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Conserved domains on  [gi|42794767|ref|NP_976226|]
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mitogen-activated protein kinase kinase kinase 3 isoform 1 [Homo sapiens]

Protein Classification

mitogen-activated protein kinase kinase kinase 3( domain architecture ID 10157387)

mitogen-activated protein kinase kinase kinase 3 (MAP3K3) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; MAP3Ks phosphorylate and activate MAP2Ks, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
392-652 0e+00

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: 568.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd06625   1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQD--EKSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd06625  79 IFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFL 631
Cdd:cd06625 159 -TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPPHVSEDARDFL 237
                       250       260
                ....*....|....*....|..
gi 42794767 632 RRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06625 238 SLIFVRnKKQRPSAEELLSHSF 259
PB1_Mekk2_3 cd06405
The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 ...
76-154 2.95e-41

The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain.


:

Pssm-ID: 99726  Cd Length: 79  Bit Score: 144.45  E-value: 2.95e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767  76 VRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQ 154
Cdd:cd06405   1 VRIKFEHNGEKRIIQFPRPVKFKDLQQKVTTAFGQPMDLHYTNNELLIPLKNQEDLDRAIELLDRSPHMKSLRILLSAP 79
 
Name Accession Description Interval E-value
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
392-652 0e+00

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: 568.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd06625   1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQD--EKSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd06625  79 IFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFL 631
Cdd:cd06625 159 -TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPPHVSEDARDFL 237
                       250       260
                ....*....|....*....|..
gi 42794767 632 RRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06625 238 SLIFVRnKKQRPSAEELLSHSF 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
393-652 3.65e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 306.38  E-value: 3.65e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK----KIKKDRERILREIKILKKLKHPNIVRLYDVFED--EDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMsg 552
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    553 tgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH--ISEHGRDF 630
Cdd:smart00220 153 --LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwdISPEAKDL 230
                          250       260
                   ....*....|....*....|...
gi 42794767    631 LRRIFV-EARQRPSAEELLTHHF 652
Cdd:smart00220 231 IRKLLVkDPEKRLTAEEALQHPF 253
Pkinase pfam00069
Protein kinase domain;
393-650 5.70e-87

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 272.17  E-value: 5.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILR---EIKILKKLNHPNIVRLYDAFED--KDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSG 552
Cdd:pfam00069  76 VLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLARQLN----SG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPT-NPQLPSHISEHGRDFL 631
Cdd:pfam00069 152 SSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYaFPELPSNLSEEAKDLL 231
                         250       260
                  ....*....|....*....|
gi 42794767   632 RRIF-VEARQRPSAEELLTH 650
Cdd:pfam00069 232 KKLLkKDPSKRLTATEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
392-652 1.86e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 160.68  E-value: 1.86e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVdtgRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHE-RIVQYYGCLRDraEKTL 470
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVL--AKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQD--EGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-VKLGDFGASKRLQ 546
Cdd:COG0515  74 YLVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TICMSGTG---MRSVTGTPYWMSPEVISG---EGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI---------- 610
Cdd:COG0515 154 DPGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptp 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42794767 611 -ATQPTNPQLPSHISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:COG0515 234 sLASPLSPSNPELISKAASDLLKKLLaKDPKNRLSSSSDLSHDL 277
PB1_Mekk2_3 cd06405
The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 ...
76-154 2.95e-41

The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain.


Pssm-ID: 99726  Cd Length: 79  Bit Score: 144.45  E-value: 2.95e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767  76 VRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQ 154
Cdd:cd06405   1 VRIKFEHNGEKRIIQFPRPVKFKDLQQKVTTAFGQPMDLHYTNNELLIPLKNQEDLDRAIELLDRSPHMKSLRILLSAP 79
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
396-632 1.69e-31

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 125.32  E-value: 1.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:PTZ00263  23 GETLGTGSFGRVRIAKHKGTGEYYAIKCLK--KREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQD--ENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ----TICms 551
Cdd:PTZ00263  99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPdrtfTLC-- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  552 gtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDFL 631
Cdd:PTZ00263 177 --------GTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL--KFPNWFDGRARDLV 246

                 .
gi 42794767  632 R 632
Cdd:PTZ00263 247 K 247
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
472-598 6.01e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 109.50  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG---Askrlqti 548
Cdd:NF033483  84 IVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiarA------- 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 42794767  549 cMSGTGM---RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:NF033483 157 -LSSTTMtqtNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
75-151 1.44e-14

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 69.15  E-value: 1.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767     75 DVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFG---QPLDLHYMNNELS-ILLKNQDDLDKAIDILDRSSSmKSLRIL 150
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGldnQSFTLKYQDEDGDlVSLTSDEDLEEAIEEYDSLGS-KKLRLH 79

                   .
gi 42794767    151 L 151
Cdd:smart00666  80 V 80
PB1 pfam00564
PB1 domain;
75-151 2.81e-14

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 68.47  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    75 DVRIKFEHNGE-RRIIAFSRPVKYEDVEHKVTTVFGQP---LDLHYMNNELS-ILLKNQDDLDKAIDILdRSSSMKSLRI 149
Cdd:pfam00564   1 TVRLKLRYGGGiRRFLSVSRGISFEELRALVEQRFGLDdvdFKLKYPDEDGDlVSLTSDEDLEEALEEA-RSLGSKSLRL 79

                  ..
gi 42794767   150 LL 151
Cdd:pfam00564  80 HV 81
 
Name Accession Description Interval E-value
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
392-652 0e+00

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: 568.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd06625   1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQD--EKSLS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd06625  79 IFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFL 631
Cdd:cd06625 159 -TGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPPHVSEDARDFL 237
                       250       260
                ....*....|....*....|..
gi 42794767 632 RRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06625 238 SLIFVRnKKQRPSAEELLSHSF 259
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
385-655 0e+00

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: 557.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 385 KSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD 464
Cdd:cd06651   1 KSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 RAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd06651  81 RAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHIS 624
Cdd:cd06651 161 LQTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHIS 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 625 EHGRDFLRRIFVEARQRPSAEELLTHHFAQL 655
Cdd:cd06651 241 EHARDFLGCIFVEARHRPSAEELLRHPFAQL 271
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
390-653 0e+00

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: 555.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKT 469
Cdd:cd06652   1 PTNWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQERT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd06652  81 LSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQTIC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRD 629
Cdd:cd06652 161 LSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAHVSDHCRD 240
                       250       260
                ....*....|....*....|....
gi 42794767 630 FLRRIFVEARQRPSAEELLTHHFA 653
Cdd:cd06652 241 FLKRIFVEAKLRPSADELLRHTFV 264
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
390-652 0e+00

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: 536.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKT 469
Cdd:cd06653   1 PVNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd06653  81 LSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTIC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRD 629
Cdd:cd06653 161 MSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPDGVSDACRD 240
                       250       260
                ....*....|....*....|...
gi 42794767 630 FLRRIFVEARQRPSAEELLTHHF 652
Cdd:cd06653 241 FLRQIFVEEKRRPTAEFLLRHPF 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
392-652 6.25e-147

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: 426.55  E-value: 6.25e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskEVSALECEIQLLKNLQHERIVQYYGClrDRAEKTLT 471
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEE---ELEALEREIRILSSLKHPNIVRYLGT--ERTENTLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMs 551
Cdd:cd06606  76 IFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIAT- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYE-AMAAIFKIATQPTNPQLPSHISEHGRDF 630
Cdd:cd06606 155 GEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGnPVAALFKIGSSGEPPPIPEHLSEEAKDF 234
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06606 235 LRKCLQrDPKKRPTADELLQHPF 257
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
393-652 1.28e-103

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: 315.50  E-value: 1.28e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:cd06632   2 WQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTERE--EDNLYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMsg 552
Cdd:cd06632  80 FLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSF-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 tgMRSVTGTPYWMSPEVIS--GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDF 630
Cdd:cd06632 158 --AKSFKGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIPDHLSPDAKDF 235
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06632 236 IRLCLqRDPEDRPTASQLLEHPF 258
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
391-652 1.49e-100

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: 307.83  E-value: 1.49e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 391 INWRRGKLLGQGAFGRVYlCYDVDTGRELASKQVQFDPDSPETS-KEVSALECEIQLLKNLQHERIVQYYG-CLRDraeK 468
Cdd:cd06631   1 IQWKKGNVLGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKAeKEYEKLQEEVDLLKTLKHVNIVGYLGtCLED---N 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd06631  77 VVSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCIN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTG---MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI-ATQPTNPQLPSHIS 624
Cdd:cd06631 157 LSSGSQsqlLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgSGRKPVPRLPDKFS 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 625 EHGRDF----LRRifvEARQRPSAEELLTHHF 652
Cdd:cd06631 237 PEARDFvhacLTR---DQDERPSAEQLLKHPF 265
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
393-652 3.65e-100

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 306.38  E-value: 3.65e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK----KIKKDRERILREIKILKKLKHPNIVRLYDVFED--EDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMsg 552
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    553 tgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH--ISEHGRDF 630
Cdd:smart00220 153 --LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwdISPEAKDL 230
                          250       260
                   ....*....|....*....|...
gi 42794767    631 LRRIFV-EARQRPSAEELLTHHF 652
Cdd:smart00220 231 IRKLLVkDPEKRLTAEEALQHPF 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
393-652 3.04e-96

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: 296.75  E-value: 3.04e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKE----VSALECEIQLLKNLQHERIVQYYGCLRDraEK 468
Cdd:cd06628   2 WIKGALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRkksmLDALQREIALLRELQHENIVQYLGSSSD--AN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd06628  80 HLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEAN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGT--GMR-SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPSHISE 625
Cdd:cd06628 160 SLSTKnnGARpSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIG-ENASPTIPSNISS 238
                       250       260
                ....*....|....*....|....*...
gi 42794767 626 HGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06628 239 EARDFLEKTFeIDHNKRPTADELLKHPF 266
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
396-650 1.31e-93

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: 289.51  E-value: 1.31e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFME 475
Cdd:cd06627   5 GDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKS---DLKSVMGEIDLLKKLNHPNIVKYIGSVKTKD--SLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticMSGTGM 555
Cdd:cd06627  80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLN---EVEKDE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPtNPQLPSHISEHGRDFLRRIF 635
Cdd:cd06627 157 NSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDD-HPPLPENISPELRDFLLQCF 235
                       250
                ....*....|....*.
gi 42794767 636 -VEARQRPSAEELLTH 650
Cdd:cd06627 236 qKDPTLRPSAKELLKH 251
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
391-653 6.93e-93

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: 288.13  E-value: 6.93e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 391 INWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKE-----VSALECEIQLLKNLQHERIVQYYGClrDR 465
Cdd:cd06629   1 FKWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSrqktvVDALKSEIDTLKDLDHPNIVQYLGF--EE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 AEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL 545
Cdd:cd06629  79 TEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMrSVTGTPYWMSPEVI--SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS-- 621
Cdd:cd06629 159 DDIYGNNGAT-SMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPEdv 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 42794767 622 HISEHGRDFLRRIF-VEARQRPSAEELLTHHFA 653
Cdd:cd06629 238 NLSPEALDFLNACFaIDPRDRPTAAELLSHPFL 270
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
393-653 9.46e-90

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: 279.96  E-value: 9.46e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd06626   2 WQRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIAD---EMKVLEGLDHPNLVRYYGVEVHREE--VYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL--QTICM 550
Cdd:cd06626  77 FMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLknNTTTM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISG---EGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAI-FKIATQPTnPQLPSH--IS 624
Cdd:cd06626 157 APGEVNSLVGTPAYMAPEVITGnkgEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAImYHVGMGHK-PPIPDSlqLS 235
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 625 EHGRDFLRRIFV-EARQRPSAEELLTHHFA 653
Cdd:cd06626 236 PEGKDFLSRCLEsDPKKRPTASELLDHPFI 265
Pkinase pfam00069
Protein kinase domain;
393-650 5.70e-87

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 272.17  E-value: 5.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILR---EIKILKKLNHPNIVRLYDAFED--KDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSG 552
Cdd:pfam00069  76 VLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLARQLN----SG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPT-NPQLPSHISEHGRDFL 631
Cdd:pfam00069 152 SSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYaFPELPSNLSEEAKDLL 231
                         250       260
                  ....*....|....*....|
gi 42794767   632 RRIF-VEARQRPSAEELLTH 650
Cdd:pfam00069 232 KKLLkKDPSKRLTATEALQH 251
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
392-650 4.79e-81

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: 257.36  E-value: 4.79e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSP-ETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktL 470
Cdd:cd06630   1 HWLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSsEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSH--F 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-VKLGDFGASKRLQT-I 548
Cdd:cd06630  79 NIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASkG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEA---MAAIFKIATQPTNPQLPSHISE 625
Cdd:cd06630 159 TGAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKIsnhLALIFKIASATTPPPIPEHLSP 238
                       250       260
                ....*....|....*....|....*.
gi 42794767 626 HGRDFLRRIFVEARQ-RPSAEELLTH 650
Cdd:cd06630 239 GLRDVTLRCLELQPEdRPPARELLKH 264
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
393-652 1.84e-80

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: 255.21  E-value: 1.84e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGC-LRDRaekTLT 471
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKI--NLESKEKKESILN---EIAILKKCKHPNIVKYYGSyLKKD---ELW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticm 550
Cdd:cd05122  74 IVMEFCSGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLS---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGR 628
Cdd:cd05122 150 DGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGP-PGLrnPKKWSKEFK 228
                       250       260
                ....*....|....*....|....*
gi 42794767 629 DFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd05122 229 DFLKKCLQkDPEKRPTAEQLLKHPF 253
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
397-652 9.02e-77

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: 246.39  E-value: 9.02e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 476
Cdd:cd06609   7 ERIGKGSFGEVYKGIDKRTNQVVAIKVIDLE----EAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGS--KLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKaYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMsgtgM 555
Cdd:cd06609  81 CGGGSVLDLLK-PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLtSTMSK----R 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTN--PQLPSH-ISEHGRDFLR 632
Cdd:cd06609 156 NTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLI---PKNnpPSLEGNkFSKPFKDFVE 232
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIFVEA-RQRPSAEELLTHHF 652
Cdd:cd06609 233 LCLNKDpKERPSAKELLKHKF 253
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
399-652 1.30e-74

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: 240.39  E-value: 1.30e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdsPE-TSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYM 477
Cdd:cd06624  16 LGKGTFGVVYAARDLSTQVRIAIKEI------PErDSREVQPLHEEIALHSRLSHKNIVQYLGSVSE--DGFFKIFMEQV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKA-YGALT--ESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS-AGNVKLGDFGASKRLQTICMSGT 553
Cdd:cd06624  88 PGGSLSALLRSkWGPLKdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCTE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 gmrSVTGTPYWMSPEVI-SGE-GYGRKADVWSLGCTVVEMLTEKPPWAEY-EAMAAIFKIATQPTNPQLPSHISEHGRDF 630
Cdd:cd06624 168 ---TFTGTLQYMAPEVIdKGQrGYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVGMFKIHPEIPESLSEEAKSF 244
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06624 245 ILRCFePDPDKRATASDLLQDPF 267
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
398-652 5.47e-74

