRYFPG 293
Cdd:cd05594 237 LI--LMEEIRFP--RTLSPEAKSLLSGLLKKDPKQRlgGGPDDAKEIMQH--KFFAG 287
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
37-282 9.68e-16

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 78.22  E-value: 9.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKW--RAKDVAIKQIE----SESERKAFIVELRQLSrvNHPNIVKLYGACL--NP------VCL 102
Cdd:cd06637   9 ELVELVGNGTYGQVYKGRHvkTGQLAAIKVMDvtgdEEEEIKQEINMLKKYS--HHRNIATYYGAFIkkNPpgmddqLWL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGaeplpyyTAAHAM--SW----CLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDF 176
Cdd:cd06637  87 VMEFCGAGSVTDLIKN-------TKGNTLkeEWiayiCREILRGLSHLHQHK---VIHRDIKGQNVLLTENAEV-KLVDF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 177 GTACDIQTHMTNNK---GSAAWMAPEVFE-----GSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpAFRIMWAVHNGTR 248
Cdd:cd06637 156 GVSAQLDRTVGRRNtfiGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMH--PMRALFLIPRNPA 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 249 PPL-IKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd06637 234 PRLkSKKWSKKFQSFIESCLVKNHSQRPSTEQLMK 268
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
41-229 1.06e-15

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 78.17  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKA----KWRAKDVAIKQI-------ESESERKAFIVELRQLSRVNHPNIVKLY---GACLNPVCLVMEY 106
Cdd:cd14040  13 LLGRGGFSEVYKAfdlyEQRYAAVKIHQLnkswrdeKKENYHKHACREYRIHKELDHPRIVKLYdyfSLDTDTFCTVLEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTV--LKICDFGTA----- 179
Cdd:cd14040  93 CEGNDLDFYLKQHKLM---SEKEARSIVMQIVNALRYLNEIKP-PIIHYDLKPGNILLVDGTACgeIKITDFGLSkimdd 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 180 ----CDIQTHMTNNKGSAAWMAPEVF----EGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14040 169 dsygVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF 226
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
34-240 1.07e-15

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 79.28  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIES----ESERKAFIVELRQ-LSRVNHPNIVKLYGACLNP--VCLVM 104
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVqlVRHKSTRKVYAMKLLSKfemiKRSDSAFFWEERDiMAFANSPWVVQLFYAFQDDryLYMVM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEpLP-----YYTAAHAMSwclqcsqgVAYLHSMqpkALIHRDLKPPNLLLVAGGTvLKICDFGTA 179
Cdd:cd05622 153 EYMPGGDLVNLMSNYD-VPekwarFYTAEVVLA--------LDAIHSM---GFIHRDVKPDNMLLDKSGH-LKLADFGTC 219
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 180 cdiqthMTNNK----------GSAAWMAPEVFEGSN----YSEKCDVFSWGIILWEVITRRKPF--DEIGGPAFRIM 240
Cdd:cd05622 220 ------MKMNKegmvrcdtavGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFyaDSLVGTYSKIM 290
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
42-224 1.23e-15

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 77.41  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKDVAIKQ-IESESE---RKAFIVELRQLSRVNHPNIV----------KLYgaclnpvcLVME 105
Cdd:cd07847   9 IGEGSYGVVfkCRNRETGQIVAIKKfVESEDDpviKKIALREIRMLKQLKHPNLVnlievfrrkrKLH--------LVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEggslYNVLHGAEPLPYYTAAHA-MSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKICDFGTACDIQT 184
Cdd:cd07847  81 YCD----HTVLNELEKNPRGVPEHLiKKIIWQTLQAVNFCHKHN---CIHRDVKPENILITKQG-QIKLCDFGFARILTG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 185 ---HMTNNKGSAAWMAPEVFEG-SNYSEKCDVFSWGIILWEVIT 224
Cdd:cd07847 153 pgdDYTDYVATRWYRAPELLVGdTQYGPPVDVWAIGCVFAELLT 196
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
40-289 1.26e-15

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 77.77  E-value: 1.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDVAIKQI---ESESERKAFivELRQLSRVNHPNIVKLYGA------CLNPVCLVMEYAEGG 110
Cdd:cd14141   1 EIKARGRFGCVWKAQLLNEYVAVKIFpiqDKLSWQNEY--EIYSLPGMKHENILQFIGAekrgtnLDVDLWLITAFHEKG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNvlhgaeplpyYTAAHAMSWCLQC------SQGVAYLHSMQP-------KALIHRDLKPPNLLLVAGGTVLkICDFG 177
Cdd:cd14141  79 SLTD----------YLKANVVSWNELChiaqtmARGLAYLHEDIPglkdghkPAIAHRDIKSKNVLLKNNLTAC-IADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQ-------THmtNNKGSAAWMAPEVFEGS-NYSE----KCDVFSWGIILWEVITR-----------RKPFDEIGG 234
Cdd:cd14141 148 LALKFEagksagdTH--GQVGTRRYMAPEVLEGAiNFQRdaflRIDMYAMGLVLWELASRctasdgpvdeyMLPFEEEVG 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 235 --PAFRIMW--AVHNGTRPPLIKNLPKPIESLM-----TRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:cd14141 226 qhPSLEDMQevVVHKKKRPVLRECWQKHAGMAMlcetiEECWDHDAEARLSAGCVEERIIQMQR 289
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
60-224 1.28e-15

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 80.66  E-value: 1.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562     60 VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCL---VMEYAEGGSLYNVLHGAEPLPYYTAAHAM 131
Cdd:TIGR03903    6 VAIKllrtdAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLlfaVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    132 swcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVA--GGTVLKICDFGT--------ACDIQ--THMTNNKGSAAWMAPE 199
Cdd:TIGR03903   86 ---LQVLDALACAHN---QGIVHRDLKPQNIMVSQtgVRPHAKVLDFGIgtllpgvrDADVAtlTRTTEVLGTPTYCAPE 159
                          170       180
                   ....*....|....*....|....*
gi 21735562    200 VFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLT 184
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
41-274 1.32e-15

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 78.12  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKD--VAIKQIE-----SESERKAFIVELRQLSRVNHPNIVKLYGAC---LNPVCLVMEYAEGG 110
Cdd:cd05616   7 VLGKGSFGKVMLAERKGTDelYAVKILKkdvviQDDDVECTMVEKRVLALSGKPPFLTQLHSCfqtMDRLYFVMEYVNGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK 190
Cdd:cd05616  87 DL---MYHIQQVGRFKEPHAVFYAAEIAIGLFFLQS---KGIIYRDLKLDNVMLDSEGHI-KIADFGMCKENIWDGVTTK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD-EIGGPAFR-IMwaVHNGTRPpliKNLPKPIESLMTR 265
Cdd:cd05616 160 tfcGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEgEDEDELFQsIM--EHNVAYP---KSMSKEAVAICKG 234

                ....*....
gi 21735562 266 CWSKDPSQR 274
Cdd:cd05616 235 LMTKHPGKR 243
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
37-295 1.40e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 77.45  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA--KDVAIKQIESES-----ERKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYA 107
Cdd:cd05609   3 ETIKLISNGAYGAVYLVRHREtrQRFAMKKINKQNlilrnQIQQVFVERDILTFAENPFVVSMYCSfeTKRHLCMVMEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLP-----YYTAAHAMswclqcsqGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTA--- 179
Cdd:cd05609  83 EGGDCATLLKNIGPLPvdmarMYFAETVL--------ALEYLHSY---GIVHRDLKPDNLLITSMGHI-KLTDFGLSkig 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 180 ------------CDIQTHMTNNK---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-----DEIGGPAFR- 238
Cdd:cd05609 151 lmslttnlyeghIEKDTREFLDKqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpEELFGQVISd 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 239 -IMWavhngtrPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHlmRYFPGAD 295
Cdd:cd05609 231 eIEW-------PEGDDALPDDAQDLITRLLQQNPLERLGTGGAEEVKQH--PFFQDLD 279
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
41-229 1.42e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 77.34  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESESERK-----AFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05631   7 VLGKGGFGEVCACQVRAtgKMYACKKLEKKRIKKrkgeaMALNEKRILEKVNSRFVVSLAYAyeTKDALCLVLTIMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L----YNVLHgaeplPYYTAAHAMSWCLQCSQGvayLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMT 187
Cdd:cd05631  87 LkfhiYNMGN-----PGFDEQRAIFYAAELCCG---LEDLQRERIVYRDLKPENILLDDRGHI-RISDLGLAVQIPEGET 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 188 --NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05631 158 vrGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
33-280 2.09e-15

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 76.40  E-value: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEiEVEEV-----VGRGAFGVVCKA-------KWRAKDVAIKQIESEserkafivELRQLSRVNHPNIVKLYGACLN-P 99
Cdd:cd13991   1 YRE-EVHWAthqlrIGRGSFGEVHRMedkqtgfQCAVKKVRLEVFRAE--------ELMACAGLTSPRVVPLYGAVREgP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 100 -VCLVMEYAEGGSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFGT 178
Cdd:cd13991  72 wVNIFMDLKEGGSLGQLIKEQGCLP---EDRALHYLGQALEGLEYLHS---RKILHGDVKADNVLLSSDGSDAFLCDFGH 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 179 ACDIQTH------MTNN--KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIggpaFRIMWAVHNGTRPP 250
Cdd:cd13991 146 AECLDPDglgkslFTGDyiPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQY----YSGPLCLKIANEPP 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 21735562 251 LIKNLPKPIESLMTRCWS----KDPSQRPSMEEI 280
Cdd:cd13991 222 PLREIPPSCAPLTAQAIQaglrKEPVHRASAAEL 255
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
35-229 2.51e-15

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 77.22  E-value: 2.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEE-VVGRGAFGVV--CKAKWRAKDVAIK----QIESESERKafIVELRQLSrvNHPNIVKLYGACLNP--VCLVME 105
Cdd:cd14180   6 ELDLEEpALGEGSFSVCrkCRHRQSGQEYAVKiisrRMEANTQRE--VAALRLCQ--SHPNIVALHEVLHDQyhTYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSmqpKALIHRDLKPPNLLLV--AGGTVLKICDFGTA---- 179
Cdd:cd14180  82 LLRGGELLDRIKKKARFSESEASQLMR---SLVSAVSFMHE---AGVVHRDLKPENILYAdeSDGAVLKVIDFGFArlrp 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21735562 180 ---CDIQTHMTnnkgSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14180 156 qgsRPLQTPCF----TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPF 204
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
32-229 2.63e-15

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 76.09  E-value: 2.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVEevVGRGAFGVVCKAKWRAKDV--AIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGAC--LNPVCLVMEY 106
Cdd:cd14108   2 DYYDIHKE--IGRGAFSYLRRVKEKSSDLsfAAKFIPVRAKKKTSARrELALLAELDHKSIVRFHDAFekRRVVIIVTEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGaeplPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGT-VLKICDFGTACDIQTH 185
Cdd:cd14108  80 CHEELLERITKR----PTVCESEVRSYMRQLLEGIEYLHQND---VLHLDLKPENLLMADQKTdQVRICDFGNAQELTPN 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 186 --MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14108 153 epQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPF 198
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
77-280 2.74e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 76.54  E-value: 2.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  77 ELRQLSRVNHPNIVKLYGACLNP----VCLVMEYAEGGSLYNVlHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaL 152
Cdd:cd14199  75 EIAILKKLDHPNVVKLVEVLDDPsedhLYMVFELVKQGPVMEV-PTLKPL---SEDQARFYFQDLIKGIEYLHYQK---I 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 153 IHRDLKPPNLLLVAGGTVlKICDFGTACDIQTH---MTNNKGSAAWMAPEVFEGS--NYSEKC-DVFSWGIILWEVITRR 226
Cdd:cd14199 148 IHRDVKPSNLLVGEDGHI-KIADFGVSNEFEGSdalLTNTVGTPAFMAPETLSETrkIFSGKAlDVWAMGVTLYCFVFGQ 226
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 227 KPF-DEiggpafRIMwAVHN--GTRP---PLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14199 227 CPFmDE------RIL-SLHSkiKTQPlefPDQPDISDDLKDLLFRMLDKNPESRISVPEI 279
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
42-227 3.21e-15

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 76.08  E-value: 3.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQIESESER------KAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGGSLY 113
Cdd:cd14160   1 IGEGEIFEVYRVRIGNRSYAVKLFKQEKKMqwkkhwKRFLSELEVLLLFQHPNILELAAYFTETekFCLVYPYMQNGTLF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLH---GAEPLPYYTAahaMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLvAGGTVLKICDFGTA----------C 180
Cdd:cd14160  81 DRLQchgVTKPLSWHER---INILIGIAKAIHYLHNSQPCTVICGNISSANILL-DDQMQPKLTDFALAhfrphledqsC 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 181 DIqtHMTNNKGSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRK 227
Cdd:cd14160 157 TI--NMTTALHKHLWYMPEEYiRQGKLSVKTDVYSFGIVIMEVLTGCK 202
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
34-287 3.90e-15

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 76.63  E-value: 3.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFI-VELRQLSRVNHPNIVKLYGACL------NPVCLVMEY 106
Cdd:cd14219   5 KQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFReTEIYQTVLMRHENILGFIAADIkgtgswTQLYLITDY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEplpyYTAAHAMSWCLQCSQGVAYLH----SMQPK-ALIHRDLKPPNLLLVAGGTVLkICDFGTAC- 180
Cdd:cd14219  85 HENGSLYDYLKSTT----LDTKAMLKLAYSSVSGLCHLHteifSTQGKpAIAHRDLKSKNILVKKNGTCC-IADLGLAVk 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 181 ------DIQTHMTNNKGSAAWMAPEVFEGS---NYSEK---CDVFSWGIILWEVITR----------RKPFDEI--GGPA 236
Cdd:cd14219 160 fisdtnEVDIPPNTRVGTKRYMPPEVLDESlnrNHFQSyimADMYSFGLILWEVARRcvsggiveeyQLPYHDLvpSDPS 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 237 FRIMWAVH--NGTRPPLIKNLP-----KPIESLMTRCWSKDPSQRPSMEEIVKIMTHL 287
Cdd:cd14219 240 YEDMREIVciKRLRPSFPNRWSsdeclRQMGKLMTECWAHNPASRLTALRVKKTLAKM 297
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
42-286 3.93e-15

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 75.44  E-value: 3.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKDVAIKQIESESER-KAFIVEL---RQLSrvNHPNIVKLYG-ACLNPVCLV--MEYAEGGSL 112
Cdd:cd13987   1 LGEGTYGKVllAVHKGSGTKMALKFVPKPSTKlKDFLREYnisLELS--VHPHIIKTYDvAFETEDYYVfaQEYAPYGDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPLPyytaAHAMSWCL-QCSQGVAYLHSmqpKALIHRDLKPPNLLLV-AGGTVLKICDFGTACDIQTHMTNNK 190
Cdd:cd13987  79 FSIIPPQVGLP----EERVKRCAaQLASALDFMHS---KNLVHRDIKPENVLLFdKDCRRVKLCDFGLTRRVGSTVKRVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWMAPEVFE-GSNYSEKC----DVFSWGIILWEVITRRKPFDE-IGGPAFRIMWAVHNGTR----PPLIKNLPKPIE 260
Cdd:cd13987 152 GTIPYTAPEVCEaKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWEKaDSDDQFYEEFVRWQKRKntavPSQWRRFTPKAL 231
                       250       260
                ....*....|....*....|....*.
gi 21735562 261 SLMTRCWSKDPSQRPSMEEIVKIMTH 286
Cdd:cd13987 232 RMFKKLLAPEPERRCSIKEVFKYLGD 257
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
41-229 5.26e-15

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 76.25  E-value: 5.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKA----KWRAKDVAIKQI-------ESESERKAFIVELRQLSRVNHPNIVKLY---GACLNPVCLVMEY 106
Cdd:cd14041  13 LLGRGGFSEVYKAfdltEQRYVAVKIHQLnknwrdeKKENYHKHACREYRIHKELDHPRIVKLYdyfSLDTDSFCTVLEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQPkALIHRDLKPPNLLLVAGGTV--LKICDFG------- 177
Cdd:cd14041  93 CEGNDLDFYLKQHKLM---SEKEARSIIMQIVNALKYLNEIKP-PIIHYDLKPGNILLVNGTACgeIKITDFGlskimdd 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 178 ---TACDIQTHMTNNKGSAAWMAPEVF----EGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14041 169 dsyNSVDGMELTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPF 227
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
27-286 1.09e-14

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 74.57  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  27 NFEEIDYKEIeveevvGRGAFGVV--CKAKWRAKDVAIKQIESESE----RKAFIVELRQLSRV-NHPNIVKLYGA--CL 97
Cdd:cd14198   7 NFYILTSKEL------GRGKFAVVrqCISKSTGQEYAAKFLKKRRRgqdcRAEILHEIAVLELAkSNPRVVNLHEVyeTT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  98 NPVCLVMEYAEGGSLYN--VLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKI 173
Cdd:cd14198  81 SEIILILEYAAGGEIFNlcVPDLAEMVS---ENDIIRLIRQILEGVYYLHQ---NNIVHLDLKPQNILLSSIYPLgdIKI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 174 CDFG------TACDIQTHMtnnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DEIGGPAFRIMWAVHNG 246
Cdd:cd14198 155 VDFGmsrkigHACELREIM----GTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFvGEDNQETFLNISQVNVD 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 247 TRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd14198 231 YSEETFSSVSQLATDFIQKLLVKNPEKRPTAEI---CLSH 267
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
42-277 1.29e-14

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 75.46  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLygacLNPVCLVMEYAEGGSLYNV 115
Cdd:cd07877  25 VGSGAYGSVCAAfdTKTGLRVAVKKLsrpfQSIIHAKRTYRELRLLKHMKHENVIGL----LDVFTPARSLEEFNDVYLV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LH--GAE-----PLPYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTHMTN 188
Cdd:cd07877 101 THlmGADlnnivKCQKLTDDHVQFLIYQILRGLKYIHSAD---IIHRDLKPSN-LAVNEDCELKILDFGLARHTDDEMTG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF---DEIGGPAFrIMWAVhnGTRPPlikNLPKPIESLMT 264
Cdd:cd07877 177 YVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFpgtDHIDQLKL-ILRLV--GTPGA---ELLKKISSESA 250
                       250
                ....*....|...
gi 21735562 265 RCWSKDPSQRPSM 277
Cdd:cd07877 251 RNYIQSLTQMPKM 263
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
41-279 1.45e-14

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 75.11  E-value: 1.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKDV--AIKQIESE-----SERKAFIVELRQLS-RVNHPNIVKLYGACLNPVCL--VMEYAEGG 110
Cdd:cd05592   2 VLGKGSFGKVMLAELKGTNQyfAIKALKKDvvledDDVECTMIERRVLAlASQHPFLTHLFCTFQTESHLffVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLynvLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaCDIQTHMTNNK 190
Cdd:cd05592  82 DL---MFHIQQSGRFDEDRARFYGAEIICGLQFLHS---RGIIYRDLKLDNVLLDREGHI-KIADFGM-CKENIYGENKA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-----DEiggpafrIMWAVHNgTRPPLIKNLPKPIES 261
Cdd:cd05592 154 stfcGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFhgedeDE-------LFWSICN-DTPHYPRWLTKEAAS 225
                       250
                ....*....|....*...
gi 21735562 262 LMTRCWSKDPSQRPSMEE 279
Cdd:cd05592 226 CLSLLLERNPEKRLGVPE 243
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
33-229 1.53e-14

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 74.18  E-value: 1.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQI-----------ESESERKAFIVELRQLSRVN-HPNIVKLYGACLN 98
Cdd:cd14182   2 YEKYEPKEILGRGVSSVVrrCIHKPTRQEYAVKIIditgggsfspeEVQELREATLKEIDILRKVSgHPNIIQLKDTYET 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  99 PVC--LVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCsqgVAYLHSMQpkaLIHRDLKPPNLLLvAGGTVLKICDF 176
Cdd:cd14182  82 NTFffLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEV---ICALHKLN---IVHRDLKPENILL-DDDMNIKLTDF 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 177 GTACDIQTHMTNNK--GSAAWMAPEVFEGS------NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14182 155 GFSCQLDPGEKLREvcGTPGYLAPEIIECSmddnhpGYGKEVDMWSTGVIMYTLLAGSPPF 215
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
40-295 1.71e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 75.12  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFG--VVCKAKWRAKDVAIKQIESE-----SERKAFIVELRQLSRVNHPNIVKLYGA--CLNPVCLVMEYAEGG 110
Cdd:cd05593  21 KLLGKGTFGkvILVREKASGKYYAMKILKKEviiakDEVAHTLTESRVLKNTRHPFLTSLKYSfqTKDRLCFVMEYVNGG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK 190
Cdd:cd05593 101 ELFFHLSRER---VFSEDRTRFYGAEIVSALDYLHSGK---IVYRDLKLENLMLDKDGHI-KITDFGLCKEGITDAATMK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPpliKNLPKPIESLMTRCW 267
Cdd:cd05593 174 tfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP---RTLSADAKSLLSGLL 250
                       250       260       270
                ....*....|....*....|....*....|
gi 21735562 268 SKDPSQR--PSMEEIVKIMTHlmRYFPGAD 295
Cdd:cd05593 251 IKDPNKRlgGGPDDAKEIMRH--SFFTGVN 278
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
37-282 2.17e-14

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 73.90  E-value: 2.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVELrqLSRV-NHPNIVKLYGACLNP--VCLVMEYAEGGS 111
Cdd:cd14177   7 ELKEDIGVGSYSVCkrCIHRATNMEFAVKIIDKSKRDPSEEIEI--LMRYgQHPNIITLKDVYDDGryVYLVTELMKGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV---AGGTVLKICDFGTAcdiqTHMTN 188
Cdd:cd14177  85 LLDRILRQK---FFSEREASAVLYTITKTVDYLHC---QGVVHRDLKPSNILYMddsANADSIRICDFGFA----KQLRG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 189 NKG-------SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFdeIGGP---AFRIMWAVHNGT---RPPLIKNL 255
Cdd:cd14177 155 ENGllltpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF--ANGPndtPEEILLRIGSGKfslSGGNWDTV 232
                       250       260
                ....*....|....*....|....*..
gi 21735562 256 PKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14177 233 SDAAKDLLSHMLHVDPHQRYTAEQVLK 259
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
52-283 2.31e-14