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: 238.32  E-value: 5.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsaleceIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYM 477
Cdd:cd06612  10 KLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKE-------ISILKQCDSPYIVKYYGSYF--KNTDLWIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMR 556
Cdd:cd06612  81 GAGSVSDIMKITNkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD---TMAKRN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDFLRRI 634
Cdd:cd06612 158 TVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPP-PTLsdPEKWSPEFNDFVKKC 236
                       250
                ....*....|....*....
gi 42794767 635 FV-EARQRPSAEELLTHHF 652
Cdd:cd06612 237 LVkDPEERPSAIQLLQHPF 255
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
399-652 6.04e-69

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: 225.17  E-value: 6.04e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd06614   8 IGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIIN------EILIMKECKHPNIVDYYDSYLV--GDELWVVMEYMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSGTGMR- 556
Cdd:cd06614  80 GGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLT----KEKSKRn 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDFLRRI 634
Cdd:cd06614 156 SVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGI-PPLknPEKWSPEFKDFLNKC 234
                       250
                ....*....|....*....
gi 42794767 635 FV-EARQRPSAEELLTHHF 652
Cdd:cd06614 235 LVkDPEKRPSAEELLQHPF 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
392-650 2.25e-67

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: 220.85  E-value: 2.25e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKII---DKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIET--ENKIY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtiCMS 551
Cdd:cd14003  76 LVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE----FRG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHGRDF 630
Cdd:cd14003 152 GSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILK--GKYPIPSHLSPDARDL 229
                       250       260
                ....*....|....*....|.
gi 42794767 631 LRRIF-VEARQRPSAEELLTH 650
Cdd:cd14003 230 IRRMLvVDPSKRITIEEILNH 250
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
392-652 3.13e-67

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: 220.80  E-value: 3.13e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPetsKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLT 471
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSE---KEREEALNEVKLLSKLKHPNIVKYYESFEEN--GKLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGS----VKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQt 547
Cdd:cd08215  76 IVMEYADGGDlaqkIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLE- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 icmSGTGM-RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPwaeYEA--MAAIF-KIATQPTNPqLPSHI 623
Cdd:cd08215 155 ---STTDLaKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHP---FEAnnLPALVyKIVKGQYPP-IPSQY 227
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 624 SEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd08215 228 SSELRDLVNSMLqKDPEKRPSANEILSSPF 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
396-650 5.80e-65

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: 214.65  E-value: 5.80e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd05117   5 GKVLGRGSFGVVRLAVHKKTGEEYAVKIID---KKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFED--DKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRLQticmSG 552
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILlasKDPDSPIKIIDFGLAKIFE----EG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP-WAEYEAMaaIFKIATQ---PTNPQLPSHISEHGR 628
Cdd:cd05117 156 EKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPfYGETEQE--LFEKILKgkySFDSPEWKNVSEEAK 233
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd05117 234 DLIKRLLvVDPKKRLTAAEALNH 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
392-648 7.89e-64

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: 211.68  E-value: 7.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRE--RFLREARALARLSHPNIVRVYDVGED--DGRPY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd14014  77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP--QLPSHISEhgrd 629
Cdd:cd14014 157 QTGS--VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPpsPLNPDVPP---- 230
                       250       260
                ....*....|....*....|....*
gi 42794767 630 FLRRIF-----VEARQRP-SAEELL 648
Cdd:cd14014 231 ALDAIIlralaKDPEERPqSAAELL 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
399-650 4.15e-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: 205.58  E-value: 4.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVI----PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFET--ENFLYLVMEYCE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRS 557
Cdd:cd00180  75 GGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 558 vTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMltekppwaeyeamaaifkiatqptnpqlpshisEHGRDFLRRIFV- 636
Cdd:cd00180 155 -TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQy 200
                       250
                ....*....|....
gi 42794767 637 EARQRPSAEELLTH 650
Cdd:cd00180 201 DPKKRPSAKELLEH 214
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
399-650 1.68e-61

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: 205.86  E-value: 1.68e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELA---------SKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKT 469
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAikifnksrlRKRREGKNDRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDPESDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVK--DQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqt 547
Cdd:cd14008  81 LYLVLEYCEGGPVMelDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 ICMSGTGMRSVT-GTPYWMSPEVISGEGY---GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHI 623
Cdd:cd14008 157 MFEDGNDTLQKTaGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPEL 236
                       250       260
                ....*....|....*....|....*...
gi 42794767 624 SEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14008 237 SPELKDLLRRMLEkDPEKRITLKEIKEH 264
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
399-648 3.61e-61

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: 204.31  E-value: 3.61e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVdtGRELASKQVQFDPDSPETSKEvsaLECEIQLLKNLQHERIVQYYG-CLRDraeKTLTIFMEYM 477
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKE---FRREVSILSKLRHPNIVQFIGaCLSP---PPLCIVTEYM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMR 556
Cdd:cd13999  73 PGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS---TTEKMT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEGYGRKADVWSLGctVV--EMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHgrdfLRRI 634
Cdd:cd13999 150 GVVGTPRWMAPEVLRGEPYTEKADVYSFG--IVlwELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPE----LSKL 223
                       250
                ....*....|....*....
gi 42794767 635 FV-----EARQRPSAEELL 648
Cdd:cd13999 224 IKrcwneDPEKRPSFSEIV 242
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
394-652 4.05e-60

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: 201.63  E-value: 4.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIF 473
Cdd:cd14099   4 RRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQRE--KLKSEIKIHRSLKHPNIVKFHDCFED--EENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmsgT 553
Cdd:cd14099  80 LELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEY-----D 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVT--GTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKIATQpTNPQLPSH--ISEHGR 628
Cdd:cd14099 155 GERKKTlcGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPF-ETSDVKETYKRIKK-NEYSFPSHlsISDEAK 232
                       250       260
                ....*....|....*....|....*
gi 42794767 629 DFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14099 233 DLIRSMLqPDPTKRPSLDEILSHPF 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
394-654 1.23e-59

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: 200.90  E-value: 1.23e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDraEKTLTIF 473
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVD-GDEEFRKQLLR---ELKTLRSCESPYVVKCYGAFYK--EGEISIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSG 552
Cdd:cd06623  78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLEN---TL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAIFKIATqptnPQLPS-HISE 625
Cdd:cd06623 155 DQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPpgqpsfFELMQAICDGPP----PSLPAeEFSP 230
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 626 HGRDFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd06623 231 EFRDFISACLQkDPKKRPSAAELLQHPFIK 260
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
393-652 2.04e-59

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: 200.78  E-value: 2.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetsKEVSALECEIQLLKNLQH---ERIVQYYGCLRDraEKT 469
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD----DDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLK--GPS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQtic 549
Cdd:cd06917  77 LWIIMDYCEGGSIRTLMRA-GPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLN--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSV-TGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIA-TQPtnPQLP-SHISE 625
Cdd:cd06917 153 -QNSSKRSTfVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPkSKP--PRLEgNGYSP 229
                       250       260
                ....*....|....*....|....*...
gi 42794767 626 HGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06917 230 LLKEFVAACLdEEPKDRLSADELLKSKW 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
396-652 8.39e-59

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: 198.08  E-value: 8.39e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd14007   5 GKPLGKGKFGNVYLAREKKSGFIVALKVISKS--QLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFED--KKRIYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-----ASKRLQTICm 550
Cdd:cd14007  81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGwsvhaPSNRRKTFC- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 sgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQptNPQLPSHISEHGRDF 630
Cdd:cd14007 160 ---------GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV--DIKFPSSVSPEAKDL 228
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14007 229 ISKLLQkDPSKRLSLEQVLNHPW 251
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
399-653 1.23e-58

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: 197.91  E-value: 1.23e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDspetsKEVSALECEIQLLKNLQHERIVQYYGC-LRdraEKTLTIFMEYM 477
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVIKLEPG-----DDFEIIQQEISMLKECRHPNIVAYFGSyLR---RDKLWIVMEYC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTIcmsgTGMR 556
Cdd:cd06613  80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLtATI----AKRK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGE---GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTNPQLPSHISEHGR----- 628
Cdd:cd06613 156 SFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLI---PKSNFDPPKLKDKEKwspdf 232
                       250       260
                ....*....|....*....|....*..
gi 42794767 629 -DFLRRIFV-EARQRPSAEELLTHHFA 653
Cdd:cd06613 233 hDFIKKCLTkNPKKRPTATKLLQHPFV 259
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
399-652 3.66e-55

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: 188.59  E-value: 3.66e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSaleCEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMP 478
Cdd:cd13983   9 LGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFK---QEIEILKSLKHPNIIKFYDSWESKSKKEVIFITELMT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANILRDSA-GNVKLGDFGASKRLQTicmsgTGM 555
Cdd:cd13983  86 SGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNtGEVKIGDLGLATLLRQ-----SFA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHG-RDFLRRI 634
Cdd:cd13983 161 KSVIGTPEFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESLSKVKDPElKDFIEKC 239
                       250
                ....*....|....*...
gi 42794767 635 FVEARQRPSAEELLTHHF 652
Cdd:cd13983 240 LKPPDERPSARELLEHPF 257
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
399-654 1.68e-54

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: 187.64  E-value: 1.68e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQI-----ESEEELEDFMVEIDILSECKHPNIVGLYEAYFY--ENKLWILIEFCD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmsgTGMRS 557
Cdd:cd06611  86 GGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKS-----TLQKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 558 VT--GTPYWMSPEVISGEG-----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGR 628
Cdd:cd06611 161 DTfiGTPYWMAPEVVACETfkdnpYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEP-PTLdqPSKWSSSFN 239
                       250       260
                ....*....|....*....|....*..
gi 42794767 629 DFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd06611 240 DFLKSCLVkDPDDRPTAAELLKHPFVS 266
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
397-652 1.59e-53

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: 184.28  E-value: 1.59e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEY 476
Cdd:cd08217   6 ETIGKGSFGTVRKVRRKSDGKILVWKEIDY---GKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANTTLYIVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGS----VKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-----IVHRDIKGANILRDSAGNVKLGDFGASKRLQT 547
Cdd:cd08217  83 CEGGDlaqlIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLARVLSH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 ICMSGTgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPqLPSHISEHG 627
Cdd:cd08217 163 DSSFAK---TYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPR-IPSRYSSEL 238
                       250       260
                ....*....|....*....|....*.
gi 42794767 628 RDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd08217 239 NEVIKSMLnVDPDKRPSVEELLQLPL 264
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
393-652 3.67e-53

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: 183.66  E-value: 3.67e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskevsALECEIQLLKNL-QHERIVQYYGCLRDR----AE 467
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEE------EIKLEINILRKFsNHPNIATFYGAFIKKdppgGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAY----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd06608  82 DQLWLVMEYCGGGSVTDLVKGLrkkgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RLQTicmsgTGMR--SVTGTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTn 616
Cdd:cd06608 162 QLDS-----TLGRrnTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPP- 235
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 617 PQL--PSHISEHGRDFLRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06608 236 PTLksPEKWSKEFNDFISECLIKnYEQRPFTEELLEHPF 274
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
399-652 1.61e-51

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: 179.09  E-value: 1.61e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskeVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06610   9 IGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS----MDELRKEIQAMSQCNHPNVVSYYTSFVVGDE--LWLVMPLLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLK---AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSGTG 554
Cdd:cd06610  83 GGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLaTGGDRTRKV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQLPSHI-----SEHGR 628
Cdd:cd06610 163 RKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDP-PSLETGAdykkySKSFR 241
                       250       260
                ....*....|....*....|....*
gi 42794767 629 DFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06610 242 KMISLCLQkDPSKRPTAEELLKHKF 266
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
398-650 1.93e-50

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: 176.13  E-value: 1.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYM 477
Cdd:cd14098   7 RLGSGTFAEVKKAVEVETGKMRAIKQIV-KRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYED--DQHIYLVMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQTicmsGTGM 555
Cdd:cd14098  84 EGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILitQDDPVIVKISDFGLAKVIHT----GTFL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGE------GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI--ATQPTNPQLPSHISEHG 627
Cdd:cd14098 160 VTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIrkGRYTQPPLVDFNISEEA 239
                       250       260
                ....*....|....*....|....
gi 42794767 628 RDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14098 240 IDFILRLLdVDPEKRMTAAQALDH 263
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
399-652 4.79e-50

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: 174.84  E-value: 4.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetsKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDE----ALQKQILRELDVLHKCNSPYIVGFYGAFYS--EGDISICMEYMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLqTICMSGTgmrs 557
Cdd:cd06605  83 GGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQL-VDSLAKT---- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 558 VTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEK---PPWAEYEAMaAIFKIATQPTN---PQLPSHI-SEHGRDF 630
Cdd:cd06605 158 FVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRfpyPPPNAKPSM-MIFELLSYIVDeppPLLPSGKfSPDFQDF 236
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06605 237 VSQCLQkDPTERPSYKELMEHPF 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
399-652 1.24e-49

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: 173.47  E-value: 1.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKK--EIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQT--EEKLYLVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmSGTGMRSV 558
Cdd:cd05123  77 GGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL-----SSDGDRTY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 T--GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP-WAEYeaMAAIF-KIATQPtnPQLPSHISEHGRDFLRRI 634
Cdd:cd05123 152 TfcGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPfYAEN--RKEIYeKILKSP--LKFPEYVSPEAKSLISGL 227
                       250       260
                ....*....|....*....|..
gi 42794767 635 FV---EAR-QRPSAEELLTHHF 652
Cdd:cd05123 228 LQkdpTKRlGSGGAEEIKAHPF 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
396-648 2.89e-49

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: 172.60  E-value: 2.89e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFME 475
Cdd:cd08529   5 LNKLGKGSFGVVYKVVRKVDGRVYALKQIDI---SRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKG--KLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 553
Cdd:cd08529  80 YAENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSD---TTN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPqLPSHISEHGRDFLRR 633
Cdd:cd08529 157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPP-ISASYSQDLSQLIDS 235
                       250
                ....*....|....*.
gi 42794767 634 IFV-EARQRPSAEELL 648
Cdd:cd08529 236 CLTkDYRQRPDTTELL 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
393-652 9.25e-49

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: 171.26  E-value: 9.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd06647   9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNL---QQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDE--LWV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSG 552
Cdd:cd06647  82 VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMrsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDF 630
Cdd:cd06647 161 STM---VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDF 236
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06647 237 LNRCLeMDVEKRGSAKELLQHPF 259
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
399-652 1.06e-48