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 73.90  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  52 KAKWRAKDVAI-----KQIESES--ERKAFIVELR----QLSRVNHPNIVKLYGACL---NPVCLVMEYAEgGSLYNVLH 117
Cdd:cd14011  16 SKKSTKQEVSVfvfekKQLEEYSkrDREQILELLKrgvkQLTRLRHPRILTVQHPLEesrESLAFATEPVF-ASLANVLG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 118 GAE---PLPYYTAAHAMS------WCLQCSQGVAYLHSMQpkALIHRDLKPPNLLLVAGGTvLKICDFGTACDIQ----- 183
Cdd:cd14011  95 ERDnmpSPPPELQDYKLYdveikyGLLQISEALSFLHNDV--KLVHGNICPESVVINSNGE-WKLAGFDFCISSEqatdq 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 184 ----THMTNNKGSAA-----WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGP--AFRIMWAVHNGTRPPLI 252
Cdd:cd14011 172 fpyfREYDPNLPPLAqpnlnYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNllSYKKNSNQLRQLSLSLL 251
                       250       260       270
                ....*....|....*....|....*....|.
gi 21735562 253 KNLPKPIESLMTRCWSKDPSQRPSMEEIVKI 283
Cdd:cd14011 252 EKVPEELRDHVKTLLNVTPEVRPDAEQLSKI 282
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
42-229 3.00e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 73.51  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLS---RVNHPNIVKLYGACLNPVCL--VMEYAEGGSLYN 114
Cdd:cd07871  13 LGEGTYATVFKGRSKLTEnlVALKEIRLEHEEGAPCTAIREVSllkNLKHANIVTLHDIIHTERCLtlVFEYLDSDLKQY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 115 VLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG--TACDIQTHMTNNKGS 192
Cdd:cd07871  93 LDNCGNLMSMHNVKIFM---FQLLRGLSYCHK---RKILHRDLKPQNLLINEKGE-LKLADFGlaRAKSVPTKTYSNEVV 165
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21735562 193 AAWM-APEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07871 166 TLWYrPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMF 204
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
43-279 3.50e-14

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 73.07  E-value: 3.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVVCKAKWR--AKDVAIKQIESESERKAFIVELRQ---LSRVN-HPNIVKL----YGACLNPVCLVMEYAEGgSL 112
Cdd:cd07831   8 GEGTFSEVLKAQSRktGKYYAIKCMKKHFKSLEQVNNLREiqaLRRLSpHPNILRLievlFDRKTGRLALVFELMDM-NL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHG-AEPLPYYTAAHAMsWCLQCSqgvayLHSMQPKALIHRDLKPPNLLLVAGgtVLKICDFGTACDI-QTHMTNNK 190
Cdd:cd07831  87 YELIKGrKRPLPEKRVKNYM-YQLLKS-----LDHMHRNGIFHRDIKPENILIKDD--ILKLADFGSCRGIySKPPYTEY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 GSAAWM-APE-VFEGSNYSEKCDVFSWGIILWEVITRRKPF-------------DEIGGPAFRIMWAVHNGTR------- 248
Cdd:cd07831 159 ISTRWYrAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFpgtneldqiakihDVLGTPDAEVLKKFRKSRHmnynfps 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21735562 249 ------PPLIKNLPKPIESLMTRCWSKDPSQRPSMEE 279
Cdd:cd07831 239 kkgtglRKLLPNASAEGLDLLKKLLAYDPDERITAKQ 275
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
35-229 4.66e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 73.30  E-value: 4.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAE 108
Cdd:cd07864   8 KFDIIGIIGEGTYGQVYKAKDKDTGelVALKKVRLDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVTDKQDALDFKKD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNV-------LHG--AEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTA 179
Cdd:cd07864  88 KGAFYLVfeymdhdLMGllESGLVHFSEDHIKSFMKQLLEGLNYCHK---KNFLHRDIKCSNILLNNKGQI-KLADFGLA 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 180 ----CDIQTHMTNNKGSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07864 164 rlynSEESRPYTNKVITLWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIF 218
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
33-229 4.70e-14

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 72.70  E-value: 4.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERkafiVELRQLSRV---------------NHPNIVKLYGA 95
Cdd:cd14181   9 YQKYDPKEVIGRGVSSVVrrCVHRHTGQEFAVKIIEVTAER----LSPEQLEEVrsstlkeihilrqvsGHPSIITLIDS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  96 CLNP--VCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSMQpkaLIHRDLKPPNLLLVAGGtVLKI 173
Cdd:cd14181  85 YESStfIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLE---AVSYLHANN---IVHRDLKPENILLDDQL-HIKL 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 174 CDFGTACDIQthmTNNK-----GSAAWMAPEVFEGS------NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14181 158 SDFGFSCHLE---PGEKlrelcGTPGYLAPEILKCSmdethpGYGKEVDLWACGVILFTLLAGSPPF 221
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
40-229 5.65e-14

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 73.08  E-value: 5.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA-------KDVAIKQIESESERKAFIVELRQLSR-VNHPNIVKLYGACLNPVCL--VMEYAEG 109
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCdgkfyavKVLQKKTILKKKEQNHIMAERNVLLKnLKHPFLVGLHYSFQTSEKLyfVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHG----AEPLPYYTAAHAMSwclqcsqGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLkICDFGTACD-IQT 184
Cdd:cd05603  81 GELFFHLQRercfLEPRARFYAAEVAS-------AIGYLHSLN---IIYRDLKPENILLDCQGHVV-LTDFGLCKEgMEP 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 185 HMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05603 150 EETTSTfcGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
40-282 5.76e-14

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 72.36  E-value: 5.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDV--AIKQieSESERKAFIVELRQLSRV-------NHPNIVKLYGACLNPVCLVM--EYAE 108
Cdd:cd14138  11 EKIGSGEFGSVFKCVKRLDGCiyAIKR--SKKPLAGSVDEQNALREVyahavlgQHSHVVRYYSAWAEDDHMLIqnEYCN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 GGSLYNVL-HGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLV------------------AGGT 169
Cdd:cd14138  89 GGSLADAIsENYRIMSYFTEPELKDLLLQVARGLKYIHSM---SLVHMDIKPSNIFISrtsipnaaseegdedewaSNKV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 170 VLKICDFGTACDIQTHMTnNKGSAAWMAPEVFEgSNYSE--KCDVFSWGIILWEViTRRKPFDEIGGpafriMW-AVHNG 246
Cdd:cd14138 166 IFKIGDLGHVTRVSSPQV-EEGDSRFLANEVLQ-ENYTHlpKADIFALALTVVCA-AGAEPLPTNGD-----QWhEIRQG 237
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21735562 247 TRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14138 238 KLPRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVK 273
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
42-229 6.39e-14

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 73.16  E-value: 6.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA---KWRAKdVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGAcLNPVCLVMEYAE------ 108
Cdd:cd07878  23 VGSGAYGSVCSAydtRLRQK-VAVKKLsrpfQSLIHARRTYRELRLLKHMKHENVIGLLDV-FTPATSIENFNEvylvtn 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 109 --GGSLYNVLHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTHM 186
Cdd:cd07878 101 lmGADLNNIVKCQK----LSDEHVQFLIYQLLRGLKYIHS---AGIIHRDLKPSN-VAVNEDCELRILDFGLARQADDEM 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 187 TNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07878 173 TGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALF 216
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
41-229 8.14e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 72.70  E-value: 8.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESE--SERKAFIVELRQ---LSRVNHPNIVKLYGA--CLNPVCLVMEYAEGGS 111
Cdd:cd05632   9 VLGKGGFGEVCACQVRAtgKMYACKRLEKKriKKRKGESMALNEkqiLEKVNSQFVVNLAYAyeTKDALCLVLTIMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L----YNVLHgaeplPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT--H 185
Cdd:cd05632  89 LkfhiYNMGN-----PGFEEERALFYAAEILCGLEDLHR---ENTVYRDLKPENILLDDYGHI-RISDLGLAVKIPEgeS 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05632 160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-229 9.77e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 72.74  E-value: 9.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDV--AIKQIESES-----ERKAFIVELRQLSR-VNHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd05602  13 KVIGKGSFGKVLLARHKSDEKfyAVKVLQKKAilkkkEEKHIMSERNVLLKnVKHPFLVGLHFSfqTTDKLYFVLDYING 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGA----EPLPYYTAAHAMSwclqcsqGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLkICDFGTaC--DIQ 183
Cdd:cd05602  93 GELFYHLQRErcflEPRARFYAAEIAS-------ALGYLHSLN---IVYRDLKPENILLDSQGHIV-LTDFGL-CkeNIE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 184 THMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05602 161 PNGTTSTfcGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
60-282 1.10e-13

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 71.39  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  60 VAIKQIESESERKAFIVeLRQLSR-------VNHPNIVKLYG--ACLNPVCLVMEYAEGGSLYNVLHGAEPLpyyTAAHA 130
Cdd:cd14070  30 VAIKVIDKKKAKKDSYV-TKNLRRegriqqmIRHPNITQLLDilETENSYYLVMELCPGGNLMHRIYDKKRL---EEREA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 131 MSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT-----HMTNNKGSAAWMAPEVFEGSN 205
Cdd:cd14070 106 RRYIRQLVSAVEHLHR---AGVVHRDLKIENLLLDENDNI-KLIDFGLSNCAGIlgysdPFSTQCGSPAYAAPELLARKK 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 206 YSEKCDVFSWGIILWEVITRRKPFDEiggPAFRIMwAVH----NGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14070 182 YGPKVDVWSIGVNMYAMLTGTLPFTV---EPFSLR-ALHqkmvDKEMNPLPTDLSPGAISFLRSLLEPDPLKRPNIKQAL 257

                .
gi 21735562 282 K 282
Cdd:cd14070 258 A 258
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
42-254 1.33e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 71.57  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLS---RVNHPNIVKLYGA--CLNPVCLVMEYAEG----- 109
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDnlVALKEIRLEHEEGAPCTAIREVSllkDLKHANIVTLHDIihTEKSLTLVFEYLDKdlkqy 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 ----GSLYNvLHGAEPLPYytaahamswclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG--TACDIQ 183
Cdd:cd07873  90 lddcGNSIN-MHNVKLFLF-----------QLLRGLAYCHR---RKVLHRDLKPQNLLINERGE-LKLADFGlaRAKSIP 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21735562 184 THMTNNKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF-----DEIGGPAFRIMWAVHNGTRPPLIKN 254
Cdd:cd07873 154 TKTYSNEVVTLWYrPPDILLGStDYSTQIDMWGVGCIFYEMSTGRPLFpgstvEEQLHFIFRILGTPTEETWPGILSN 231
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
37-231 1.69e-13