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: 172.22  E-value: 1.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDsPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMP 478
Cdd:cd06621   9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPN-PDVQKQILR---ELEINKSCASPYIVKYYGAFLDEQDSSIGIAMEYCE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSV----KDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTiCMSGTg 554
Cdd:cd06621  85 GGSLdsiyKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVN-SLAGT- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 mrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMAAIFK----IATQPtNPQLPSHI------ 623
Cdd:cd06621 163 ---FTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFpPEGEPPLGPIEllsyIVNMP-NPELKDEPengikw 238
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 624 SEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06621 239 SESFKDFIEKCLEkDGTRRPGPWQMLAHPW 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
399-652 5.60e-48

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: 168.94  E-value: 5.60e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISR---KKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKT--EDFIYLVLEYCA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKRLQTICMSGTgm 555
Cdd:cd14009  76 GGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMAET-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 rsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---------AEYEAMAAIFKIAtqptnpqLPSHISEH 626
Cdd:cd14009 154 --LCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFrgsnhvqllRNIERSDAVIPFP-------IAAQLSPD 224
                       250       260
                ....*....|....*....|....*..
gi 42794767 627 GRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14009 225 CKDLLRRLLrRDPAERISFEEFFAHPF 251
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
399-652 1.23e-47

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: 169.44  E-value: 1.23e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMP 478
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIE-----TKSEEELEDYMVEIEILATCNHPYIVKLLGAFY--WDGKLWIMIEFCP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKD-QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS-KRLQTIcmsgTGMR 556
Cdd:cd06644  93 GGAVDAiMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSaKNVKTL----QRRD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEG-----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIA-TQPTNPQLPSHISEHGRDF 630
Cdd:cd06644 169 SFIGTPYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAkSEPPTLSQPSKWSMEFRDF 248
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06644 249 LKTALdKHPETRPSAAQLLEHPF 271
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
392-652 4.47e-47

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: 166.66  E-value: 4.47e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLT 471
Cdd:cd14081   2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIV--NKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENK--KYLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG------ASKRL 545
Cdd:cd14081  78 LVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmaslqpEGSLL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICmsgtgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPtnPQLPSHIS 624
Cdd:cd14081 158 ETSC----------GSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV--FHIPHFIS 225
                       250       260
                ....*....|....*....|....*....
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14081 226 PDAQDLLRRMLeVNPEKRITIEEIKKHPW 254
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
399-652 1.38e-46

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: 166.36  E-value: 1.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPETSKEVSALECEIQLLKNLQHERIVQ-----YYgclrdraEKTLTIF 473
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVI-----DTKSEEELEDYMVEIDILASCDHPNIVKlldafYY-------ENNLWIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKD-QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS-KRLQTIcms 551
Cdd:cd06643  81 IEFCAGGAVDAvMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSaKNTRTL--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gTGMRSVTGTPYWMSPEVISGEG-----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIA-TQPTNPQLPSHISE 625
Cdd:cd06643 158 -QRRDSFIGTPYWMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAkSEPPTLAQPSRWSP 236
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 626 HGRDFLRRIF---VEARQrpSAEELLTHHF 652
Cdd:cd06643 237 EFKDFLRKCLeknVDARW--TTSQLLQHPF 264
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
399-654 2.86e-46

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: 164.55  E-value: 2.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFD-PDSPETSKEVSAlecEIQLLKNLQHERIVQYYGC-LRdraEKTLTIFMEY 476
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSgKQSTEKWQDIIK---EVKFLRQLRHPNTIEYKGCyLR---EHTAWLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGgSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqTICMSGTgm 555
Cdd:cd06607  83 CLG-SASDIVEVHkKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA----SLVCPAN-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 rSVTGTPYWMSPEVISG--EG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPS-HISEHGRDF- 630
Cdd:cd06607 156 -SFVGTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIA-QNDSPTLSSgEWSDDFRNFv 233
                       250       260
                ....*....|....*....|....*..
gi 42794767 631 ---LRRIfveARQRPSAEELLTHHFAQ 654
Cdd:cd06607 234 dscLQKI---PQDRPSAEDLLKHPFVT 257
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
397-652 3.32e-46

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: 163.94  E-value: 3.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNL----QHERIVQYYGCLRDRAEKTLTI 472
Cdd:cd05118   5 RKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALR------EIKLLKHLndveGHPNIVKLLDVFEHRGGNHLCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMpGGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA-GNVKLGDFGASkrlqtiCM 550
Cdd:cd05118  79 VFELM-GMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLA------RS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYW-MSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLpshisehgR 628
Cdd:cd05118 152 FTSPPYTPYVATRWyRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTPEA--------L 223
                       250       260
                ....*....|....*....|....*
gi 42794767 629 DFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd05118 224 DLLSKMLKyDPAKRITASQALAHPY 248
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
401-652 8.00e-46

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: 163.54  E-value: 8.00e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 401 QGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIqlLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMPGG 480
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNI--LSQAQNPFVVKLYYSFQGK--KNLYLVMEYLPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 481 SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK----RLQTICMSGTGM- 555
Cdd:cd05579  79 DLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvRRQIKLSIQKKSn 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 -------RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMaaIF-KIATQPTN-PQLPShISE 625
Cdd:cd05579 159 gapekedRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFhAETPEE--IFqNILNGKIEwPEDPE-VSD 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 626 HGRDFLRRIF-VEARQRP---SAEELLTHHF 652
Cdd:cd05579 236 EAKDLISKLLtPDPEKRLgakGIEEIKNHPF 266
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
397-650 4.79e-45

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: 161.79  E-value: 4.79e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQ---FDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF 473
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCKKVAIKIINkrkFTIGSRREINKPRNIETEIEILKKLSHPCIIKIEDFFD--AEDDYYIV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKRLQTICM 550
Cdd:cd14084  90 LELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGETSL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 sgtgMRSVTGTPYWMSPEVI---SGEGYGRKADVWSLGCTVVEMLTEKPPWAE-YEAMAAIFKIATQPTN--PQLPSHIS 624
Cdd:cd14084 170 ----MKTLCGTPTYLAPEVLrsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEeYTQMSLKEQILSGKYTfiPKAWKNVS 245
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRR-IFVEARQRPSAEELLTH 650
Cdd:cd14084 246 EEAKDLVKKmLVVDPSRRPSIEEALEH 272
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
399-652 8.38e-45

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: 160.96  E-value: 8.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdspetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 478
Cdd:cd06646  17 VGSGTYGDVYKARNLHTGELAAVKIIKLEP-----GDDFSLIQQEIFMVKECKHCNIVAYFGSYLSR--EKLWICMEYCG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSGTGMRSV 558
Cdd:cd06646  90 GGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAK---ITATIAKRKSF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGE---GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIF---KIATQPTNPQLPSHISEHGRDFLR 632
Cdd:cd06646 167 IGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFlmsKSNFQPPKLKDKTKWSSTFHNFVK 246
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06646 247 ISLTKnPKKRPTAERLLTHLF 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
399-652 1.64e-44

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: 160.34  E-value: 1.64e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSkeVSALEcEIQLLKNLQHERIVQyygcLRD--RAEKTLTIFMEY 476
Cdd:cd07829   7 LGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIP--STALR-EISLLKELKHPNIVK----LLDviHTENKLYLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPggsvKDqLKAY-----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTIcms 551
Cdd:cd07829  80 CD----QD-LKKYldkrpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLA-RAFGI--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gtGMRSVTG---TPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPT--------- 615
Cdd:cd07829 151 --PLRTYTHevvTLWYRAPEILLGSkHYSTAVDIWSVGCIFAELITGKPLFPgdsEIDQLFKIFQILGTPTeeswpgvtk 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794767 616 ----NPQLPSH-----------ISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07829 229 lpdyKPTFPKWpkndlekvlprLDPEGIDLLSKMLQyNPAKRISAKEALKHPY 281
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
399-633 4.03e-44

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: 158.54  E-value: 4.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQ----FDPDSPETSKevsaleCEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFM 474
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKkrhiVQTRQQEHIF------SEKEILEECNSPFIVKLYRTFKDK--KYLYMLM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ------TI 548
Cdd:cd05572  73 EYCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGsgrktwTF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE-----YEAMAAIFKIATQptnPQLPSHI 623
Cdd:cd05572 153 C----------GTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGddedpMKIYNIILKGIDK---IEFPKYI 219
                       250
                ....*....|
gi 42794767 624 SEHGRDFLRR 633
Cdd:cd05572 220 DKNAKNLIKQ 229
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
399-652 6.24e-44

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: 158.68  E-value: 6.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKII----DLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTK--LWIIMEYLG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMRSV 558
Cdd:cd06642  86 GGSALDLLKP-GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD---TQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTNPQlPSHISEHGRDFlrRIFVEA 638
Cdd:cd06642 162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLI---PKNSP-PTLEGQHSKPF--KEFVEA 235
                       250       260
                ....*....|....*....|
gi 42794767 639 ------RQRPSAEELLTHHF 652
Cdd:cd06642 236 clnkdpRFRPTAKELLKHKF 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
396-652 8.75e-44

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: 158.15  E-value: 8.75e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKE--VSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIF 473
Cdd:cd05581   6 GKPLGEGSYSTVVLAKEKETGKEYAIKVL----DKRHIIKEkkVKYVTIEKEVLSRLAHPGIVKLYYTFQDESK--LYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-------- 545
Cdd:cd05581  80 LEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLgpdsspes 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 ------QTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIatqptN 616
Cdd:cd05581 160 tkgdadSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFrgsNEYLTFQKIVKL-----E 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42794767 617 PQLPSHISEHGRDFLRRIFV-EARQRP------SAEELLTHHF 652
Cdd:cd05581 235 YEFPENFPPDAKDLIQKLLVlDPSKRLgvnengGYDELKAHPF 277
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
393-655 9.56e-44

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: 158.73  E-value: 9.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd06654  22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNL---QQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDE--LWV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSG 552
Cdd:cd06654  95 VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ---ITPEQ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDF 630
Cdd:cd06654 171 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSAIFRDF 249
                       250       260
                ....*....|....*....|....*.
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHFAQL 655
Cdd:cd06654 250 LNRCLeMDVEKRGSAKELLQHQFLKI 275
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
393-652 1.01e-43

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: 158.31  E-value: 1.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGC-LRDraeKTLT 471
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKII----DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSyLKD---TKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd06641  79 IIMEYLGGGSALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMrsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTN--PQLPSHISEHGRD 629
Cdd:cd06641 158 RN*F---VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLI---PKNnpPTLEGNYSKPLKE 231
                       250       260
                ....*....|....*....|....
gi 42794767 630 FLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd06641 232 FVEACLnKEPSFRPTAKELLKHKF 255
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
393-655 1.25e-43

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: 158.73  E-value: 1.25e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd06655  21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINL---QKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDE--LFV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSG 552
Cdd:cd06655  94 VMEYLAGGSLTDVVTE-TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ---ITPEQ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDF 630
Cdd:cd06655 170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPEKLSPIFRDF 248
                       250       260
                ....*....|....*....|....*.
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHFAQL 655
Cdd:cd06655 249 LNRCLeMDVEKRGSAKELLQHPFLKL 274
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
392-652 1.86e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 160.68  E-value: 1.86e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVdtgRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHE-RIVQYYGCLRDraEKTL 470
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKVL--AKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQD--EGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-VKLGDFGASKRLQ 546
Cdd:COG0515  74 YLVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TICMSGTG---MRSVTGTPYWMSPEVISG---EGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI---------- 610
Cdd:COG0515 154 DPGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptp 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42794767 611 -ATQPTNPQLPSHISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:COG0515 234 sLASPLSPSNPELISKAASDLLKKLLaKDPKNRLSSSSDLSHDL 277
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
393-655 2.40e-43

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: 157.96  E-value: 2.40e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd06656  21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNL---QQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDE--LWV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSG 552
Cdd:cd06656  94 VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ---ITPEQ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHGRDF 630
Cdd:cd06656 170 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPERLSAVFRDF 248
                       250       260
                ....*....|....*....|....*.
gi 42794767 631 LRRIF-VEARQRPSAEELLTHHFAQL 655
Cdd:cd06656 249 LNRCLeMDVDRRGSAKELLQHPFLKL 274
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
396-636 8.64e-43

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: 155.81  E-value: 8.64e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQvqFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd05580   6 LKTLGTGSFGRVRLVKHKDSGKYYALKI--LKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQD--DRNLYMVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL----QTICms 551
Cdd:cd05580  82 YVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVkdrtYTLC-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHGRDFL 631
Cdd:cd05580 160 --------GTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILE--GKIRFPSFFDPDAKDLI 229

                ....*
gi 42794767 632 RRIFV 636
Cdd:cd05580 230 KRLLV 234
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
399-650 1.13e-42

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: 154.35  E-value: 1.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdsPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 478
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFI------PKRDKKKEAVLREISILNQLQHPRIIQLHEAYESP--TELVLILELCS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS--AGNVKLGDFGASKRLQTICMSGTgmr 556
Cdd:cd14006  73 GGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLNPGEELKE--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 sVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKI---ATQPTNpqlpSHISEHGRDF 630
Cdd:cd14006 150 -IFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLgedDQETLANISACrvdFSEEYF----SSVSQEAKDF 224
                       250       260
                ....*....|....*....|.
gi 42794767 631 LRRIFVEA-RQRPSAEELLTH 650
Cdd:cd14006 225 IRKLLVKEpRKRPTAQEALQH 245
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
399-652 1.58e-42

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: 154.12  E-value: 1.58e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDT--GRELAS-KQV---QFDPDspETskeVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTI 472
Cdd:cd08222   8 LGSGNFGTVYLVSDLKAtaDEELKVlKEIsvgELQPD--ET---VDANR-EAKLLSKLDHPAIVKFHDSFVEK--ESFCI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAY----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAgnVKLGDFGASKRLQT 547
Cdd:cd08222  80 VTEYCEGGDLDDKISEYkksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIfLKNNV--IKVGDFGISRILMG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 ICMSGTgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQLPSHISEHG 627
Cdd:cd08222 158 TSDLAT---TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGET-PSLPDKYSKEL 233
                       250       260
                ....*....|....*....|....*.
gi 42794767 628 RDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd08222 234 NAIYSRMLNkDPALRPSAAEILKIPF 259
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
396-652 1.67e-42

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: 157.06  E-value: 1.67e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPET---SKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:cd05573   6 IKVIGRGAFGEVWLVRDKDTGQVYAMKIL-----RKSDmlkREQIAHVRAERDILADADSPWIVRLHYAFQD--EDHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL------- 545
Cdd:cd05573  79 VMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnksgdre 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 -------QTICMSGTGMR------------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA 606
Cdd:cd05573 159 sylndsvNTLFQDNVLARrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVET 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 607 IFKIATQPTNPQLPSH--ISEHGRDFLRRIFVEARQR-PSAEELLTHHF 652
Cdd:cd05573 239 YSKIMNWKESLVFPDDpdVSPEAIDLIRRLLCDPEDRlGSAEEIKAHPF 287
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
399-652 1.90e-42