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 70.77  E-value: 1.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVvGRGAFGVV--CKAKWRAKDVAIKQIESE-SERKAFIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYAEGGS 111
Cdd:cd14113  11 EVAEL-GRGRFSVVkkCDQRGTKRAVATKFVNKKlMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTsyILVLEMADQGR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 L--YNVLHGAeplpyYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGT--VLKICDFGTACDIQT--H 185
Cdd:cd14113  90 LldYVVRWGN-----LTEEKIRFYLREILEALQYLHNCR---IAHLDLKPENILVDQSLSkpTIKLADFGDAVQLNTtyY 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21735562 186 MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DE 231
Cdd:cd14113 162 IHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFlDE 208
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
57-276 2.40e-13

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 70.99  E-value: 2.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  57 AKDVAIKQIESESERKAFIVELRQLSRvnHPNIVKLYGACLNPVCLVME-----------------YAEGGSLYNV---- 115
Cdd:cd14018  45 APNVALLGEYGEVTRLGLQNGRKLLAP--HPNIIRVQRAFTDSVPLLPGaiedypdvlparlnpsgLGHNRTLFLVmkny 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 ---LHG--AEPLPYYTAAHAMswCLQCSQGVAYLHSmqpKALIHRDLKPPNLLL---VAGGTVLKICDFGT--ACDI--- 182
Cdd:cd14018 123 pctLRQylWVNTPSYRLARVM--ILQLLEGVDHLVR---HGIAHRDLKSDNILLeldFDGCPWLVIADFGCclADDSigl 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 ----QTHMTNNKGSAAWMAPEVFEGS-------NYSeKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMwAVHNGTRPPL 251
Cdd:cd14018 198 qlpfSSWYVDRGGNACLMAPEVSTAVpgpgvviNYS-KADAWAVGAIAYEIFGLSNPFYGLGDTMLESR-SYQESQLPAL 275
                       250       260
                ....*....|....*....|....*
gi 21735562 252 IKNLPKPIESLMTRCWSKDPSQRPS 276
Cdd:cd14018 276 PSAVPPDVRQVVKDLLQRDPNKRVS 300
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
33-229 2.60e-13

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 70.31  E-value: 2.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  33 YKEIEVEEVVGRGAFGVV--CKAKWRAKDVAIKQIES--ESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVMEY 106
Cdd:cd14114   1 YDHYDILEELGTGAFGVVhrCTERATGNNFAAKFIMTphESDKETVRKEIQIMNQLHHPKLINLHDAFEddNEMVLILEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 107 AEGGSLYNVLhgAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLL-VAGGTVLKICDFGTAcdiqTH 185
Cdd:cd14114  81 LSGGELFERI--AAEHYKMSEAEVINYMRQVCEGLCHMHE---NNIVHLDIKPENIMCtTKRSNEVKLIDFGLA----TH 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNK------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14114 152 LDPKEsvkvttGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPF 201
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
39-289 2.68e-13

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 72.96  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   39 EEVVGRGAFGVVCKAKWRAKDV--AIKQI-ESESERKAFIVELRQLsrvNHPNIVKLYGACLNPVC--LVMEYAEGGSLY 113
Cdd:PLN00113 695 ENVISRGKKGASYKGKSIKNGMqfVVKEInDVNSIPSSEIADMGKL---QHPNIVKLIGLCRSEKGayLIHEYIEGKNLS 771
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  114 NVLHGaeplpyytaahaMSW------CLQCSQGVAYLHSMQPKALIHRDLKPPNLLL-VAGGTVLKICDFGTACdiqthM 186
Cdd:PLN00113 772 EVLRN------------LSWerrrkiAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIdGKDEPHLRLSLPGLLC-----T 834
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  187 TNNKG-SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD-EIGGPAFRIMWAVHNGTR-------PPLIK---- 253
Cdd:PLN00113 835 DTKCFiSSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADaEFGVHGSIVEWARYCYSDchldmwiDPSIRgdvs 914
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 21735562  254 -NLPKPIE--SLMTRCWSKDPSQRPSMEEIVKIMTHLMR 289
Cdd:PLN00113 915 vNQNEIVEvmNLALHCTATDPTARPCANDVLKTLESASR 953
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
37-224 2.79e-13

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 71.07  E-value: 2.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVckakWRAKD------VAIKQIESESE-RKAFIVELRQLSRVN-----HP---NIVKLY------GA 95
Cdd:cd14136  13 HVVRKLGWGHFSTV----WLCWDlqnkrfVALKVVKSAQHyTEAALDEIKLLKCVReadpkDPgreHVVQLLddfkhtGP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  96 CLNPVCLVMEYaeGGSlyNVLHGAE-------PLPYytaahAMSWCLQCSQGVAYLHSmQPKaLIHRDLKPPNLLLVAGG 168
Cdd:cd14136  89 NGTHVCMVFEV--LGP--NLLKLIKrynyrgiPLPL-----VKKIARQVLQGLDYLHT-KCG-IIHTDIKPENVLLCISK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 169 TVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14136 158 IEVKIADLGNACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELAT 213
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
29-229 6.00e-13

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 70.37  E-value: 6.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  29 EEIDYKEIEVEEV------VGRGAFGVVCKAKWR--AKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGAC 96
Cdd:cd07880   4 QEVNKTIWEVPDRyrdlkqVGSGAYGTVCSALDRrtGAKVAIKKLyrpfQSELFAKRAYRELRLLKHMKHENVIGLLDVF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  97 --------LNPVCLVMEYAegGSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGG 168
Cdd:cd07880  84 tpdlsldrFHDFYLVMPFM--GTDLGKLMKHEKL---SEDRIQFLVYQMLKGLKYIHA---AGIIHRDLKPGN-LAVNED 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21735562 169 TVLKICDFGTACDIQTHMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07880 155 CELKILDFGLARQTDSEMTGYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLF 216
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-229 6.07e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 69.99  E-value: 6.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFG--VVCKAKWRAKDVAIKQIE-----SESERKAFIVELRQLSR-VNHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd05604   2 KVIGKGSFGkvLLAKRKRDGKYYAVKVLQkkvilNRKEQKHIMAERNVLLKnVKHPFLVGLHYSfqTTDKLYFVLDFVNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVLkICDFG---TACDIQTHM 186
Cdd:cd05604  82 GELFFHLQRER---SFPEPRARFYAAEIASALGYLHSIN---IVYRDLKPENILLDSQGHIV-LTDFGlckEGISNSDTT 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 187 TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05604 155 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
40-274 6.31e-13

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 69.97  E-value: 6.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQIESE-----SERKAFIVELRQLSRV-NHPNIVKLYGA--CLNPVCLVMEYAEG 109
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGeyFAVKALKKDvvlidDDVECTMVEKRVLALAwENPFLTHLYCTfqTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLYNVLHGAEPLPYYTAAHAMSWCLqCsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaCDIQTHMTNN 189
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIV-C--GLQFLHS---KGIIYRDLKLDNVMLDRDGHI-KIADFGM-CKENVFGDNR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 190 K----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDeiGGPAFRIMWAVHNGTrPPLIKNLPKPIESLMTR 265
Cdd:cd05620 153 AstfcGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFH--GDDEDELFESIRVDT-PHYPRWITKESKDILEK 229

                ....*....
gi 21735562 266 CWSKDPSQR 274
Cdd:cd05620 230 LFERDPTRR 238
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
42-229 6.34e-13

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 70.45  E-value: 6.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAkwRAKD----VAIKQ-----IESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGG 110
Cdd:cd05600  19 VGQGGYGSVFLA--RKKDtgeiCALKImkkkvLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPenVYLAMEYVPGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEPLPYYTAAHAMSWCLQCsqgVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT--HMTN 188
Cdd:cd05600  97 DFRTLLNNSGILSEEHARFYIAEMFAA---ISSLHQL---GYIHRDLKPENFLIDSSGHI-KLTDFGLASGTLSpkKIES 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 189 NK--------------------------------------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05600 170 MKirleevkntafleltakerrniyramrkedqnyansvvGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPF 248
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
37-224 6.45e-13

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 69.94  E-value: 6.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRA---KDVAIKQIES-ESERKAFIVELRQLSRVNH--PN----IVKLYGACL--NPVCLVM 104
Cdd:cd14135   3 RVYGYLGKGVFSNVVRARDLArgnQEVAIKIIRNnELMHKAGLKELEILKKLNDadPDdkkhCIRLLRHFEhkNHLCLVF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EyaeggSLYNVLHgaEPLPYYTAAHAMSwcLQCSQGVAY-----LHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTA 179
Cdd:cd14135  83 E-----SLSMNLR--EVLKKYGKNVGLN--IKAVRSYAQqlflaLKHLKKCNILHADIKPDNILVNEKKNTLKLCDFGSA 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 180 CDIQ-THMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14135 154 SDIGeNEITPYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYT 199
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
42-280 6.70e-13

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 69.21  E-value: 6.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAK----WRAKDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSL 112
Cdd:cd14206   5 IGNGWFGKVILGEifsdYTPAQVVVKELRVSAgplEQRKFISEAQPYRSLQHPNILQCLGLCTEtiPFLLIMEFCQLGDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEP-------LPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD---I 182
Cdd:cd14206  85 KRYLRAQRKadgmtpdLPTRDLRTLQRMAYEITLGLLHLHK---NNYIHSDLALRNCLLTSDLTV-RIGDYGLSHNnykE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 183 QTHMTNNKG--SAAWMAPEVFE---GS----NYSEKCDVFSWGIILWEVIT-RRKPFDEIGGP---AFRIMWAVHNGTRP 249
Cdd:cd14206 161 DYYLTPDRLwiPLRWVAPELLDelhGNlivvDQSKESNVWSLGVTIWELFEfGAQPYRHLSDEevlTFVVREQQMKLAKP 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 21735562 250 PLIKNLPKPIESLMTRCWsKDPSQRPSMEEI 280
Cdd:cd14206 241 RLKLPYADYWYEIMQSCW-LPPSQRPSVEEL 270
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
38-229 7.43e-13

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 69.12  E-value: 7.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGACLNPVCLVM--EYAEGGSL 112
Cdd:cd14104   4 IAEELGRGQFGIVhrCVETSSKKTYMAKFVKVKGADQVLVKkEISILNIARHRNILRLHESFESHEELVMifEFISGVDI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAG-GTVLKICDFGTACDIQTHMTNNKG 191
Cdd:cd14104  84 FERITTARF--ELNEREIVSYVRQVCEALEFLHS---KNIGHFDIRPENIIYCTRrGSYIKIIEFGQSRQLKPGDKFRLQ 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21735562 192 --SAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14104 159 ytSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPF 198
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
41-229 9.46e-13