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: 154.14  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKMDL---RKQQRREL--LFNEVVIMRDYQHPNIVEMYSSYLVGDE--LWVVMEFLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMRSV 558
Cdd:cd06648  88 GGALTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSK---EVPRRKSL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT-QPTNPQLPSHISEHGRDFLRRIFV- 636
Cdd:cd06648 164 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDnEPPKLKNLHKVSPRLRSFLDRMLVr 243
                       250
                ....*....|....*.
gi 42794767 637 EARQRPSAEELLTHHF 652
Cdd:cd06648 244 DPAQRATAAELLNHPF 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
392-652 2.53e-42

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: 153.56  E-value: 2.53e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKqvqFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLT 471
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALK---FIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFE--TKKEFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqTICMS 551
Cdd:cd14002  77 VVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR---AMSCN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDFL 631
Cdd:cd14002 153 TLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPV--KWPSNMSPEFKSFL 230
                       250       260
                ....*....|....*....|..
gi 42794767 632 RRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14002 231 QGLLNkDPSKRLSWPDLLEHPF 252
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
392-650 3.22e-42

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: 153.19  E-value: 3.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYgclrDRAEKTLT 471
Cdd:cd14079   3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKIL--NRQKIKSLDMEEKIRREIQILKLFRHPHIIRLY----EVIETPTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IF--MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTIC 549
Cdd:cd14079  77 IFmvMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFG----LSNIM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEyEAMAAIF-KIATqpTNPQLPSHISEHG 627
Cdd:cd14079 153 RDGEFLKTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDD-EHIPNLFkKIKS--GIYTIPSHLSPGA 229
                       250       260
                ....*....|....*....|....
gi 42794767 628 RDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14079 230 RDLIKRMLvVDPLKRITIPEIRQH 253
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
399-652 5.38e-42

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: 153.87  E-value: 5.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKE---VSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTL--TIF 473
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKIRM-----ENEKEgfpITAIR-EIKLLQKLDHPNVVRLKEIVTSKGSAKYkgSIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 M--EYMP----GGSVKDQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqt 547
Cdd:cd07840  81 MvfEYMDhdltGLLDNPEVK----FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 iCMSGTGMRSVTG---TPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLP 620
Cdd:cd07840 153 -PYTKENNADYTNrviTLWYRPPELLLGAtRYGPEVDMWSVGCILAELFTGKPIFqgkTELEQLEKIFELCGSPTEENWP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 621 --------------------------SHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07840 232 gvsdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTlDPKKRISADQALQHEY 290
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
399-651 6.31e-42

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: 153.36  E-value: 6.31e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpETSKEVSAlecEIQLLKNLQHERIVQYYG-CLRDraEKTLTIFMEYM 477
Cdd:cd06620  13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKS-SVRKQILR---ELQILHECHSPYIVSFYGaFLNE--NNNIIICMEYM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHS-NMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSgtgm 555
Cdd:cd06620  87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELiNSIADT---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 rsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE-------YEAMAAIFKIATQPTN---PQLPSHI-- 623
Cdd:cd06620 163 --FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGsnddddgYNGPMGILDLLQRIVNeppPRLPKDRif 240
                       250       260
                ....*....|....*....|....*....
gi 42794767 624 SEHGRDFLRRIFVE-ARQRPSAEELLTHH 651
Cdd:cd06620 241 PKDLRDFVDRCLLKdPRERPSPQLLLDHD 269
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
387-652 9.87e-42

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: 152.86  E-value: 9.87e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 387 PSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSpETSKEVsalECEIQLLKNLQ-HERIVQYYGCLRDR 465
Cdd:cd06638  14 PDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKIL--DPIH-DIDEEI---EAEYNILKALSdHPNVVKFYGMYYKK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 AEKT---LTIFMEYMPGGSVKDQLKAY----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGD 538
Cdd:cd06638  88 DVKNgdqLWLVLELCNGGSVTDLVKGFlkrgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 539 FGASKRLqticmSGTGMRSVT--GTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIa 611
Cdd:cd06638 168 FGVSAQL-----TSTRLRRNTsvGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKI- 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 612 tqPTNP----QLPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06638 242 --PRNPpptlHQPELWSNEFNDFIRKCLTkDYEKRPTVSDLLQHVF 285
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
399-652 1.04e-41

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: 153.65  E-value: 1.04e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGC-LRDRaekTLTIFMEYM 477
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYS--GKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCyLKDH---TAWLVMEYC 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGgSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticmsGTGMR 556
Cdd:cd06633 104 LG-SASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASI-------ASPAN 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISG--EG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPSH-ISEHGRDFLR 632
Cdd:cd06633 176 SFVGTPYWMAPEVILAmdEGqYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIA-QNDSPTLQSNeWTDSFRGFVD 254
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIFVEARQ-RPSAEELLTHHF 652
Cdd:cd06633 255 YCLQKIPQeRPSSAELLRHDF 275
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
399-652 1.53e-41

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: 152.13  E-value: 1.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKII----DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTK--LWIIMEYLG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMRSV 558
Cdd:cd06640  86 GGSALDLLRA-GPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD---TQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTNPQlPSHISEHGRDFlrRIFVEA 638
Cdd:cd06640 162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLI---PKNNP-PTLVGDFSKPF--KEFIDA 235
                       250       260
                ....*....|....*....|
gi 42794767 639 ------RQRPSAEELLTHHF 652
Cdd:cd06640 236 clnkdpSFRPTAKELLKHKF 255
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
397-652 1.78e-41

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: 152.08  E-value: 1.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHER-IVQYYGCLRDRA----EKTLT 471
Cdd:cd06636  22 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL------EINMLKKYSHHRnIATYYGAFIKKSppghDDQLW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIc 549
Cdd:cd06636  96 LVMEFCGAGSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 msgTGMR-SVTGTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQLPSH- 622
Cdd:cd06636 175 ---VGRRnTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP-PKLKSKk 250
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 ISEHGRDFLRRIFVEAR-QRPSAEELLTHHF 652
Cdd:cd06636 251 WSKKFIDFIEGCLVKNYlSRPSTEQLLKHPF 281
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
396-648 1.79e-41

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 151.14  E-value: 1.79e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    396 GKLLGQGAFGRVYLCY----DVDTGRELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:smart00219   4 GKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLK----EDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTE--EEPLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    472 IFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticm 550
Cdd:smart00219  78 IVMEYMEGGDLLSYLRKNrPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY---- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    551 SGTGMRSVTGT-PY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIATQPTNPQlPSHISEHG 627
Cdd:smart00219 154 DDDYYRKRGGKlPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPQ-PPNCPPEL 232
                          250       260
                   ....*....|....*....|..
gi 42794767    628 RDFLRRIFVE-ARQRPSAEELL 648
Cdd:smart00219 233 YDLMLQCWAEdPEDRPTFSELV 254
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
399-652 2.22e-41

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: 151.74  E-value: 2.22e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdspetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVIKLEP-----GEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDK--LWICMEFCG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSGTGMRSV 558
Cdd:cd06645  92 GGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQ---ITATIAKRKSF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGE---GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIF---KIATQPtnPQLPSHI--SEHGRDF 630
Cdd:cd06645 169 IGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFlmtKSNFQP--PKLKDKMkwSNSFHHF 246
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06645 247 VKMALTKnPKKRPTAEKLLQHPF 269
PB1_Mekk2_3 cd06405
The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 ...
76-154 2.95e-41

The PB1 domain is present in the two mitogen-activated protein kinase kinases MEKK2 and MEKK3 which are two members of the signaling kinase cascade involved in angiogenesis and early cardiovascular development. The PB1 domain of MEKK2 (and/or MEKK3) interacts with the PB1 domain of another member of the kinase cascade Map2k5. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The MEKK2 and MEKK3 proteins contain a type II PB1 domain.


Pssm-ID: 99726  Cd Length: 79  Bit Score: 144.45  E-value: 2.95e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767  76 VRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQ 154
Cdd:cd06405   1 VRIKFEHNGEKRIIQFPRPVKFKDLQQKVTTAFGQPMDLHYTNNELLIPLKNQEDLDRAIELLDRSPHMKSLRILLSAP 79
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
393-600 3.54e-41

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: 150.56  E-value: 3.54e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAekTLTI 472
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKK---EVCIQKMLSHKNVVRFYGHRREGE--FQYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSG 552
Cdd:cd14069  78 FLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKER 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 553 TGMRSVtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd14069 158 LLNKMC-GTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQ 205
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
397-650 4.26e-41

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: 150.98  E-value: 4.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd14046  12 QVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILR----EVMLLSRLNHQHVVRYYQAWIERAN--LYIQMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTG-M 555
Cdd:cd14046  86 CEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQdI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVT--------------GTPYWMSPEVISGEG--YGRKADVWSLGCTVVEMLteKPPWAEYEAMAAIfkiatqpTNPQL 619
Cdd:cd14046 166 NKSTsaalgssgdltgnvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--YPFSTGMERVQIL-------TALRS 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42794767 620 PSHisEHGRDFLR-RIFVEAR-----------QRPSAEELLTH 650
Cdd:cd14046 237 VSI--EFPPDFDDnKHSKQAKlirwllnhdpaKRPSAQELLKS 277
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
399-654 1.29e-40

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: 150.97  E-value: 1.29e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGC-LRdraEKTLTIFMEYM 477
Cdd:cd06635  33 IGHGSFGAVYFARDVRTSEVVAIKKMSYS--GKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCyLR---EHTAWLVMEYC 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGgSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqticmSGTGMR 556
Cdd:cd06635 108 LG-SASDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS-------IASPAN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISG--EG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPS-HISEHGRDFLR 632
Cdd:cd06635 180 SFVGTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIA-QNESPTLQSnEWSDYFRNFVD 258
                       250       260
                ....*....|....*....|...
gi 42794767 633 RIFVEARQ-RPSAEELLTHHFAQ 654
Cdd:cd06635 259 SCLQKIPQdRPTSEELLKHMFVL 281
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
399-654 1.47e-40

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: 150.56  E-value: 1.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGC-LRdraEKTLTIFMEYM 477
Cdd:cd06634  23 IGHGSFGAVYFARDVRNNEVVAIKKMSYS--GKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCyLR---EHTAWLVMEYC 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGgSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmsgtgMR 556
Cdd:cd06634  98 LG-SASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP-------AN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISG--EG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAtQPTNPQLPS-HISEHGRDFLR 632
Cdd:cd06634 170 SFVGTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIA-QNESPALQSgHWSEYFRNFVD 248
                       250       260
                ....*....|....*....|...
gi 42794767 633 RIFVEARQ-RPSAEELLTHHFAQ 654
Cdd:cd06634 249 SCLQKIPQdRPTSDVLLKHRFLL 271
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
397-650 1.66e-40

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: 148.69  E-value: 1.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd08530   6 KKLGKGSYGSVYKVKRLSDNQVYALKEVNL---GSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLD--GNRLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGA----LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmsg 552
Cdd:cd08530  81 APFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGM-RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKIATQPTNPQLPSHISEHGRDFL 631
Cdd:cd08530 155 KNLaKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRYKVCRGKFPPIPPVYSQDLQQII 233
                       250       260
                ....*....|....*....|
gi 42794767 632 RRIF-VEARQRPSAEELLTH 650
Cdd:cd08530 234 RSLLqVNPKKRPSCDKLLQS 253
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
394-609 1.90e-40

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 148.41  E-value: 1.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   394 RRGKLLGQGAFGRVYLCY----DVDTGRELASKQVqfDPDSpeTSKEVSALECEIQLLKNLQHERIVQYYG-CLRDraeK 468
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL--KEGA--DEEEREDFLEEASIMKKLDHPNIVKLLGvCTQG---E 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   469 TLTIFMEYMPGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 547
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767   548 icMSGTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAE---YEAMAAIFK 609
Cdd:pfam07714 155 --DDYYRKRGGGKLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLgEQPYPGmsnEEVLEYLED 219
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
396-648 3.88e-40

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: 147.70  E-value: 3.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    396 GKLLGQGAFGRVYLCY----DVDTGRELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:smart00221   4 GKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLK----EDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTE--EEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    472 IFMEYMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQtic 549
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRpkELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY--- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    550 mSGTGMRSVTGT-PY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIATQPTNPQlPSHISEH 626
Cdd:smart00221 155 -DDDYYKVKGGKlPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPK-PPNCPPE 232
                          250       260
                   ....*....|....*....|...
gi 42794767    627 GRDFLRRIFVE-ARQRPSAEELL 648
Cdd:smart00221 233 LYKLMLQCWAEdPEDRPTFSELV 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
392-648 7.14e-40

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: 147.03  E-value: 7.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSALEC--EIQLLKNLQHERIVQYYGCLRDRAEkt 469
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIF----EMMDAKARQDClkEIDLLQQLNHPNIIKYLASFIENNE-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGA----LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG----- 540
Cdd:cd08224  75 LNIVLELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGlgrff 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLQTicmsgtgmRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP-WAEYEAMAAIFKIATQPTNPQL 619
Cdd:cd08224 155 SSKTTAA--------HSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPfYGEKMNLYSLCKKIEKCEYPPL 226
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 620 PS-HISEHGRDFLRR-IFVEARQRPSAEELL 648
Cdd:cd08224 227 PAdLYSQELRDLVAAcIQPDPEKRPDISYVL 257
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
395-652 7.97e-40

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: 146.70  E-value: 7.97e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFM 474
Cdd:cd14188   5 RGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQRE--KIDKEIELHRILHHKHVVQFYHYFEDK--ENIYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcmsGTG 554
Cdd:cd14188  81 EYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPL---EHR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKiATQPTNPQLPSHISEHGRDFLRRI 634
Cdd:cd14188 158 RRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPF-ETTNLKETYR-CIREARYSLPSSLLAPAKHLIASM 235
                       250
                ....*....|....*....
gi 42794767 635 FVEARQ-RPSAEELLTHHF 652
Cdd:cd14188 236 LSKNPEdRPSLDEIIRHDF 254
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
392-650 1.37e-39

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: 146.03  E-value: 1.37e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQI---PVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLE--DKALM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-VKLGDFGASKRLQTI 548
Cdd:cd08220  76 IVMEYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPqlpshISEHGR 628
Cdd:cd08220 156 SKAYT----VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAP-----ISDRYS 226
                       250       260
                ....*....|....*....|....*..
gi 42794767 629 DFLRRIF-----VEARQRPSAEELLTH 650
Cdd:cd08220 227 EELRHLIlsmlhLDPNKRPTLSEIMAQ 253
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
397-648 1.70e-39

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: 145.76  E-value: 1.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCY---DVDTGRELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIF 473
Cdd:cd00192   1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLK----EDASESERKDFLKEARVMKKLGHPNVVRLLGVCTE--EEPLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTR---------KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd00192  75 MEYMEGGDLLDFLRKSRPVFPSPEPstlslkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 L---QTICMSGTGMRSVtgtpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEY---EAMAAIfkiaTQPTNP 617
Cdd:cd00192 155 IyddDYYRKKTGGKLPI----RWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLgATPYPGLsneEVLEYL----RKGYRL 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 618 QLPSHISEHGRDFLRRIFV-EARQRPSAEELL 648
Cdd:cd00192 227 PKPENCPDELYELMLSCWQlDPEDRPTFSELV 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
399-648 6.86e-39

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: 144.37  E-value: 6.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGREL--ASKQVQFDPDSpETSKEVSA-LECEIQLLKNLQHERIVQYYGCLRDRAEKTlTIFME 475
Cdd:cd13994   1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRRRDDE-SKRKDYVKrLTSEYIISSKLHHPNIVKVLDLCQDLHGKW-CLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-----QTICM 550
Cdd:cd13994  79 YCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgmpaeKESPM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGtGMRsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPW----------AEYEAMAAIFKIATQPTNPQL 619
Cdd:cd13994 159 SA-GLC---GSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsakksdsayKAYEKSGDFTNGPYEPIENLL 234
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 620 PSHIsehgRDFLRRIF-VEARQRPSAEELL 648
Cdd:cd13994 235 PSEC----RRLIYRMLhPDPEKRITIDEAL 260
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
397-649 8.01e-39

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: 143.72  E-value: 8.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevSALEcEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd08221   6 RVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERR--DALN-EIDILSLLNHDNIITYYNHFLD--GESLFIEMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTG 554
Cdd:cd08221  81 CNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDS---ESSM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT---QPTNPQLPSHISEHGRDFL 631
Cdd:cd08221 158 AESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQgeyEDIDEQYSEEIIQLVHDCL 237
                       250
                ....*....|....*...
gi 42794767 632 RRifvEARQRPSAEELLT 649
Cdd:cd08221 238 HQ---DPEDRPTAEELLE 252
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
390-652 9.34e-39

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: 144.95  E-value: 9.34e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPdspetskEVSALECEIqlLKNLQHERIVQYYGCLRDRAEKT 469
Cdd:cd14137   3 EISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDK-------RYKNRELQI--MRRLKHPNIVKLKYFFYSSGEKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 ----LTIFMEYMPGgSV----KDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFG 540
Cdd:cd14137  74 devyLNLVMEYMPE-TLyrviRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLQT-------ICmsgtgmrsvtgTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFK 609
Cdd:cd14137 153 SAKRLVPgepnvsyIC-----------SRYYRAPELIFGaTDYTTAIDIWSAGCVLAELLLGQPLFPgesSVDQLVEIIK 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 610 IATQPT-------NPQ-----------------LPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14137 222 VLGTPTreqikamNPNytefkfpqikphpwekvFPKRTPPDAIDLLSKILVyNPSKRLTALEALAHPF 289
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
397-649 2.12e-38

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: 143.20  E-value: 2.12e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd13996  12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLR----EVKALAKLNHPNIVRYYTAWVE--EPPLYIQMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK---AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAGNVKLGDFGASKR-------- 544
Cdd:cd13996  86 CEGGTLRDWIDrrnSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIfLDNDDLQVKIGDFGLATSignqkrel 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 --LQTICMSGTGMRSV-TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTekPPWAEYEAmaaiFKIATQPTNPQLP- 620
Cdd:cd13996 166 nnLNNNNNGNTSNNSVgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH--PFKTAMER----STILTDLRNGILPe 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 621 ----SHISEHgrDFLRR-IFVEARQRPSAEELLT 649
Cdd:cd13996 240 sfkaKHPKEA--DLIQSlLSKNPEERPSAEQLLR 271
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
396-650 2.21e-38

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: 142.71  E-value: 2.21e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCY--DVDTGRELASKQVqfdpDSPETSKE--VSALECEIQLLKNLQHERIVQYYGCLrDRAEKtLT 471
Cdd:cd14080   5 GKTIGEGSYSKVKLAEytKSGLKEKVACKII----DKKKAPKDflEKFLPRELEILRKLRHPNIIQVYSIF-ERGSK-VF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtiCMS 551
Cdd:cd14080  79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARL----CPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMR-SVT--GTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEaMAAIFKIATQP--TNPQLPSHISE 625
Cdd:cd14080 155 DDGDVlSKTfcGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSN-IKKMLKDQQNRkvRFPSSVKKLSP 233
                       250       260
                ....*....|....*....|....*.
gi 42794767 626 HGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14080 234 ECKDLIDQLLePDPTKRATIEEILNH 259
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
397-652 3.80e-38

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: 143.32  E-value: 3.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHER-IVQYYGCLRDR----AEKTLT 471
Cdd:cd06637  12 ELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQ------EINMLKKYSHHRnIATYYGAFIKKnppgMDDQLW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIc 549
Cdd:cd06637  86 LVMEFCGAGSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 msgTGMRSV-TGTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQLPS-H 622
Cdd:cd06637 165 ---VGRRNTfIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPA-PRLKSkK 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 ISEHGRDFLRRIFVEAR-QRPSAEELLTHHF 652
Cdd:cd06637 241 WSKKFQSFIESCLVKNHsQRPSTEQLMKHPF 271
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
396-650 5.16e-38

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: 141.77  E-value: 5.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQyygcLRDRAEKTLTIF-- 473
Cdd:cd14663   5 GRTLGEGTFAKVKFARNTKTGESVAIKII--DKEQVAREGMVEQIKREIAIMKLLRHPNIVE----LHEVMATKTKIFfv 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcMSGT 553
Cdd:cd14663  79 MELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQF-RQDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHGRDFLR 632
Cdd:cd14663 158 LLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMK--GEFEYPRWFSPGAKSLIK 235
                       250
                ....*....|....*....
gi 42794767 633 RIFV-EARQRPSAEELLTH 650
Cdd:cd14663 236 RILDpNPSTRITVEQIMAS 254
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
435-652 8.54e-38

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: 140.96  E-value: 8.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 435 KEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKT----LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSY 510
Cdd:cd14012  40 KQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEY 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 511 LHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQTICMSG--TGMRSvtgtPYWMSPEVI-SGEGYGRKADVWSL 584
Cdd:cd14012 120 LHRNGVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLDMCSRGslDEFKQ----TYWLPPELAqGSKSPTRKTDVWDL 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 585 GCTVVEMLTEKPPWAEYEAMAAIfkiatqPTNPQLPshisEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14012 196 GLLFLQMLFGLDVLEKYTSPNPV------LVSLDLS----ASLQDFLSKCLsLDPKKRPTALELLPHEF 254
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
395-652 1.62e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; 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. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 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: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 140.06  E-value: 1.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 474
Cdd:cd14189   5 KGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQRE--KIVNEIELHRDLHHKHVVKFSHHFED--AENIYIFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTG 554
Cdd:cd14189  81 ELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEP---PEQR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKIATQpTNPQLPSHISEHGRDFLRRI 634
Cdd:cd14189 158 KKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPF-ETLDLKETYRCIKQ-VKYTLPASLSLPARHLLAGI 235
                       250
                ....*....|....*....
gi 42794767 635 FVEA-RQRPSAEELLTHHF 652
Cdd:cd14189 236 LKRNpGDRLTLDQILEHEF 254
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
399-652 1.65e-37

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: 141.66  E-value: 1.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMDL---RKQQRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEE--LWVLMEYLQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSGTGMRSV 558
Cdd:cd06659 102 GGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQ---ISKDVPKRKSL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH-ISEHGRDFLRRIFV- 636
Cdd:cd06659 178 VGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHkASPVLRDFLERMLVr 257
                       250
                ....*....|....*.
gi 42794767 637 EARQRPSAEELLTHHF 652
Cdd:cd06659 258 DPQERATAQELLDHPF 273
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
399-650 2.74e-37

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: 139.28  E-value: 2.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKC-----RKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPRE--MVLVMEYVA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGS-----VKDQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN-VKLGDFGASKRLQTicms 551
Cdd:cd14103  74 GGElfervVDDDFE----LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDP---- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLG--CTVveMLTEKPPW---AEYEAMAAIFKIATQPTNPQLpSHISEH 626
Cdd:cd14103 146 DKKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGviCYV--LLSGLSPFmgdNDAETLANVTRAKWDFDDEAF-DDISDE 222
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14103 223 AKDFISKLLVkDPRKRMSAAQCLQH 247
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
398-652 3.07e-37

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: 140.53  E-value: 3.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevSALEcEIQLLKNLQHERIVQyygcLRD--RAEKTLTIFME 475
Cdd:cd07833   8 VVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKK--TALR-EVKVLRQLRHENIVN----LKEafRRKGRLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGgSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQtiCMSGTG 554
Cdd:cd07833  81 YVER-TLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALT--ARPASP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI------------ATQPTNPQL-- 619
Cdd:cd07833 158 LTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIqkclgplppshqELFSSNPRFag 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 620 -----PSHI-----------SEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd07833 238 vafpePSQPeslerrypgkvSSPALDFLKACLrMDPKERLTCDELLQHPY 287
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
397-652 4.76e-37

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: 138.94  E-value: 4.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPdSPETSKEVSalECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTK-MPVKEKEAS--KKEVILLAKMKHPNIVTFFASFQE--NGRLFIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQL-KAYGAL-TESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV-KLGDFGASKRLQTicmSGT 553
Cdd:cd08225  81 CDGGDLMKRInRQRGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLND---SME 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPsHISEHGRDFLRR 633
Cdd:cd08225 158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISP-NFSRDLRSLISQ 236
                       250       260
                ....*....|....*....|
gi 42794767 634 IF-VEARQRPSAEELLTHHF 652
Cdd:cd08225 237 LFkVSPRDRPSITSILKRPF 256
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
392-652 5.22e-37

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: 139.12  E-value: 5.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQ----------LLKNLQHERIVQYYGC 461
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISrdirtireaaLSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 462 LRDRAEkTLTIFmEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd14077  82 LRTPNH-YYMLF-EYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 S------KRLQTICmsgtgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQP 614
Cdd:cd14077 160 SnlydprRLLRTFC----------GSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKI--KK 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 615 TNPQLPSHISEHGRDFLRR-IFVEARQRPSAEELLTHHF 652
Cdd:cd14077 228 GKVEYPSYLSSECKSLISRmLVVDPKKRATLEQVLNHPW 266
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
397-647 8.87e-37

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: 139.05  E-value: 8.87e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLC-YDV---DTGRELASKQVQfdPDSPETSKevSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTI 472
Cdd:cd05038  10 KQLGEGHFGSVELCrYDPlgdNTGEQVAVKSLQ--PSGEEQHM--SDFKREIEILRTLDHEYIVKYKGVCESPGRRSLRL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd05038  86 IMEYLPSGSLRDYLQRHRDQIDLKRLlLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGmRSVTGTP-YWMSPEVISGEGYGRKADVWSLGCTVVEMLT----EKPPWAEYeaMAAIFKIATQPTNPQLPSHISEH 626
Cdd:cd05038 166 YYV-KEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYELFTygdpSQSPPALF--LRMIGIAQGQMIVTRLLELLKSG 242
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 627 GR------------DFLRRIF-VEARQRPSAEEL 647
Cdd:cd05038 243 ERlprppscpdevyDLMKECWeYEPQDRPSFSDL 276
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
397-649 1.08e-36

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: 137.80  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdsPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEY 476
Cdd:cd08219   6 RVVGEGSFGRALLVQHVNSDQKYAMKEIRL----PKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFE--ADGHLYIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK-AYGAL-TESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTG 554
Cdd:cd08219  80 CDGGDLMQKIKlQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTS---PGAY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPqLPSHISEHGRDFLRRI 634
Cdd:cd08219 157 ACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKP-LPSHYSYELRSLIKQM 235
                       250
                ....*....|....*.
gi 42794767 635 FVE-ARQRPSAEELLT 649
Cdd:cd08219 236 FKRnPRSRPSATTILS 251
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
392-652 1.10e-36

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: 138.97  E-value: 1.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSpETSKEVsalECEIQLLKNL-QHERIVQYYGCLRdRAEK-- 468
Cdd:cd06639  23 TWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL--DPIS-DVDEEI---EAEYNILRSLpNHPNVVKFYGMFY-KADQyv 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 --TLTIFMEYMPGGSVKDQLKAY----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 542
Cdd:cd06639  96 ggQLWLVLELCNGGSVTELVKGLlkcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 KRLqticmSGTGMRSVT--GTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPT 615
Cdd:cd06639 176 AQL-----TSARLRRNTsvGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPP 250
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42794767 616 nPQL--PSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06639 251 -PTLlnPEKWCRGFSHFISQCLIkDFEKRPSVTHLLEHPF 289
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
398-652 1.12e-36

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: 138.26  E-value: 1.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASK--QVQFDPDSPETSKEV-SALECEIQLLKNLQ-HERIVQyygcLRDRAEKTLTIF 473
Cdd:cd14093  10 ILGRGVSSTVRRCIEKETGQEFAVKiiDITGEKSSENEAEELrEATRREIEILRQVSgHPNIIE----LHDVFESPTFIF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 M--EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmS 551
Cdd:cd14093  86 LvfELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLD----E 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVI------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT---QPTNPQLpSH 622
Cdd:cd14093 162 GEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEgkyEFGSPEW-DD 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 ISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14093 241 ISDTAKDLISKLLvVDPKKRLTAEEALEHPF 271
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
397-652 1.55e-36

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: 137.73  E-value: 1.55e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDtGRELASKQVQFDPDSPETskeVSALECEIQLLKNLQHE-RIVQYYGCLRDRAEKTLTIFME 475
Cdd:cd14131   7 KQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGADEQT---LQSYKNEIELLKKLKGSdRIIQLYDYEVTDEDDYLYMVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YmpgGSVkD-----QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGASKRLQT--- 547
Cdd:cd14131  83 C---GEI-DlatilKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQNdtt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 -IcmsgtgMRSVT-GTPYWMSPEVI-----SGEGY-----GRKADVWSLGCTVVEMLTEKPPWAEY-EAMAAIFKIATQP 614
Cdd:cd14131 158 sI------VRDSQvGTLNYMSPEAIkdtsaSGEGKpkskiGRPSDVWSLGCILYQMVYGKTPFQHItNPIAKLQAIIDPN 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 615 TNPQLPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14131 232 HEIEFPDIPNPDLIDVMKRCLQrDPKKRPSIPELLNHPF 270
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
401-650 1.61e-36