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 69.65  E-value: 9.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA--KDVAIKQIESES-----ERKAFIVELRQL-SRVNHPNIV----------KLYgaclnpvcL 102
Cdd:cd05575   2 VIGKGSFGKVLLARHKAegKLYAVKVLQKKAilkrnEVKHIMAERNVLlKNVKHPFLVglhysfqtkdKLY--------F 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVL----HGAEPLPYYTAAHAMSwclqcsqGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd05575  74 VLDYVNGGELFFHLqrerHFPEPRARFYAAEIAS-------ALGYLHSLN---IIYRDLKPENILLDSQGHV-VLTDFGL 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 179 aC--DIQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05575 143 -CkeGIEPSDTTSTfcGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
42-223 1.11e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 69.67  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGAC--------LNPVCLVMEYA 107
Cdd:cd07876  29 IGSGAQGIVCAAfdTVLGINVAVKKLsrpfQNQTHAKRAYRELVLLKCVNHKNIISLLNVFtpqksleeFQDVYLVMELM 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGgSLYNVLHgaeplpYYTAAHAMSWCL-QCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTH- 185
Cdd:cd07876 109 DA-NLCQVIH------MELDHERMSYLLyQMLCGIKHLHS---AGIIHRDLKPSN-IVVKSDCTLKILDFGLARTACTNf 177
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21735562 186 -MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVI 223
Cdd:cd07876 178 mMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
77-280 1.30e-12

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 68.44  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  77 ELRQLSRVNHPNIVKLYGACLNP----VCLVMEYAEGGSLYNVlHGAEPlpyYTAAHAMSWCLQCSQGVAYLHSMQpkaL 152
Cdd:cd14200  73 EIAILKKLDHVNIVKLIEVLDDPaednLYMVFDLLRKGPVMEV-PSDKP---FSEDQARLYFRDIVLGIEYLHYQK---I 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 153 IHRDLKPPNLLLVAGGTVlKICDFGTACDIQ---THMTNNKGSAAWMAPEVFE--GSNYSEKC-DVFSWGIILWEVITRR 226
Cdd:cd14200 146 VHRDIKPSNLLLGDDGHV-KIADFGVSNQFEgndALLSSTAGTPAFMAPETLSdsGQSFSGKAlDVWAMGVTLYCFVYGK 224
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 227 KPF-DEiggpafrIMWAVHNGTRP-----PLIKNLPKPIESLMTRCWSKDPSQRPSMEEI 280
Cdd:cd14200 225 CPFiDE-------FILALHNKIKNkpvefPEEPEISEELKDLILKMLDKNPETRITVPEI 277
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
35-231 1.49e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 69.32  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVV--CK----AKWRA------KDVAIKQIESESERKAFIVELrqLSRVNHPNIVKLYGACLNP--V 100
Cdd:cd05633   6 DFSVHRIIGRGGFGEVygCRkadtGKMYAmkcldkKRIKMKQGETLALNERIMLSL--VSTGDCPFIVCMTYAFHTPdkL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVL--HGAeplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd05633  84 CFILDLMNGGDLHYHLsqHGV-----FSEKEMRFYATEIILGLEHMHN---RFVVYRDLKPANILLDEHGHV-RISDLGL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 179 ACDIQTHMTN-NKGSAAWMAPEVFE-GSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd05633 155 ACDFSKKKPHaSVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQ 209
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
37-229 1.54e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 68.11  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCK--AKWRAKDVAIKQIESES--ERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGG 110
Cdd:cd14191   5 DIEERLGSGKFGQVFRlvEKKTKKVWAGKFFKAYSakEKENIRQEISIMNCLHHPKLVQCVDAFEEKanIVMVLEMVSGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEPlpYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV-AGGTVLKICDFGTACDIQTHMTNN 189
Cdd:cd14191  85 ELFERIIDEDF--ELTERECIKYMRQISEGVEYIHK---QGIVHLDLKPENIMCVnKTGTKIKLIDFGLARRLENAGSLK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21735562 190 K--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14191 160 VlfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPF 201
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
38-229 1.65e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 68.80  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  38 VEEVVGRGAFGVVCKAKWRAKD--VAIKQIESE-----SERKAFIVELRQLSRV-NHPNIVKLYgaCL----NPVCLVME 105
Cdd:cd05619   9 LHKMLGKGSFGKVFLAELKGTNqfFAIKALKKDvvlmdDDVECTMVEKRVLSLAwEHPFLTHLF--CTfqtkENLFFVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEP--LPYYTAAHAMSWClqcsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD-- 181
Cdd:cd05619  87 YLNGGDLMFHIQSCHKfdLPRATFYAAEIIC-----GLQFLHS---KGIVYRDLKLDNILLDKDGHI-KIADFGMCKEnm 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21735562 182 IQTHMTNN-KGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05619 158 LGDAKTSTfCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPF 206
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
42-231 1.70e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 67.68  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIV-ELRQLSRVNHPNIVKLYGACLNPVC--LVMEYAEGGSLYNVL 116
Cdd:cd14115   1 IGRGRFSIVkkCLHKATRKDVAVKFVSKKMKKKEQAAhEAALLQHLQHPQYITLHDTYESPTSyiLVLELMDDGRLLDYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 117 HGAEPLPYYTAAHAMSWCLQCSQgvaYLHSMQpkaLIHRDLKPPNLL--LVAGGTVLKICDFGTACDIQTHMTNNK--GS 192
Cdd:cd14115  81 MNHDELMEEKVAFYIRDIMEALQ---YLHNCR---VAHLDIKPENLLidLRIPVPRVKLIDLEDAVQISGHRHVHHllGN 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21735562 193 AAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF-DE 231
Cdd:cd14115 155 PEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFlDE 194
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
41-229 1.85e-12

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 67.85  E-value: 1.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVV--CKAKWRAKDVAIK-----QIESESERKAFIVELRQLSRVNH----PNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd05606   1 IIGRGGFGEVygCRKADTGKMYAMKcldkkRIKMKQGETLALNERIMLSLVSTggdcPFIVCMTYAFQTPdkLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVL--HGAeplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTH 185
Cdd:cd05606  81 NGGDLHYHLsqHGV-----FSEAEMRFYAAEVILGLEHMHN---RFIVYRDLKPANILLDEHGHV-RISDLGLACDFSKK 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 186 MTNNK-GSAAWMAPEVF-EGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05606 152 KPHASvGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPF 197
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
41-229 1.85e-12

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 68.59  E-value: 1.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIV-----------ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYA 107
Cdd:cd05584   3 VLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIVrnqkdtahtkaERNILEAVKHPFIVDLHYAFQTGgkLYLILEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGGSLYNVLHGAEPLPYYTAAHAMSwclQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTaC------D 181
Cdd:cd05584  83 SGGELFMHLEREGIFMEDTACFYLA---EITLALGHLHSL---GIIYRDLKPENILLDAQGHV-KLTDFGL-CkesihdG 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 182 IQTHMTNnkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05584 155 TVTHTFC--GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPF 200
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
40-282 2.60e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 67.65  E-value: 2.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKDV--AIKQ-----IESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVM--EYAEGG 110
Cdd:cd14139   6 EKIGVGEFGSVYKCIKRLDGCvyAIKRsmrpfAGSSNEQLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIqnEYCNGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVL-HGAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLV---------------------AGG 168
Cdd:cd14139  86 SLQDAIsENTKSGNHFEEPELKDILLQVSMGLKYIHN---SGLVHLDIKPSNIFIChkmqsssgvgeevsneedeflSAN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 169 TVLKICDFGTACDIQTHMTNnKGSAAWMAPEVF-EGSNYSEKCDVFSWGIILwEVITRRKPFDEIGGPAFRImwavHNGT 247
Cdd:cd14139 163 VVYKIGDLGHVTSINKPQVE-EGDSRFLANEILqEDYRHLPKADIFALGLTV-ALAAGAEPLPTNGAAWHHI----RKGN 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21735562 248 RPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd14139 237 FPDVPQELPESFSSLLKNMIQPDPEQRPSATALAR 271
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
35-229 3.85e-12

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 68.50  E-value: 3.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFG--VVCKAKWRAKDVAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVME 105
Cdd:cd05624  73 DFEIIKVIGRGAFGevAVVKMKNTERIYAMKilnkwEMLKRAETACFREERNVLVNGDCQWITTLHYAFQdeNYLYLVMD 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEP-LPYYTAAHAMSwclqcsQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFGTACDIQT 184
Cdd:cd05624 153 YYVGGDLLTLLSKFEDkLPEDMARFYIG------EMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHI-RLADFGSCLKMND 225
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 185 HMTNNK----GSAAWMAPEVFEG-----SNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05624 226 DGTVQSsvavGTPDYISPEILQAmedgmGKYGPECDWWSLGVCMYEMLYGETPF 279
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
35-423 4.30e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 69.38  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562    35 EIEVEEVVGRGAFGVVCKAK---------WRAkdVAIKQIEsESERKAFIVELRQLSRVNHPNIVKLYGACLNP----VC 101
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKhkrtqeffcWKA--ISYRGLK-EREKSQLVIEVNVMRELKHKNIVRYIDRFLNKanqkLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   102 LVMEYAEGGSLYNVLHGAEPLPYYTAAHAM-SWCLQCSQGVAYLHSMQP----KALIHRDLKPPNLLL------------ 164
Cdd:PTZ00266   91 ILMEFCDAGDLSRNIQKCYKMFGKIEEHAIvDITRQLLHALAYCHNLKDgpngERVLHRDLKPQNIFLstgirhigkita 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   165 ----VAGGTVLKICDFGTACD--IQTHMTNNKGSAAWMAPEVF--EGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPA 236
Cdd:PTZ00266  171 qannLNGRPIAKIGDFGLSKNigIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFS 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   237 fRIMWAVHNGTRPPlIKNLPKPIESLMTRCWSKDPSQRPSMEEIV--KIMTHLMryfpgadeplqyPCQYSDEGQSNSAT 314
Cdd:PTZ00266  251 -QLISELKRGPDLP-IKGKSKELNILIKNLLNLSAKERPSALQCLgyQIIKNVG------------PPVGAAGGGAGVAA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   315 STGSFmdIASTNTSNKSDT----NMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSA 390
Cdd:PTZ00266  317 APGAV--VARRNPSKEHPGlqlaAMEKAKHAEAANYGISPNTLINQRNEEQHGRRSSSCASRQSANNVTNITSITSVTSV 394
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 21735562   391 DMSEIEARIAATTAYSKPKRG----HRKTASFGNILD 423
Cdd:PTZ00266  395 ASVASVASVPSKDDRKYPQDGathcHAVNGHYGGRVD 431
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
37-221 4.44e-12

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 67.66  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVV--CKAKWRAKDVAIKQIESeseRKAF----IVELRQLSRVN-------HPNIVKLYG--ACLNPVC 101
Cdd:cd14212   2 LVLDLLGQGTFGQVvkCQDLKTNKLVAVKVLKN---KPAYfrqaMLEIAILTLLNtkydpedKHHIVRLLDhfMHHGHLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAeGGSLY-----NVLHGaepLPYYTAAHAMSWCLQCsqgvayLHSMQPKALIHRDLKPPNLLLVAGGT-VLKICD 175
Cdd:cd14212  79 IVFELL-GVNLYellkqNQFRG---LSLQLIRKFLQQLLDA------LSVLKDARIIHCDLKPENILLVNLDSpEIKLID 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 176 FGTACD--------IQthmtnnkgSAAWMAPEVFEGSNYSEKCDVFSWGIILWE 221
Cdd:cd14212 149 FGSACFenytlytyIQ--------SRFYRSPEVLLGLPYSTAIDMWSLGCIAAE 194
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
37-229 4.63e-12