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: 137.45  E-value: 1.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 401 QGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskevsalECEIQllKNLQHERIVQYYGCLRdrAEKTLTIFMEYMPGG 480
Cdd:cd13995  14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS--------DVEIQ--ACFRHENIAELYGALL--WEETVHLFMEAGEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 481 SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVkLGDFGASKRLQTICMSGTGMRsvtG 560
Cdd:cd13995  82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLR---G 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 561 TPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA----IFKIATQ-PTNPQLPSHISEHGRDFLRRIF 635
Cdd:cd13995 158 TEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQaPPLEDIAQDCSPAMRELLEAAL 237
                       250
                ....*....|....*.
gi 42794767 636 VE-ARQRPSAEELLTH 650
Cdd:cd13995 238 ERnPNHRSSAAELLKH 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
399-650 1.76e-36

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: 136.86  E-value: 1.76e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL-CYdvdTGRELASKQVQfdpDSPETskevsalecEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFMEY 476
Cdd:cd14059   1 LGSGAQGAVFLgKF---RGEEVAVKKVR---DEKET---------DIKHLRKLNHPNIIKFKGvCTQ---APCYCILMEY 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcmsGTGMr 556
Cdd:cd14059  63 CPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEK---STKM- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIF- 635
Cdd:cd14059 139 SFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVPSTCPDGFKLLMKQCWn 218
                       250
                ....*....|....*
gi 42794767 636 VEARQRPSAEELLTH 650
Cdd:cd14059 219 SKPRNRPSFRQILMH 233
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
392-652 2.22e-36

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: 138.47  E-value: 2.22e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKE---VSALEcEIQLLKNLQHERIVQyygcLRD--RA 466
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIK--LGERKEAKDginFTALR-EIKLLQELKHPNIIG----LLDvfGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKTLTIFMEYMPG---GSVKDQLKAygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd07841  74 KSNINLVFEFMETdleKVIKDKSIV---LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RLqticmsGTGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTN 616
Cdd:cd07841 151 SF------GSPNRKMTHqvvTRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPgdsDIDQLGKIFEALGTPTE 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 617 PQLP-----------------------SHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07841 225 ENWPgvtslpdyvefkpfpptplkqifPAASDDALDLLQRLLTlNPNKRITARQALEHPY 284
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
392-641 3.45e-36

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: 137.57  E-value: 3.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdsPETS--KEVSALECEIQLLKNLQHERIVQYYGCLRDraEKT 469
Cdd:cd05612   2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAI----PEVIrlKQEQHVHNEKRVLKEVSHPFIIRLFWTEHD--QRF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ--- 546
Cdd:cd05612  76 LYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRdrt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 -TICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAiFKIatqptnpQL 619
Cdd:cd05612 156 wTLC----------GTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDdnpfgiYEKILA-GKL-------EF 217
                       250       260
                ....*....|....*....|..
gi 42794767 620 PSHISEHGRDFLRRIFVEARQR 641
Cdd:cd05612 218 PRHLDLYAKDLIKKLLVVDRTR 239
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
396-650 3.46e-36

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: 136.66  E-value: 3.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEV--SALECEIQLLKNLQHERIVQYYGCLrdraEKTLTIF 473
Cdd:cd14162   5 GKTLGHGSYAVVKKAYSTKHKCKVAIKIV----SKKKAPEDYlqKFLPREIEVIKGLKHPNLICFYEAI----ETTSRVY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 --MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtiCMS 551
Cdd:cd14162  77 iiMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARG----VMK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPY-----WMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPsHISE 625
Cdd:cd14162 153 TKDGKPKLSETYcgsyaYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNP-TVSE 231
                       250       260
                ....*....|....*....|....*
gi 42794767 626 HGRDFLRRIFVEARQRPSAEELLTH 650
Cdd:cd14162 232 ECKDLILRMLSPVKKRITIEEIKRD 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
397-648 4.04e-36

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: 136.70  E-value: 4.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASK-QVQFDPDSPETSKEvsalecEIQLLKNL-QHERIVQYYGC--LRDRAEKTLTI 472
Cdd:cd13985   6 KQLGEGGFSYVYLAHDVNTGRRYALKrMYFNDEEQLRVAIK------EIEIMKRLcGHPNIVQYYDSaiLSSEGRKEVLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGgSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd13985  80 LMEYCPG-SLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTG-------MRSVTgTPYWMSPEVI---SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQ 618
Cdd:cd13985 159 LERAEEvniieeeIQKNT-TPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPEQPR 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 619 LPSHIsehgRDFLRRIF-VEARQRPSAEELL 648
Cdd:cd13985 238 YSPEL----HDLIRHMLtPDPAERPDIFQVI 264
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
397-585 7.35e-36

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: 135.59  E-value: 7.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaEKtLTIFMEY 476
Cdd:cd14073   7 ETLGKGTYGKVKLAIERATGREVAIKSIK--KDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENK-DK-IVIVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS------KRLQTICm 550
Cdd:cd14073  83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSnlyskdKLLQTFC- 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42794767 551 sgtgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLG 585
Cdd:cd14073 162 ---------GSPLYASPEIVNGTPYqGPEVDCWSLG 188
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
394-619 8.03e-36

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: 136.21  E-value: 8.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLC-YDVD---TGRELASKQVQfdpdsPETSKEVSA-LECEIQLLKNLQHERIVQYYGCLRDRAEK 468
Cdd:cd05079   7 KRIRDLGEGHFGKVELCrYDPEgdnTGEQVAVKSLK-----PESGGNHIAdLKKEIEILRNLYHENIVKYKGICTEDGGN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 547
Cdd:cd05079  82 GIKLIMEFLPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794767 548 ICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPpwAEYEAMAAIFKIaTQPTNPQL 619
Cdd:cd05079 162 DKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCD--SESSPMTLFLKM-IGPTHGQM 230
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
399-652 1.14e-35

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: 135.19  E-value: 1.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYlcydvdTGR-------ELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGClrdrAEKTLT 471
Cdd:cd14120   1 IGHGAFAVVF------KGRhrkkpdlPVAIKCIT----KKNLSKSQNLLGKEIKILKELSHENVVALLDC----QETSSS 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IF--MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL------RDSAGN---VKLGDFG 540
Cdd:cd14120  67 VYlvMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILlshnsgRKPSPNdirLKIADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLQTICMSGTgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---------AEYEAMAAIFkia 611
Cdd:cd14120 147 FARFLQDGMMAAT----LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFqaqtpqelkAFYEKNANLR--- 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42794767 612 tqptnPQLPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14120 220 -----PNIPSGTSPALKDLLLGLLKrNPKDRIDFEDFFSHPF 256
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
393-652 2.17e-35

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: 134.17  E-value: 2.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRaeKTLTI 472
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRK---EVAVLSKMKHPNIVQYQESFEEN--GNLYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGAL--TESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicm 550
Cdd:cd08218  77 VMDYCDGGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNS--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIaTQPTNPQLPSHISEHGRDF 630
Cdd:cd08218 154 TVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKI-IRGSYPPVPSRYSYDLRSL 232
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFVEA-RQRPSAEELLTHHF 652
Cdd:cd08218 233 VSQLFKRNpRDRPSINSILEKPF 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
399-652 2.56e-35

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: 133.95  E-value: 2.56e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRE-LASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQyygcLRDRA--EKTLTIFME 475
Cdd:cd14121   3 LGSGTYATVYKAYRKSGAREvVAVKCVS---KSSLNKASTENLLTEIELLKKLKHPHIVE----LKDFQwdEEHIYLIME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV--KLGDFGASKRLqticMSGT 553
Cdd:cd14121  76 YCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHL----KPND 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE--YEAMAAifKIATQ-----PTNPqlpsHISEH 626
Cdd:cd14121 152 EAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASrsFEELEE--KIRSSkpieiPTRP----ELSAD 225
                       250       260
                ....*....|....*....|....*..
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14121 226 CRDLLLRLLQrDPDRRISFEEFFAHPF 252
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
392-585 3.92e-35

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: 133.41  E-value: 3.92e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASK---QVQFDPDSpetskeVSALECEIQLLKNLQHERIVQYYGCLRdrAEK 468
Cdd:cd14072   1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKiidKTQLNPSS------LQKLFREVRIMKILNHPNIVKLFEVIE--TEK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQti 548
Cdd:cd14072  73 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFT-- 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42794767 549 cmSGTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLG 585
Cdd:cd14072 151 --PGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLG 186
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
397-650 6.35e-35

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: 133.96  E-value: 6.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSkevsaLECEIQLLKNLQHERIVQyygcLRDRAEKTLTIF--M 474
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSS-----LENEIAVLKRIKHENIVT----LEDIYESTTHYYlvM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR---DSAGNVKLGDFGASKrlqticMS 551
Cdd:cd14166  80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK------ME 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTG-MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEyEAMAAIF-KIATQPTNPQLP--SHISEHG 627
Cdd:cd14166 154 QNGiMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYE-ETESRLFeKIKEGYYEFESPfwDDISESA 232
                       250       260
                ....*....|....*....|....
gi 42794767 628 RDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14166 233 KDFIRHLLeKNPSKRYTCEKALSH 256
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
443-652 7.88e-35

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: 133.19  E-value: 7.88e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 443 EIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIK 522
Cdd:cd14010  44 EVRLTHELKHPNVLKFYEWYETSNH--LWLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLK 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 523 GANILRDSAGNVKLGDFGASKRLQTI-------------CMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVV 589
Cdd:cd14010 122 PSNILLDGNGTLKLSDFGLARREGEIlkelfgqfsdegnVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLY 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 590 EMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFV----EARQRPSAEELLTHHF 652
Cdd:cd14010 202 EMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSSKPSPDFKSLLKGllekDPAKRLSWDELVKHPF 268
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
387-652 8.22e-35

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: 132.75  E-value: 8.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 387 PSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDS----PETSKEVSAlecEIQLLKNLQHERIVQYYGCL 462
Cdd:cd14187   3 PRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIV---PKSlllkPHQKEKMSM---EIAIHRSLAHQHVVGFHGFF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 463 RDraEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 542
Cdd:cd14187  77 ED--NDFVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 KRLQticMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFkIATQPTNPQLPSH 622
Cdd:cd14187 155 TKVE---YDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPF-ETSCLKETY-LRIKKNEYSIPKH 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 ISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14187 230 INPVAASLIQKMLqTDPTARPTINELLNDEF 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
395-652 9.03e-35

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: 132.83  E-value: 9.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYlcydvdTGR-------ELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYgclrDRAE 467
Cdd:cd14202   6 RKDLIGHGAFAVVF------KGRhkekhdlEVAVKCI----NKKNLAKSQTLLGKEIKILKELKHENIVALY----DFQE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIF--MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL------RDSAGN---VKL 536
Cdd:cd14202  72 IANSVYlvMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILlsysggRKSNPNnirIKI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 537 GDFGASKRLQTICMSGTgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMAAIFKIATQPT 615
Cdd:cd14202 152 ADFGFARYLQNNMMAAT----LCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFqASSPQDLRLFYEKNKSL 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42794767 616 NPQLPSHISEHGRDFLRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd14202 228 SPNIPRETSSHLRQLLLGLLQRnQKDRMDFDEFFHHPF 265
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
398-652 1.33e-34

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: 132.79  E-value: 1.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPD--SPETSKEV-SALECEIQLLKNLQ-HERIVQyygcLRDRAEKTLTIF 473
Cdd:cd14181  17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAErlSPEQLEEVrSSTLKEIHILRQVSgHPSIIT----LIDSYESSTFIF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEY--MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmS 551
Cdd:cd14181  93 LVFdlMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLE----P 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVI------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT---QPTNPQLPSH 622
Cdd:cd14181 169 GEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEgryQFSSPEWDDR 248
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 iSEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14181 249 -SSTVKDLISRLLvVDPEIRLTAEQALQHPF 278
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
393-652 1.54e-34

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: 132.44  E-value: 1.54e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLC-YDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYgclrDRAEKTLT 471
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGrHRKKTDWEVAIKSI----NKKNLSKSQILLGKEIKILKELQHENIVALY----DVQEMPNS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IF--MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG---------NVKLGDFG 540
Cdd:cd14201  80 VFlvMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLQTICMSGTgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMAAIFKIATQPTNPQL 619
Cdd:cd14201 160 FARYLQSNMMAAT----LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFqANSPQDLRMFYEKNKNLQPSI 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 620 PSHISEHGRDFLRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd14201 236 PRETSPYLADLLLGLLQRnQKDRMDFEAFFSHPF 269
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
392-650 1.90e-34

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: 131.62  E-value: 1.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKqVQFDPDSPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRAEktLT 471
Cdd:cd14116   6 DFEIGRPLGKGKFGNVYLAREKQSKFILALK-VLFKAQLEKAGVE-HQLRREVEIQSHLRHPNILRLYGYFHDATR--VY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-----ASKRLQ 546
Cdd:cd14116  82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGwsvhaPSSRRT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATqptnpQLPSHI 623
Cdd:cd14116 162 TLC----------GTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFeanTYQETYKRISRVEF-----TFPDFV 226
                       250       260
                ....*....|....*....|....*...
gi 42794767 624 SEHGRDFLRRIFVE-ARQRPSAEELLTH 650
Cdd:cd14116 227 TEGARDLISRLLKHnPSQRPMLREVLEH 254
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
398-652 2.11e-34

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: 132.40  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDspETSKEVSALEcEIQLLKNLQ---HERIVQYY----GCLRDRaEKTL 470
Cdd:cd07838   6 EIGEGAYGTVYKARDLQDGRFVALKKVRVPLS--EEGIPLSTIR-EIALLKQLEsfeHPNVVRLLdvchGPRTDR-ELKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMpggsvkDQ-LKAY------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASk 543
Cdd:cd07838  82 TLVFEHV------DQdLATYldkcpkPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLA- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RLQTICMSGTgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLP 620
Cdd:cd07838 155 RIYSFEMALT---SVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFrgsSEADQLGKIFDVIGLPSEEEWP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 621 ----------------------SHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07838 232 rnsalprssfpsytprpfksfvPEIDEEGLDLLKKMLTfNPHKRISAFEALQHPY 286
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
399-650 2.73e-34

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: 131.23  E-value: 2.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFD-----PDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDRAEKTLTIF 473
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRklrriPNGEANVKR------EIQILRRLNHRNVIKLVDVLYNEEKQKLYMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMpGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd14119  75 MEYC-VGGLQEMLDSAPDkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVtGTPYWMSPEVISGEGY--GRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIF-KIATQPTnpQLPSHISEHGR 628
Cdd:cd14119 154 DTCTTSQ-GSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPF-EGDNIYKLFeNIGKGEY--TIPDDVDPDLQ 229
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14119 230 DLLRGMLeKDPEKRFTIEQIRQH 252
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
399-647 7.00e-34

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: 130.32  E-value: 7.00e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspetskEVSALEcEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMP 478
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVRL---------EVFRAE-ELMACAGLTSPRVVPLYGAVREGP--WVNIFMDLKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG-NVKLGDFGASKRLQTicmSGTGMRS 557
Cdd:cd13991  82 GGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDP---DGLGKSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 558 VT-----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnP--QLPSHIS----EH 626
Cdd:cd13991 159 FTgdyipGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPP-PlrEIPPSCApltaQA 237
                       250       260
                ....*....|....*....|.
gi 42794767 627 GRDFLRRifvEARQRPSAEEL 647
Cdd:cd13991 238 IQAGLRK---EPVHRASAAEL 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
396-652 9.70e-34