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 66.48  E-value: 4.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKA---------KWRAKDVAIKQIESESERKAFIVELRQLSRVN-HPNIVKLYGACLNP--VCLVM 104
Cdd:cd14019   4 RIIEKIGEGTFSSVYKAedklhdlydRNKGRLVALKHIYPTSSPSRILNELECLERLGgSNNVSGLITAFRNEdqVVAVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLH--GAEPLPYYTaahamsWCLqcSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFGTA--- 179
Cdd:cd14019  84 PYIEHDDFRDFYRkmSLTDIRIYL------RNL--FKALKHVHS---FGIIHRDVKPGNFLYNRETGKGVLVDFGLAqre 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21735562 180 CDIQTHMTNNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14019 153 EDRPEQRAPRAGTRGFRAPEVlFKCPHQTTAIDIWSAGVILLSILSGRFPF 203
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
41-230 4.94e-12

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 67.42  E-value: 4.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  41 VVGRGAFGVVCKAKWRA-----------KDVAIKQIESESErkafIVELRQLSRVNHPN-IVKLYgACLNPV---CLVME 105
Cdd:cd05587   3 VLGKGSFGKVMLAERKGtdelyaikilkKDVIIQDDDVECT----MVEKRVLALSGKPPfLTQLH-SCFQTMdrlYFVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSL-YNVLHGAEplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTaCdiQT 184
Cdd:cd05587  78 YVNGGDLmYHIQQVGK----FKEPVAVFYAAEIAVGLFFLHS---KGIIYRDLKLDNVMLDAEGHI-KIADFGM-C--KE 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 185 HMTNNK------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd05587 147 GIFGGKttrtfcGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFD 198
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
40-282 4.96e-12

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 66.19  E-value: 4.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFG-------VVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGG 110
Cdd:cd14188   7 KVLGKGGFAkcyemtdLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKenIYILLEYCSRR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLlVAGGTVLKICDFGTACDIQTHMTNNK 190
Cdd:cd14188  87 SMAHILKARKVL---TEPEVRYYLRQIVSGLKYLHEQE---ILHRDLKLGNFF-INENMELKVGDFGLAARLEPLEHRRR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 191 ---GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGgpaFRIMWAVHNGTRPPLIKNLPKPIESLMTRCW 267
Cdd:cd14188 160 ticGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTN---LKETYRCIREARYSLPSSLLAPAKHLIASML 236
                       250
                ....*....|....*
gi 21735562 268 SKDPSQRPSMEEIVK 282
Cdd:cd14188 237 SKNPEDRPSLDEIIR 251
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
86-229 5.26e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 66.72  E-value: 5.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  86 HPNIVKLYGACLNPV------------CLVMEYAEGGSLYNVL---HGaeplpyYTAAHAMSWCLQCSQGVAYLHSMQpk 150
Cdd:cd14171  58 HPNIVQIYDVYANSVqfpgessprarlLIVMELMEGGELFDRIsqhRH------FTEKQAAQYTKQIALAVQHCHSLN-- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 151 aLIHRDLKPPNLLLV--AGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSN-----------------YSEKCD 211
Cdd:cd14171 130 -IAHRDLKPENLLLKdnSEDAPIKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCD 208
                       170
                ....*....|....*...
gi 21735562 212 VFSWGIILWEVITRRKPF 229
Cdd:cd14171 209 MWSLGVIIYIMLCGYPPF 226
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
42-280 5.32e-12

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 66.55  E-value: 5.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV----CKAKWRAKDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGAC--LNPVCLVMEYAEGGSL 112
Cdd:cd05087   5 IGHGWFGKVflgeVNSGLSSTQVVVKELKASAsvqDQMQFLEEAQPYRALQHTNLLQCLAQCaeVTPYLLVMEFCPLGDL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVL---HGAEPL-PYYTAAHAMSWCLQCsqGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTA-CDIQT--H 185
Cdd:cd05087  85 KGYLrscRAAESMaPDPLTLQRMACEVAC--GLLHLHR---NNFVHSDLALRNCLLTADLTV-KIGDYGLShCKYKEdyF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 MTNNKGSAA--WMAPEVFEG-------SNYSEKCDVFSWGIILWEVItrrkpfdEIGGPAFRimwavHNGTRPPL---IK 253
Cdd:cd05087 159 VTADQLWVPlrWIAPELVDEvhgnllvVDQTKQSNVWSLGVTIWELF-------ELGNQPYR-----HYSDRQVLtytVR 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21735562 254 ----NLPKPIESL---------MTRCWSKdPSQRPSMEEI 280
Cdd:cd05087 227 eqqlKLPKPQLKLslaerwyevMQFCWLQ-PEQRPTAEEV 265
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
42-237 5.35e-12

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 66.78  E-value: 5.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKAKWRAKDVAIKQI---ESESERKA---FIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYAEGGSLY 113
Cdd:cd14157   1 ISEGTFADIYKGYRHGKQYVIKRLketECESPKSTerfFQTEVQICFRCCHPNILPLLGFCVESDchCLIYPYMPNGSLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 114 NVLH---GAEPLPYytaAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVA------GGTVLKICDFGTACD--- 181
Cdd:cd14157  81 DRLQqqgGSHPLPW---EQRLSISLGLLKAVQHLHNFG---ILHGNIKSSNVLLDGnllpklGHSGLRLCPVDKKSVytm 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 182 IQTHMTnnKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF 237
Cdd:cd14157 155 MKTKVL--QISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTGIKAMDEFRSPVY 208
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
42-229 6.08e-12

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 67.23  E-value: 6.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVC--------LVMEYa 107
Cdd:cd07879  23 VGSGAYGSVCSAidKRTGEKVAIKKLsrpfQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSgdefqdfyLVMPY- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 eggsLYNVLHGAEPLPYyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTHMT 187
Cdd:cd07879 102 ----MQTDLQKIMGHPL-SEDKVQYLVYQMLCGLKYIHS---AGIIHRDLKPGN-LAVNEDCELKILDFGLARHADAEMT 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 188 NNKGSAAWMAPEV-FEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07879 173 GYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLF 215
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-229 7.64e-12

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 66.25  E-value: 7.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKA---FIVELRQLSRVNHPNIVKLYG-----ACLNpvcLVMEYAEg 109
Cdd:cd07844   6 DKLGEGSYATVYKGRSKLTGqlVALKEIRLEHEEGApftAIREASLLKDLKHANIVTLHDiihtkKTLT---LVFEYLD- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 gslynvlhgaEPLPYYtaahaMSWC-------------LQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDF 176
Cdd:cd07844  82 ----------TDLKQY-----MDDCggglsmhnvrlflFQLLRGLAYCHQ---RRVLHRDLKPQNLLISERGE-LKLADF 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21735562 177 G--TACDIQTHMTNNKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07844 143 GlaRAKSVPSKTYSNEVVTLWYrPPDVLLGStEYSTSLDMWGVGCIFYEMATGRPLF 199
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
40-228 9.98e-12

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 66.01  E-value: 9.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRA--KDVAIKQIESESERKAF-------IVELRQLSRVNHpnIVKLYG---------ACLNpvc 101
Cdd:cd07837   7 EKIGEGTYGKVYKARDKNtgKLVALKKTRLEMEEEGVpstalreVSLLQMLSQSIY--IVRLLDvehveengkPLLY--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGG-SLYNVLHG---AEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVLKICDFG 177
Cdd:cd07837  82 LVFEYLDTDlKKFIDSYGrgpHNPLP---AKTIQSFMYQLCKGVAHCHS---HGVMHRDLKPQNLLVDKQKGLLKIADLG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 178 --TACDIQTHMTNNKGSAAWM-APEVFEGS-NYSEKCDVFSWGIILWEVItRRKP 228
Cdd:cd07837 156 lgRAFTIPIKSYTHEIVTLWYrAPEVLLGStHYSTPVDMWSVGCIFAEMS-RKQP 209
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
42-229 9.99e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 65.73  E-value: 9.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV--CKAKWRAKDVAIKQIESESE----RKAFIVELR--QLSRVNhPNIVKLYGACLNP--VCLVMEYAEGGS 111
Cdd:cd14197  17 LGRGKFAVVrkCVEKDSGKEFAAKFMRKRRKgqdcRMEIIHEIAvlELAQAN-PWVINLHEVYETAseMILVLEYAAGGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 112 LYNVLHgAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTV--LKICDFGtacdIQTHMTNN 189
Cdd:cd14197  96 IFNQCV-ADREEAFKEKDVKRLMKQILEGVSFLHN---NNVVHLDLKPQNILLTSESPLgdIKIVDFG----LSRILKNS 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 190 K------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14197 168 EelreimGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPF 213
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
102-286 1.12e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 65.40  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLH--GAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVA--GGTVLKICDFG 177
Cdd:cd14172  78 IIMECMEGGELFSRIQerGDQAFTEREASEIMR---DIGTAIQYLHSMN---IAHRDVKPENLLYTSkeKDAVLKLTDFG 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACD--IQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF------RIMWAVHnGTRP 249
Cdd:cd14172 152 FAKEttVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAIspgmkrRIRMGQY-GFPN 230
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21735562 250 PLIKNLPKPIESLMTRCWSKDPSQRPSMEEivkIMTH 286
Cdd:cd14172 231 PEWAEVSEEAKQLIRHLLKTDPTERMTITQ---FMNH 264
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
37-224 1.13e-11

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 66.69  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAkWRAKD---VAIKQIESE-------SERKAFIVELRQLSRVNHPNIVKL--YGACLNPVCLVM 104
Cdd:cd14224  68 EVLKVIGKGSFGQVVKA-YDHKThqhVALKMVRNEkrfhrqaAEEIRILEHLKKQDKDNTMNVIHMleSFTFRNHICMTF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGgSLYNVLHGAE----PLPYYTA-AHAMswcLQCsqgvayLHSMQPKALIHRDLKPPNLLLVAGG-TVLKICDFGT 178
Cdd:cd14224 147 ELLSM-NLYELIKKNKfqgfSLQLVRKfAHSI---LQC------LDALHRNKIIHCDLKPENILLKQQGrSGIKVIDFGS 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 179 ACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14224 217 SCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLT 262
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
42-257 1.14e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 66.65  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLYGAC--------LNPVCLVMEYA 107
Cdd:cd07874  25 IGSGAQGIVCAAydAVLDRNVAIKKLsrpfQNQTHAKRAYRELVLMKCVNHKNIISLLNVFtpqksleeFQDVYLVMELM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGgSLYNVLHgaeplpYYTAAHAMSWCL-QCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTH- 185
Cdd:cd07874 105 DA-NLCQVIQ------MELDHERMSYLLyQMLCGIKHLHS---AGIIHRDLKPSN-IVVKSDCTLKILDFGLARTAGTSf 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 186 -MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRR-------------KPFDEIGGPAFRIMWAVHNGTRpPL 251
Cdd:cd07874 174 mMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKilfpgrdyidqwnKVIEQLGTPCPEFMKKLQPTVR-NY 252

                ....*.
gi 21735562 252 IKNLPK 257
Cdd:cd07874 253 VENRPK 258
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
34-233 1.22e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 66.59  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKD------VAIKQIESESERKAFIVELRQL--SRVNHPNIVKLYgACLNP---VCL 102
Cdd:cd05618  20 QDFDLLRVIGRGSYAKVLLVRLKKTEriyamkVVKKELVNDDEDIDWVQTEKHVfeQASNHPFLVGLH-SCFQTesrLFF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD- 181
Cdd:cd05618  99 VIEYVNGGDLMFHMQRQRKLP---EEHARFYSAEISLALNYLHE---RGIIYRDLKLDNVLLDSEGHI-KLTDYGMCKEg 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21735562 182 IQTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIG 233
Cdd:cd05618 172 LRPGDTTSTfcGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVG 225
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
35-231 1.37e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 65.84  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVV--CK----AKWRA------KDVAIKQIESESERKAFIVELrqLSRVNHPNIVKLYGACLNP--V 100
Cdd:cd14223   1 DFSVHRIIGRGGFGEVygCRkadtGKMYAmkcldkKRIKMKQGETLALNERIMLSL--VSTGDCPFIVCMSYAFHTPdkL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 101 CLVMEYAEGGSLYNVL--HGAeplpyYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGT 178
Cdd:cd14223  79 SFILDLMNGGDLHYHLsqHGV-----FSEAEMRFYAAEIILGLEHMHS---RFVVYRDLKPANILLDEFGHV-RISDLGL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 179 ACDIQTHMTN-NKGSAAWMAPEVFE-GSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:cd14223 150 ACDFSKKKPHaSVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQ 204
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
40-228 1.40e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 65.53  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWR--AKDVAIKQIESESERKAF----IVELRQLSRVNHPNIVKLYGACL--NPVCLVMEYAEGG- 110
Cdd:cd07839   6 EKIGEGTYGTVFKAKNRetHEIVALKRVRLDDDDEGVpssaLREICLLKELKHKNIVRLYDVLHsdKKLTLVFEYCDQDl 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 -SLYNVLHGaeplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTvLKICDFGTA--CDIQTHMT 187
Cdd:cd07839  86 kKYFDSCNG-----DIDPEIVKSFMFQLLKGLAFCHSHN---VLHRDLKPQNLLINKNGE-LKLADFGLAraFGIPVRCY 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 188 NNKGSAAWM-APEVFEGSN-YSEKCDVFSWGIILWEVITRRKP 228
Cdd:cd07839 157 SAEVVTLWYrPPDVLFGAKlYSTSIDMWSAGCIFAELANAGRP 199
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-229 1.46e-11

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 65.72  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVV--CKAKWRAKDVAIKQIESES--ER---KAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGG 110
Cdd:cd05574   7 KLLGKGDVGRVylVRLKGTGKLFAMKVLDKEEmiKRnkvKRVLTEREILATLDHPFLPTLYASFQTSthLCFVMDYCPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 111 SLYNVLHgAEPLPYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVLkICDF--GTACDIQTH--- 185
Cdd:cd05574  87 ELFRLLQ-KQPGKRLPEEVARFYAAEVLLALEYLHLL---GFVYRDLKPENILLHESGHIM-LTDFdlSKQSSVTPPpvr 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 186 ---------MTNNK------------------GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05574 162 kslrkgsrrSSVKSieketfvaepsarsnsfvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPF 232
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
102-274 1.47e-11

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 65.11  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFGTACD 181
Cdd:cd05583  76 LILDYVNGGELFTHLYQRE---HFTESEVRIYIGEIVLALEHLHKL---GIIYRDIKLENILLDSEGHV-VLTDFGLSKE 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNK----GSAAWMAPEVFEG--SNYSEKCDVFSWGIILWEVITRRKPFDEIGGP------AFRIMWavhngTRP 249
Cdd:cd05583 149 FLPGENDRAysfcGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGERnsqseiSKRILK-----SHP 223
                       170       180
                ....*....|....*....|....*
gi 21735562 250 PLIKNLPKPIESLMTRCWSKDPSQR 274
Cdd:cd05583 224 PIPKTFSAEAKDFILKLLEKDPKKR 248
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
40-230 1.78e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 65.70  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQ-----IESESERKAFIVELRQLSRV-NHPNIVKLYGACLNP--VCLVMEYAEG 109
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGrlYAVKVlkkdvILQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPdrLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 GSLynVLHgAEPLPYYTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTA----CDIQTH 185
Cdd:cd05590  81 GDL--MFH-IQKSRRFDEARARFYAAEITSALMFLHD---KGIIYRDLKLDNVLLDHEGHC-KLADFGMCkegiFNGKTT 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21735562 186 MTNNkGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFD 230
Cdd:cd05590 154 STFC-GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFE 197
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
102-301 1.87e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 65.44  E-value: 1.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 102 LVMEYAEGGSLYNVLH--GAEPLPYYTAAHAMSwclQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAG--GTVLKICDFG 177
Cdd:cd14170  76 IVMECLDGGELFSRIQdrGDQAFTEREASEIMK---SIGEAIQYLHSIN---IAHRDVKPENLLYTSKrpNAILKLTDFG 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 TACDIQTH--MTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAF------RIMWAVHNGTRP 249
Cdd:cd14170 150 FAKETTSHnsLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmktRIRMGQYEFPNP 229
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 250 PLiKNLPKPIESLMTRCWSKDPSQRPSMEEivkIMTHlmryfPGADEPLQYP 301
Cdd:cd14170 230 EW-SEVSEEVKMLIRNLLKTEPTQRMTITE---FMNH-----PWIMQSTKVP 272
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
29-306 2.30e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 65.55  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   29 EEIDYKEIEVEEVVGRGAFGVVCKA--KWRAKDVAIKQIESeSERKAFIVELRQL-----------------SRVNHPNI 89
Cdd:PTZ00024   4 FSISERYIQKGAHLGEGTYGKVEKAydTLTGKIVAIKKVKI-IEISNDVTKDRQLvgmcgihfttlrelkimNEIKHENI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   90 VKLYGACLNP--VCLVMEYAEGgSLYNVLHGAEPLpyyTAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAG 167
Cdd:PTZ00024  83 MGLVDVYVEGdfINLVMDIMAS-DLKKVVDRKIRL---TESQVKCILLQILNGLNVLHK---WYFMHRDLSPANIFINSK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  168 GtVLKICDFG----TACDI-------------QTHMTNNKGSAAWMAPEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PTZ00024 156 G-ICKIADFGlarrYGYPPysdtlskdetmqrREEMTSKVVTLWYRAPELLMGAEkYHFAVDMWSVGCIFAELLTGKPLF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  230 ---DEIG--GPAFRIMwAVHNGTRPPLIKNLPK----------------PIES-----LMTRCWSKDPSQRPSMEEIVKi 283
Cdd:PTZ00024 235 pgeNEIDqlGRIFELL-GTPNEDNWPQAKKLPLyteftprkpkdlktifPNASddaidLLQSLLKLNPLERISAKEALK- 312
                        330       340
                 ....*....|....*....|...
gi 21735562  284 mtHlmRYFpgADEPLqyPCQYSD 306
Cdd:PTZ00024 313 --H--EYF--KSDPL--PCDPSQ 327
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
43-177 3.46e-11

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 60.92  E-value: 3.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  43 GRGAFGVV--CKAKWRAKDVAIKQIESESERKAFIVE-----LRQLSRVNhPNIVKLYGACLN--PVCLVMEYAEGGSLY 113
Cdd:cd13968   2 GEGASAKVfwAEGECTTIGVAVKIGDDVNNEEGEDLEsemdiLRRLKGLE-LNIPKVLVTEDVdgPNILLMELVKGGTLI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21735562 114 NVLHGAEPLPYYTAahamSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFG 177
Cdd:cd13968  81 AYTQEEELDEKDVE----SIMYQLAECMRLLHSFH---LIHRDLNNDNILLSEDGNV-KLIDFG 136
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
37-222 3.98e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 64.78  E-value: 3.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFI-VELRQLSRVNHP-----NIVKLYgACL---NPVCLVME 105
Cdd:cd14211   2 EVLEFLGRGTFGQVVKCWKRGTNeiVAIKILKNHPSYARQGqIEVSILSRLSQEnadefNFVRAY-ECFqhkNHTCLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGgSLYNVLHGAE--PLPyytAAHAMSWCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTV---LKICDFGTAC 180
Cdd:cd14211  81 MLEQ-NLYDFLKQNKfsPLP---LKYIRPILQQVLTALLKLKSL---GLIHADLKPENIMLVDPVRQpyrVKVIDFGSAS 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 181 DIQTHMTNNK-GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEV 222
Cdd:cd14211 154 HVSKAVCSTYlQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 196
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
34-232 3.99e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 65.04  E-value: 3.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLSR------VNHPNIVKLYGACLNP--VCLV 103
Cdd:cd05617  15 QDFDLIRVIGRGSYAKVLLVRLKKNDqiYAMKVVKKELVHDDEDIDWVQTEKhvfeqaSSNPFLVGLHSCFQTTsrLFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 104 MEYAEGGSLYNVLHGAEPLPyytAAHAMSWCLQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTVlKICDFGTACD-I 182
Cdd:cd05617  95 IEYVNGGDLMFHMQRQRKLP---EEHARFYAAEICIALNFLHE---RGIIYRDLKLDNVLLDADGHI-KLTDYGMCKEgL 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21735562 183 QTHMTNNK--GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEI 232
Cdd:cd05617 168 GPGDTTSTfcGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDII 219
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
34-229 4.16e-11

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 65.04  E-value: 4.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  34 KEIEVEEVVGRGAFGVVCKAKWRAKD--VAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACL--NPVCLVM 104
Cdd:cd05623  72 EDFEILKVIGRGAFGEVAVVKLKNADkvFAMKilnkwEMLKRAETACFREERDVLVNGDSQWITTLHYAFQddNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 105 EYAEGGSLYNVLHGAEP-LPYYTAAHAMSWCLQCSQGVAYLHsmqpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQ 183
Cdd:cd05623 152 DYYVGGDLLTLLSKFEDrLPEDMARFYLAEMVLAIDSVHQLH------YVHRDIKPDNILMDMNGHI-RLADFGSCLKLM 224
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21735562 184 THMTNNK----GSAAWMAPEVFEG-----SNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05623 225 EDGTVQSsvavGTPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLYGETPF 279
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
85-231 4.22e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 63.72  E-value: 4.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   85 NHPNIVKLYGAC--LNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMswcLQCSQGVAYLHSMQpkaLIHRDLKPPNL 162
Cdd:PHA03390  67 DNPNFIKLYYSVttLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKII---RQLVEALNDLHKHN---IIHNDIKLENV 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562  163 LLVAGGTVLKICDFGTaCDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDE 231
Cdd:PHA03390 141 LYDRAKDRIYLCDYGL-CKIIGTPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE 208
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
42-257 4.84e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 64.68  E-value: 4.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVVCKA--KWRAKDVAIKQI----ESESERKAFIVELRQLSRVNHPNIVKLygacLNPVCLVMEYAEGGSLYNV 115
Cdd:cd07875  32 IGSGAQGIVCAAydAILERNVAIKKLsrpfQNQTHAKRAYRELVLMKCVNHKNIIGL----LNVFTPQKSLEEFQDVYIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 116 LHGAEP-----LPYYTAAHAMSWCL-QCSQGVAYLHSmqpKALIHRDLKPPNlLLVAGGTVLKICDFGTACDIQTH--MT 187
Cdd:cd07875 108 MELMDAnlcqvIQMELDHERMSYLLyQMLCGIKHLHS---AGIIHRDLKPSN-IVVKSDCTLKILDFGLARTAGTSfmMT 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 188 NNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRR-------------KPFDEIGGPAFRIMWAVHNGTRpPLIKN 254
Cdd:cd07875 184 PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGvlfpgtdhidqwnKVIEQLGTPCPEFMKKLQPTVR-TYVEN 262