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: 129.48  E-value: 9.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaEKTLTIFME 475
Cdd:cd08223   5 LRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNAS---KRERKAAEQEAKLLSKLKHPNIVSYKESFEGE-DGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC-MSG 552
Cdd:cd08223  81 FCEGGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSdMAT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQLPSHISEHGRDFLR 632
Cdd:cd08223 161 T----LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKL-PPMPKQYSPELGELIK 235
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIF-VEARQRPSAEELLTHHF 652
Cdd:cd08223 236 AMLhQDPEKRPSVKRILRQPY 256
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
399-652 1.26e-33

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: 130.14  E-value: 1.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQV----QFDPDSPETSKEVSAL-ECEiqllknlQHERIVQyygcLRD--RAEKTLT 471
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKKValrkLEGGIPNQALREIKALqACQ-------GHPYVVK----LRDvfPHGTGFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGgSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLqticM 550
Cdd:cd07832  77 LVFEYMLS-SLSEVLRDEeRPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA-RL----F 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVT---GTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKP--------------------P----WAEYE 602
Cdd:cd07832 151 SEEDPRLYShqvATRWYRAPELLYGsRKYDEGVDLWAVGCIFAELLNGSPlfpgendieqlaivlrtlgtPnektWPELT 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 603 AMAAIFKIaTQPTNPQLP--SHI---SEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07832 231 SLPDYNKI-TFPESKGIRleEIFpdcSPEAIDLLKGLLVyNPKKRLSAEEALRHPY 285
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
397-650 1.84e-33

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: 129.03  E-value: 1.84e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 476
Cdd:cd14083   9 EVLGTGAFSEVVLAEDKATGKLVAIKCI---DKKALKGKE-DSLENEIAVLRKIKHPNIVQLLDIYESKS--HLYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-----RDSagNVKLGDFGASKrlqticMS 551
Cdd:cd14083  83 VTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyyspdEDS--KIMISDFGLSK------ME 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTG-MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLpSHISEHG 627
Cdd:cd14083 155 DSGvMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFydeNDSKLFAQILKAEYEFDSPYW-DDISDSA 233
                       250       260
                ....*....|....*....|....
gi 42794767 628 RDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14083 234 KDFIRHLMeKDPNKRYTCEQALEH 257
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
397-652 1.85e-33

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: 130.81  E-value: 1.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKE-VSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLR---KSEMLEKEqVAHVRAERDILAEADNPWVVKLYYSFQD--EENLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSgtgm 555
Cdd:cd05599  82 FLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLA---- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS--HISEHGRDFLRR 633
Cdd:cd05599 158 YSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPevPISPEAKDLIER 237
                       250       260
                ....*....|....*....|..
gi 42794767 634 IFVEARQR---PSAEELLTHHF 652
Cdd:cd05599 238 LLCDAEHRlgaNGVEEIKSHPF 259
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
397-609 2.99e-33

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: 128.37  E-value: 2.99e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKevsaleceiQLLKNLQHER---IVQYYGCLRDR------AE 467
Cdd:cd05611   2 KPISKGAFGSVYLAKKRSTGDYFAIKVL---KKSDMIAK---------NQVTNVKAERaimMIQGESPYVAKlyysfqSK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqt 547
Cdd:cd05611  70 DYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR---- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794767 548 ICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFK 609
Cdd:cd05611 146 NGLEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPF-HAETPDAVFD 206
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
398-650 3.23e-33

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: 129.58  E-value: 3.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYM 477
Cdd:cd14094  10 VIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYS--SDGMLYMVFEFM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGS-----VKDQLKAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd14094  88 DGADlcfeiVKRADAGF-VYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVAIQLGESG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMrsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaeYEAMAAIFKIATQ---PTNPQLPSHISEH 626
Cdd:cd14094 167 LVAGGR---VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKgkyKMNPRQWSHISES 241
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14094 242 AKDLVRRMLmLDPAERITVYEALNH 266
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
396-650 7.52e-33

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: 127.28  E-value: 7.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPET-SKEVSALECEIQLLKNLQHERIVQyygcLRDRAE--KTLTI 472
Cdd:cd14097   6 GRKLGQGSFGVVIEATHKETQTKWAIKKI----NREKAgSSAVKLLEREVDILKHVNHAHIIH----LEEVFEtpKRMYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG-------NVKLGDFGASkrL 545
Cdd:cd14097  78 VMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLS--V 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLPSh 622
Cdd:cd14097 156 QKYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFvakSEEKLFEEIRKGDLTFTQSVWQS- 234
                       250       260
                ....*....|....*....|....*....
gi 42794767 623 ISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14097 235 VSDAAKNVLQQLLkVDPAHRMTASELLDN 263
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
398-604 8.04e-33

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: 127.70  E-value: 8.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLC-YDV---DTGRELASKQVQFDpdspeTSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIF 473
Cdd:cd05081  11 QLGKGNFGSVELCrYDPlgdNTGALVAVKQLQHS-----GPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRSLRLV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL----QTI 548
Cdd:cd05081  86 MEYLPSGCLRDFLqRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpldkDYY 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVtgtpYWMSPEVISGEGYGRKADVWSLGCTVVEMLT----EKPPWAEYEAM 604
Cdd:cd05081 166 VVREPGQSPI----FWYAPESLSDNIFSRQSDVWSFGVVLYELFTycdkSCSPSAEFLRM 221
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
396-650 8.54e-33

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: 127.08  E-value: 8.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLK-NLQHERIVQYYGCLRDRAEktLTIFM 474
Cdd:cd14106  13 STPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILH---EIAVLElCKDCPRVVNLHEVYETRSE--LILIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRLQTicms 551
Cdd:cd14106  88 ELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILltsEFPLGDIKLCDFGISRVIGE---- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIA-TQPTNpqLPSHISEHG 627
Cdd:cd14106 164 GEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGgddKQETFLNISQCNlDFPEE--LFKDVSPLA 241
                       250       260
                ....*....|....*....|....
gi 42794767 628 RDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14106 242 IDFIKRLLVkDPEKRLTAKECLEH 265
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
397-655 3.07e-32

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: 127.26  E-value: 3.07e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSALEC--EIQLLKNLQHERIVQYYGCLRDRAE---KTLT 471
Cdd:cd07834   6 KPIGSGAYGVVCSAYDKRTGRKVAIKKIS-----NVFDDLIDAKRIlrEIKILRHLKHENIIGLLDILRPPSPeefNDVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPG--GSVkdqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTIC 549
Cdd:cd07834  81 IVTELMETdlHKV---IKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA-RGVDPD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKP--PWAEY----------------EAMAAIFK- 609
Cdd:cd07834 157 EDKGFLTEYVVTRWYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPlfPGRDYidqlnlivevlgtpseEDLKFISSe 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 610 -----IATQPTNP-----QLPSHISEHGRDFLRRIFV-EARQRPSAEELLTH-HFAQL 655
Cdd:cd07834 237 karnyLKSLPKKPkkplsEVFPGASPEAIDLLEKMLVfNPKKRITADEALAHpYLAQL 294
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
397-607 3.37e-32

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: 126.17  E-value: 3.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYL-CYDV---DTGRELASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDRAEKTLTI 472
Cdd:cd05080  10 RDLGEGHFGKVSLyCYDPtndGTGEMVAVKALKADCGPQHRSGWKQ----EIDILKTLYHENIVKYKGCCSEQGGKSLQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT----I 548
Cdd:cd05080  86 IMEYVPLGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEgheyY 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 549 CMSGTGMRSVtgtpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE----KPPWAEYEAMAAI 607
Cdd:cd05080 165 RVREDGDSPV----FWYAPECLKEYKFYYASDVWSFGVTLYELLTHcdssQSPPTKFLEMIGI 223
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
396-650 5.13e-32

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: 125.07  E-value: 5.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVS--ALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIF 473
Cdd:cd14196  10 GEELGSGQFAIVKKCREKSTGLEYAAKFIK-KRQSRASRRGVSreEIEREVSILRQVLHPNIITLHDVYENRTD--VVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAG---NVKLGDFGASKRLQtic 549
Cdd:cd14196  87 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIE--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHISEH 626
Cdd:cd14196 164 -DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVSYD-FDEEFFSHTSEL 241
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14196 242 AKDFIRKLLVkETRKRLTIQEALRH 266
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
392-656 5.35e-32

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: 125.14  E-value: 5.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSALEC--EIQLLKNLQHERIVQYYGCLRDRAEkt 469
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIF----EMMDAKARQDCvkEIDLLKQLNHPNVIKYLDSFIEDNE-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGA----LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL 545
Cdd:cd08228  77 LNIVLELADAGDLSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTicmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIATQPTNPQLPS-HI 623
Cdd:cd08228 157 SS---KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAAlQSPFYGDKMNLFSLCQKIEQCDYPPLPTeHY 233
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 624 SEHGRDFLRR-IFVEARQRPSAEelLTHHFAQLM 656
Cdd:cd08228 234 SEKLRELVSMcIYPDPDQRPDIG--YVHQIAKQM 265
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
398-596 6.53e-32

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: 125.23  E-value: 6.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYM 477
Cdd:cd07846   8 LVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKK--IAMR-EIKMLKQLRHENLVNLIEVFRRK--KRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 pGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqTICMSGTGMR 556
Cdd:cd07846  83 -DHTVLDDLEKYpNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---TLAAPGEVYT 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42794767 557 SVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07846 159 DYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGEP 199
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
397-604 6.85e-32

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: 125.13  E-value: 6.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLC-YDV---DTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTI 472
Cdd:cd14205  10 QQLGKGNFGSVEMCrYDPlqdNTGEVVAVKKLQH-----STEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd14205  85 IMEYLPYGSLRDYLqKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEY 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT----EKPPWAEYEAM 604
Cdd:cd14205 165 YKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyiekSKSPPAEFMRM 221
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
397-654 6.92e-32

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: 125.03  E-value: 6.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALE----CEIQLLKNLQ-HERIVQyygcLRDRAEKTLT 471
Cdd:cd14182   9 EILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVQELReatlKEIDILRKVSgHPNIIQ----LKDTYETNTF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEY--MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQtic 549
Cdd:cd14182  85 FFLVFdlMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLD--- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSVTGTPYWMSPEVI------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT---QPTNPQLP 620
Cdd:cd14182 162 -PGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSgnyQFGSPEWD 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42794767 621 SHiSEHGRDFLRRIF-VEARQRPSAEELLTHHFAQ 654
Cdd:cd14182 241 DR-SDTVKDLISRFLvVQPQKRYTAEEALAHPFFQ 274
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
399-652 9.72e-32

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: 124.45  E-value: 9.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIFMEY 476
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCELQ---DRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKKCIVLVTEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGASKRLQTicmsgT 553
Cdd:cd14031  95 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIfITGPTGSVKIGDLGLATLMRT-----S 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISE-HGRDFLR 632
Cdd:cd14031 170 FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDpEVKEIIE 248
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIFVEAR-QRPSAEELLTHHF 652
Cdd:cd14031 249 GCIRQNKsERLSIKDLLNHAF 269
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
397-652 1.10e-31

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: 125.50  E-value: 1.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELA----SKQVQFDPDspetskEVSALECEIQLLKNLQHERI--VQYYGCLRDRaektL 470
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAmkilRKEVIIAKD------EVAHTVTESRVLQNTRHPFLtaLKYAFQTHDR----L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicm 550
Cdd:cd05595  71 CFVMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGIT--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDF 630
Cdd:cd05595 148 DGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEI--RFPRTLSPEAKSL 225
                       250       260
                ....*....|....*....|....*...
gi 42794767 631 LRRIF-VEARQR----PS-AEELLTHHF 652
Cdd:cd05595 226 LAGLLkKDPKQRlgggPSdAKEVMEHRF 253
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
399-655 1.13e-31

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: 124.77  E-value: 1.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDL-----RKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDE--LWVVMEFLE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSGTGMRSV 558
Cdd:cd06658 103 GGALTD-IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQ---VSKEVPKRKSL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQ-PTNPQLPSHISEHGRDFLRRIFV- 636
Cdd:cd06658 179 VGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNlPPRVKDSHKVSSVLRGFLDLMLVr 258
                       250
                ....*....|....*....
gi 42794767 637 EARQRPSAEELLTHHFAQL 655
Cdd:cd06658 259 EPSQRATAQELLQHPFLKL 277
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
399-650 1.17e-31

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: 123.65  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASK---QVQFDPDSPETSKEVSALeceiqllKNLQHERIVQYYGCLrdraEKTLTIFM- 474
Cdd:cd14078  11 IGSGGFAKVKLATHILTGEKVAIKimdKKALGDDLPRVKTEIEAL-------KNLSHQHICRLYHVI----ETDNKIFMv 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 -EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-ASK-------RL 545
Cdd:cd14078  80 lEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGlCAKpkggmdhHL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICmsgtgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQPTNPQLPSHIS 624
Cdd:cd14078 160 ETCC----------GSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKI--QSGKYEEPEWLS 227
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14078 228 PSSKLLLDQMLqVDPKKRITVKELLNH 254
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
392-649 1.22e-31

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: 124.03  E-value: 1.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKL---LGQGAFGRVYLC-YdvdTGRELASKQVQFDPDSPETSKEVSAlecEIQLLkNLQHERIVQYY----GCLR 463
Cdd:cd13979   1 DWEPLRLqepLGSGGFGSVYKAtY---KGETVAVKIVRRRRKNRASRQSFWA---ELNAA-RLRHENIVRVLaaetGTDF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 464 DRAEktlTIFMEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 542
Cdd:cd13979  74 ASLG---LIIMEYCGNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 KRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQL 619
Cdd:cd13979 151 VKLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAglrQHVLYAVVAKDLRPDLSGLE 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 620 PSHISEHGRDFLRRIF-VEARQRPSAEELLT 649
Cdd:cd13979 231 DSEFGQRLRSLISRCWsAQPAERPNADESLL 261
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
396-632 1.69e-31

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 125.32  E-value: 1.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:PTZ00263  23 GETLGTGSFGRVRIAKHKGTGEYYAIKCLK--KREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQD--ENRVYFLLE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ----TICms 551
Cdd:PTZ00263  99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPdrtfTLC-- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  552 gtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDFL 631
Cdd:PTZ00263 177 --------GTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRL--KFPNWFDGRARDLV 246

                 .
gi 42794767  632 R 632
Cdd:PTZ00263 247 K 247
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
392-652 1.73e-31