                ...
gi 21735562 255 LPK 257
Cdd:cd07875 263 RPK 265
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
42-286 5.35e-11

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 63.38  E-value: 5.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  42 VGRGAFGVV----CKAKWRAKDVAIKQIESES---ERKAFIVELRQLSRVNHPNIVKLYGACLN--PVCLVMEYAEGGSL 112
Cdd:cd05042   3 IGNGWFGKVllgeIYSGTSVAQVVVKELKASAnpkEQDTFLKEGQPYRILQHPNILQCLGQCVEaiPYLLVMEFCDLGDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 113 YNVLHGAEPlPYYTAAHAMS---WCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTA-CDIQT--HM 186
Cdd:cd05042  83 KAYLRSERE-HERGDSDTRTlqrMACEVAAGLAHLHKLN---FVHSDLALRNCLLTSDLTV-KIGDYGLAhSRYKEdyIE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 187 TNNKG--SAAWMAPEV---FEGS----NYSEKCDVFSWGIILWEVITR-RKPFDEIGGP---AFRIMWAVHNGTRPPLIK 253
Cdd:cd05042 158 TDDKLwfPLRWTAPELvteFHDRllvvDQTKYSNIWSLGVTLWELFENgAQPYSNLSDLdvlAQVVREQDTKLPKPQLEL 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 21735562 254 NLPKPIESLMTRCWsKDPSQRPSMEEIVKIMTH 286
Cdd:cd05042 238 PYSDRWYEVLQFCW-LSPEQRPAAEDVHLLLTY 269
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
35-229 6.92e-11

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 63.91  E-value: 6.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  35 EIEVEEVVGRGAFGVVCKAKWRA--KDVAIK-----QIESESERKAFIVELRQLSRVNHPNIVKLYGACLNP--VCLVME 105
Cdd:cd05597   2 DFEILKVIGRGAFGEVAVVKLKSteKVYAMKilnkwEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDEnyLYLVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGGSLYNVLHGAEP-LP-----YYTAAHAMSwclqcsqgvayLHSMQPKALIHRDLKPPNLLLVAGGTVlKICDFGTA 179
Cdd:cd05597  82 YYCGGDLLTLLSKFEDrLPeemarFYLAEMVLA-----------IDSIHQLGYVHRDIKPDNVLLDRNGHI-RLADFGSC 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21735562 180 CDIQTHMTNNK----GSAAWMAPEVFEGS-----NYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd05597 150 LKLREDGTVQSsvavGTPDYISPEILQAMedgkgRYGPECDWWSLGVCMYEMLYGETPF 208
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
40-229 7.07e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 63.47  E-value: 7.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  40 EVVGRGAFGVVCKAKWRAKD--VAIKQIESESERKAFIVELRQLS---RVNHPNIVKLYGACLN--PVCLVMEYAEG--- 109
Cdd:cd07872  12 EKLGEGTYATVFKGRSKLTEnlVALKEIRLEHEEGAPCTAIREVSllkDLKHANIVTLHDIVHTdkSLTLVFEYLDKdlk 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 110 ------GSLYNvLHGAEPLPYytaahamswclQCSQGVAYLHSmqpKALIHRDLKPPNLLLVAGGTvLKICDFG--TACD 181
Cdd:cd07872  92 qymddcGNIMS-MHNVKIFLY-----------QILRGLAYCHR---RKVLHRDLKPQNLLINERGE-LKLADFGlaRAKS 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21735562 182 IQTHMTNNKGSAAWM-APEVFEGSN-YSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd07872 156 VPTKTYSNEVVTLWYrPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLF 205
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
37-224 7.57e-11

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 63.95  E-value: 7.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESeseRKAF----IVE------LRQLSRVNHPNIVKL--YGACLNPVCL 102
Cdd:cd14225  46 EILEVIGKGSFGQVVKALDHKTNehVAIKIIRN---KKRFhhqaLVEvkildaLRRKDRDNSHNVIHMkeYFYFRNHLCI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAeGGSLY-----NVLHGAEPLPYYTAAHAMswcLQCsqgvayLHSMQPKALIHRDLKPPNLLLVA-GGTVLKICDF 176
Cdd:cd14225 123 TFELL-GMNLYelikkNNFQGFSLSLIRRFAISL---LQC------LRLLYRERIIHCDLKPENILLRQrGQSSIKVIDF 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21735562 177 GTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVIT 224
Cdd:cd14225 193 GSSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYT 240
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
136-281 9.07e-11

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 62.64  E-value: 9.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 136 QCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAGGTVlKICDFGTACDIQTHMTNNK---GSAAWMAPEVFEGSNYSEKCDV 212
Cdd:cd14187 115 QIILGCQYLHRNR---VIHRDLKLGNLFLNDDMEV-KIGDFGLATKVEYDGERKKtlcGTPNYIAPEVLSKKGHSFEVDI 190
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21735562 213 FSWGIILWEVITRRKPFDEiggpafrimwAVHNGTRPPLIKN---LPKPIE----SLMTRCWSKDPSQRPSMEEIV 281
Cdd:cd14187 191 WSIGCIMYTLLVGKPPFET----------SCLKETYLRIKKNeysIPKHINpvaaSLIQKMLQTDPTARPTINELL 256
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
32-295 1.30e-10

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 63.33  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEVeevVGRGAFGVV--CKAKWRAKDVAIKQ-IESESERKAFIVELRQ----LSRVNHPNIVKLYGAC--LNPVCL 102
Cdd:cd05629   2 DFHTVKV---IGKGAFGEVrlVQKKDTGKIYAMKTlLKSEMFKKDQLAHVKAerdvLAESDSPWVVSLYYSFqdAQYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 103 VMEYAEGGSLYNVLhgaepLPYYTAAHAMS--WCLQCSQGVAYLHSMqpkALIHRDLKPPNLLLVAGGTVlKICDFG--- 177
Cdd:cd05629  79 IMEFLPGGDLMTML-----IKYDTFSEDVTrfYMAECVLAIEAVHKL---GFIHRDIKPDNILIDRGGHI-KLSDFGlst 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 178 -----------------------------TACD-IQTHMTNNKGSAAW-----------------MAPEVFEGSNYSEKC 210
Cdd:cd05629 150 gfhkqhdsayyqkllqgksnknridnrnsVAVDsINLTMSSKDQIATWkknrrlmaystvgtpdyIAPEIFLQQGYGQEC 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 211 DVFSWGIILWEVITRRKPF-DEIGGPAFR-IMWAVHNGTRPPLIkNLPKPIESLMTRCWSkDPSQRPSMEEIVKIMTHlm 288
Cdd:cd05629 230 DWWSLGAIMFECLIGWPPFcSENSHETYRkIINWRETLYFPDDI-HLSVEAEDLIRRLIT-NAENRLGRGGAHEIKSH-- 305

                ....*..
gi 21735562 289 RYFPGAD 295
Cdd:cd05629 306 PFFRGVD 312
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
77-229 1.45e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 63.32  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562   77 ELRQLSRVNHPNIVKLYGACLNP--VCLVMEYAEGgSLYNVLHGAEPLPYYTAAHAMSWCLQcsqGVAYLHSmqpKALIH 154
Cdd:PHA03207 136 EIDILKTISHRAIINLIHAYRWKstVCMVMPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLE---ALAYLHG---RGIIH 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  155 RDLKPPNLLLVAGGTVLkICDFGTACDIQTHMTNNK-----GSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:PHA03207 209 RDVKTENIFLDEPENAV-LGDFGAACKLDAHPDTPQcygwsGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
37-222 1.60e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 62.74  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  37 EVEEVVGRGAFGVVCKAKWRAKD--VAIKQIESE-SERKAFIVELRQLSRVNHPN-----IVKLYgACL---NPVCLVME 105
Cdd:cd14229   3 EVLDFLGRGTFGQVVKCWKRGTNeiVAVKILKNHpSYARQGQIEVGILARLSNENadefnFVRAY-ECFqhrNHTCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 106 YAEGgSLYNVLHGAE--PLPYytaaHAMSWCLQcsQGVAYLHSMQPKALIHRDLKPPNLLL---VAGGTVLKICDFGTAC 180
Cdd:cd14229  82 MLEQ-NLYDFLKQNKfsPLPL----KVIRPILQ--QVATALKKLKSLGLIHADLKPENIMLvdpVRQPYRVKVIDFGSAS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21735562 181 DI-QTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEV 222
Cdd:cd14229 155 HVsKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAEL 197
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
32-229 1.77e-10

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 61.76  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  32 DYKEIEvEEVVGRGAFGVVCKAKWRAK-DVAIKQIESESErkAFIVELRQLSRVNHPNIVKLYGACLN---PVCLVMEYA 107
Cdd:cd14109   3 ELYEIG-EEDEKRAAQGAPFHVTERSTgRNFLAQLRYGDP--FLMREVDIHNSLDHPNIVQMHDAYDDeklAVTVIDNLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 108 EGG--SLYNVLHGAEplpYYTAAHAMSWCLQCSQGVAYLHSMQpkaLIHRDLKPPNLLLVAggTVLKICDFGTACDIQTH 185
Cdd:cd14109  80 STIelVRDNLLPGKD---YYTERQVAVFVRQLLLALKHMHDLG---IAHLDLRPEDILLQD--DKLKLADFGQSRRLLRG 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21735562 186 M--TNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPF 229
Cdd:cd14109 152 KltTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPF 197
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
73-282 2.04e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 61.88  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562  73 AFIVELRQLSRVNHPNIVKLYGACLNPV--CLVMEYAEGGSLYNVLH-GAEPLpyyTAAHAMSWCLQCSQGVAYLhsmQP 149
Cdd:cd05077  54 AFFETASMMRQVSHKHIVLLYGVCVRDVenIMVEEFVEFGPLDLFMHrKSDVL---TTPWKFKVAKQLASALSYL---ED 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21735562 150 KALIHRDLKPPNLLLV------AGGTVLKICDFGTACDIQTHMTNNKgSAAWMAPEVFEGS-NYSEKCDVFSWGIILWEV 222
Cdd:cd05077 128 KDLVHGNVCTKNILLAregidgECGPFIKLSDPGIPITVLSRQECVE-RIPWIAPECVEDSkNLSIAADKWSFGTTLWEI 206
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21735562 223 ITRRK-PFDEIGGPAFRIMWAVHNGTRPPLIKNLPKpiesLMTRCWSKDPSQRPSMEEIVK 282
Cdd:cd05077 207 CYNGEiPLKDKTLAEKERFYEGQCMLVTPSCKELAD----LMTHCMNYDPNQRPFFRAIMR 263
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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