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: 124.15  E-value: 1.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDS---PETSKEvsalecEIQLLKNLQHERIVQyygcLRD--RA 466
Cdd:cd07860   1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETegvPSTAIR------EISLLKELNHPNIVK----LLDviHT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKTLTIFMEYMpggsvKDQLKAY------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd07860  71 ENKLYLVFEFL-----HQDLKKFmdasalTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLqticmsGTGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEK---PPWAEYEAMAAIFKIATQ 613
Cdd:cd07860 146 LARAF------GVPVRTYTHevvTLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTRRalfPGDSEIDQLFRIFRTLGT 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 614 PTN------PQLPSH------------------ISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07860 220 PDEvvwpgvTSMPDYkpsfpkwarqdfskvvppLDEDGRDLLSQMLHyDPNKRISAKAALAHPF 283
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
398-633 2.23e-31

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: 123.58  E-value: 2.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEV----SALECEIQllKNLQHERIVQYYGCLRDRAEKTLTIf 473
Cdd:cd13990   7 LLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQNyikhALREYEIH--KSLDHPRIVKLYDVFEIDTDSFCTV- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYL--HSNMIVHRDIKGANILRDS---AGNVKLGDFGASKRLQTI 548
Cdd:cd13990  84 LEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSgnvSGEIKITDFGLSKIMDDE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGM---RSVTGTPYWMSPEV-ISGEGYGR---KADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI-----ATQPTN 616
Cdd:cd13990 164 SYNSDGMeltSQGAGTYWYLPPECfVVGKTPPKissKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEEntilkATEVEF 243
                       250
                ....*....|....*..
gi 42794767 617 PQLPsHISEHGRDFLRR 633
Cdd:cd13990 244 PSKP-VVSSEAKDFIRR 259
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
399-652 4.17e-31

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: 122.78  E-value: 4.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDS---PETskevsALEcEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvPST-----AIR-EISLLKELNHPNIVRLLDVVHS--ENKLYLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMpggsvkDQ-LKAY------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqti 548
Cdd:cd07835  79 FL------DLdLKKYmdssplTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cmsGTGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTN----- 616
Cdd:cd07835 150 ---GVPVRTYTHevvTLWYRAPEILLGsKHYSTPVDIWSVGCIFAEMVTRRPLFPgdsEIDQLFRIFRTLGTPDEdvwpg 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 617 -----------PQ-----LPSHI---SEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07835 227 vtslpdykptfPKwarqdLSKVVpslDEDGLDLLSQMLVyDPAKRISAKAALQHPY 282
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
392-652 7.68e-31

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: 121.51  E-value: 7.68e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLT 471
Cdd:cd14186   2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMI--DKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFED--SNYVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticM 550
Cdd:cd14186  78 LVLEMCHNGEMSRYLKNRKkPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLK---M 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHGRDF 630
Cdd:cd14186 155 PHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVL--ADYEMPAFLSREAQDL 232
                       250       260
                ....*....|....*....|...
gi 42794767 631 LRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd14186 233 IHQLLRKnPADRLSLSSVLDHPF 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
392-596 7.94e-31

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: 122.81  E-value: 7.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKE---VSALEcEIQLLKNLQHERIVQYYGCLRDRAEK 468
Cdd:cd07866   9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILM-----HNEKDgfpITALR-EIKILKKLKHPNVVPLIDMAVERPDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TL----TIFM--EYM----------PggSVKdqlkaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG 532
Cdd:cd07866  83 SKrkrgSVYMvtPYMdhdlsgllenP--SVK--------LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 533 NVKLGDFG-------ASKRLQTicMSGTGMRSVTG---TPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07866 153 ILKIADFGlarpydgPPPNPKG--GGGGGTRKYTNlvvTRWYRPPELLLGErRYTTAVDIWGIGCVFAEMFTRRP 225
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
398-649 8.25e-31

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: 121.35  E-value: 8.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDvdTGRELASKQVQFDPDSpETSKEVSALECEIQLLKNLQHERIVQYYG-CLrdrAEKTLTIFMEY 476
Cdd:cd14061   1 VIGVGGFGKVYRGIW--RGEEVAVKAARQDPDE-DISVTLENVRQEARLFWMLRHPNIIALRGvCL---QPPNLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNM---IVHRDIKGANILRDSAGN--------VKLGDFGASKRL 545
Cdd:cd14061  75 ARGGALNRVLAGR-KIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIEnedlenktLKITDFGLAREW 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTIcmsgTGMrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISE 625
Cdd:cd14061 154 HKT----TRM-SAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTLPIPSTCPE 228
                       250       260
                ....*....|....*....|....*
gi 42794767 626 HGRDFLRRIF-VEARQRPSAEELLT 649
Cdd:cd14061 229 PFAQLMKDCWqPDPHDRPSFADILK 253
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
399-652 1.32e-30

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: 121.52  E-value: 1.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMP 478
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDI-TVELQKQIMS---ELEILYKCDSPYIIGFYGAFF--VENRISICTEFMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSvkdqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmSGTGMRSV 558
Cdd:cd06619  83 GGS----LDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL-----VNSIAKTY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 559 TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA------IFKIATQPTNPQLPSH-ISEHGRDFL 631
Cdd:cd06619 154 VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGslmplqLLQCIVDEDPPVLPVGqFSEKFVHFI 233
                       250       260
                ....*....|....*....|..
gi 42794767 632 RRIFVEA-RQRPSAEELLTHHF 652
Cdd:cd06619 234 TQCMRKQpKERPAPENLMDHPF 255
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
399-617 1.40e-30

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: 120.88  E-value: 1.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIFMEY 476
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSE---EVEMLKGLQHPNIVRFYDSWKStvRGHKCIILVTEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGaskrLQTIcMSGT 553
Cdd:cd14033  86 MTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIfITGPTGSVKIGDLG----LATL-KRAS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 554 GMRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP 617
Cdd:cd14033 161 FAKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKP 223
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
396-650 1.91e-30

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: 120.67  E-value: 1.91e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFD---PDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTI 472
Cdd:cd14076   6 GRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKlirRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLK--TKKYIGI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSG 552
Cdd:cd14076  84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDH--FNG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPE-VISGEGY-GRKADVWSLGCTVVEMLTEKPPW------AEYEAMAAIFKIATQpTNPQLPSHIS 624
Cdd:cd14076 162 DLMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFdddphnPNGDNVPRLYRYICN-TPLIFPEYVT 240
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14076 241 PKARDLLRRILVpNPRKRIRLSAIMRH 267
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
399-650 2.16e-30

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: 120.54  E-value: 2.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASK---------QVQF----DP--DSPETSKEVSALEC---EIQLLKNLQHERIVQYYG 460
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKilskkkllkQAGFfrrpPPrrKPGALGKPLDPLDRvyrEIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 461 CLRDRAEKTLTIFMEYMPGGSVKdQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd14118  82 VLDDPNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRLQTICMSGTgmrSVTGTPYWMSPEVISGEGY---GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTN- 616
Cdd:cd14118 161 VSNEFEGDDALLS---STAGTPAFMAPEALSESRKkfsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVf 237
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42794767 617 PQLPShISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14118 238 PDDPV-VSEQLKDLILRMLDkNPSERITLPEIKEH 271
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
397-652 2.83e-30

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: 121.55  E-value: 2.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELA----SKQVQF---DPDSPETSKEVSALECEiqllknlqHERIVQYYGCLRDraEKT 469
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAikvlKKEVIIeddDVECTMTEKRVLALANR--------HPFLTGLHACFQT--EDR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK------ 543
Cdd:cd05570  71 LYFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKegiwgg 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 -RLQTICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMaaIFKiATQPTNPQLPS 621
Cdd:cd05570 151 nTTSTFC----------GTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFeGDDEDE--LFE-AILNDEVLYPR 217
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 42794767 622 HISEHGRDFLRRIFVEARQR-----PSAE-ELLTHHF 652
Cdd:cd05570 218 WLSREAVSILKGLLTKDPARrlgcgPKGEaDIKAHPF 254
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
399-650 4.03e-30

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: 119.23  E-value: 4.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKqvqFDPDSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd14114  10 LGTGAFGVVHRCTERATGNNFAAK---FIMTPHESDKET--VRKEIQIMNQLHHPKLINLHDAFEDDNE--MVLILEFLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQticmSGTGM 555
Cdd:cd14114  83 GGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMctTKRSNEVKLIDFGLATHLD----PKESV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHGRDFLRR 633
Cdd:cd14114 159 KVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSafSGISEEAKDFIRK 238
                       250
                ....*....|....*...
gi 42794767 634 IFV-EARQRPSAEELLTH 650
Cdd:cd14114 239 LLLaDPNKRMTIHQALEH 256
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
397-652 4.30e-30

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: 119.30  E-value: 4.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd14192  10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKV-----KGAKEREEVKNEINIMNQLNHVNLIQLYDAFESK--TNLTLIMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQL--KAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN-VKLGDFGASKRLQticmSG 552
Cdd:cd14192  83 VDGGELFDRItdESY-QLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYK----PR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKiATQPTNPQLPSHISEHGRD 629
Cdd:cd14192 158 EKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFlgeTDAETMNNIVN-CKWDFDAEAFENLSEEAKD 236
                       250       260
                ....*....|....*....|....
gi 42794767 630 FLRRIFVEARQ-RPSAEELLTHHF 652
Cdd:cd14192 237 FISRLLVKEKScRMSATQCLKHEW 260
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
400-652 4.87e-30

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: 118.90  E-value: 4.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 400 GQGAFGRVYLCYDVDTGRELASKqvqfdpdspETSK-------EVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:cd05578   9 GKGSFGKVCIVQKKDTKKMFAMK---------YMNKqkciekdSVRNVLNELEILQELEHPFLVNLWYSFQD--EEDMYM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmsG 552
Cdd:cd05578  78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTD----G 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKI-ATQPTN-PQLPSHISEHGRDF 630
Cdd:cd05578 154 TLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPY-EIHSRTSIEEIrAKFETAsVLYPAGWSEEAIDL 232
                       250       260
                ....*....|....*....|....
gi 42794767 631 LRRIF-VEARQRPSA-EELLTHHF 652
Cdd:cd05578 233 INKLLeRDPQKRLGDlSDLKNHPY 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
395-652 7.47e-30

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: 118.59  E-value: 7.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLlGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevsALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFM 474
Cdd:cd14075   7 RGEL-GSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQR---LLSREISSMEKLHHPNIIRLYEVVE--TLSKLHLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqTICMSGTG 554
Cdd:cd14075  81 EYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFS----THAKRGET 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPwaeyeamaaiFKIATQPT--------NPQLPSHISE 625
Cdd:cd14075 157 LNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMP----------FRAETVAKlkkcilegTYTIPSYVSE 226
                       250       260
                ....*....|....*....|....*...
gi 42794767 626 HGRDFLRRIFVEA-RQRPSAEELLTHHF 652
Cdd:cd14075 227 PCQELIRGILQPVpSDRYSIDEIKNSEW 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
392-634 9.50e-30

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: 119.05  E-value: 9.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLT 471
Cdd:cd14209   2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIL--DKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNS--NLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ----T 547
Cdd:cd14209  78 MVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKgrtwT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 ICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHG 627
Cdd:cd14209 158 LC----------GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS--GKVRFPSHFSSDL 225

                ....*..
gi 42794767 628 RDFLRRI 634
Cdd:cd14209 226 KDLLRNL 232
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
397-652 9.80e-30

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: 118.52  E-value: 9.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETS-KEVSALEceiQLLKNLQ--HERIVQYYGCLRDRaEKTLTIF 473
Cdd:cd14133   5 EVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSlDEIRLLE---LLNKKDKadKYHIVRLKDVFYFK-NHLCIVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 -------MEYMpggsvKDQLKAYgaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASkr 544
Cdd:cd14133  81 ellsqnlYEFL-----KQNKFQY--LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILlaSYSRCQIKIIDFGSS-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 lqtiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPtnpqlPS 621
Cdd:cd14133 152 ----CFLTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFpgaSEVDQLARIIGTIGIP-----PA 222
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 622 HISEHGR-------DFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14133 223 HMLDQGKaddelfvDFLKKLLeIDPKERPTASQALSHPW 261
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
399-620 1.09e-29

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: 118.32  E-value: 1.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVsaLEcEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKAL--LK-EAEKMERARHSYVLPLLGVCVERRS--LGLVMEYME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKA-YGALTESVTRKYTRQILEGMSYLHsNM---IVHRDIKGANILRDSAGNVKLGDFGASK-RLQTICMSGT 553
Cdd:cd13978  76 NGSLKSLLEReIQDVPWSLRFRIIHEIALGMNFLH-NMdppLLHHDLKPENILLDNHFHVKISDFGLSKlGMKSISANRR 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 554 -GMRSVTGTPYWMSPEVISgEGYGR---KADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP 620
Cdd:cd13978 155 rGTENLGGTPIYMAPEAFD-DFNKKptsKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPSLD 224
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
400-648 1.10e-29

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: 117.75  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 400 GQGAFGRVYLCYDVDTGRELASKQVqfdpdspetskevSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMPG 479
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKL-------------LKIEKEAEILSVLSHRNIIQFYGAILE--APNYGIVTEYASY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 480 GSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNM---IVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSgt 553
Cdd:cd14060  67 GSLFDYLNSNESeeMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHsHTTHMS-- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 gmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRR 633
Cdd:cd14060 145 ----LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRR 220
                       250
                ....*....|....*.
gi 42794767 634 IF-VEARQRPSAEELL 648
Cdd:cd14060 221 CWeADVKERPSFKQII 236
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
396-650 1.13e-29

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: 118.58  E-value: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSA--LECEIQLLKNLQHERIVQYYGCLRDRAEktLTIF 473
Cdd:cd14194  10 GEELGSGQFAVVKKCREKSTGLQYAAKFIK-KRRTKSSRRGVSRedIEREVSILKEIQHPNVITLHEVYENKTD--VILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAG-NVKLGDFGASKRLQtic 549
Cdd:cd14194  87 LELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMlldRNVPKpRIKIIDFGLAHKID--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHISEH 626
Cdd:cd14194 164 -FGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANVSAVNYE-FEDEYFSNTSAL 241
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14194 242 AKDFIRRLLVkDPKKRMTIQDSLQH 266
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
396-650 1.26e-29

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: 118.50  E-value: 1.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQ-HERIVQYYGCLRDRAEKTLTifM 474
Cdd:cd14197  14 GRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIH---EIAVLELAQaNPWVINLHEVYETASEMILV--L 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQtic 549
Cdd:cd14197  89 EYAAGGEIFNQCVAdrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILK--- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLpSHISEH 626
Cdd:cd14197 166 -NSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLgddKQETFLNISQMNVSYSEEEF-EHLSES 243
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14197 244 AIDFIKTLLIkKPENRATAEDCLKH 268
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
392-652 1.34e-29

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: 120.72  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQV----QFDPDspetskEVSALECEIQLLKNLQHERIVQYYGCLRDRAe 467
Cdd:cd05629   2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLlkseMFKKD------QLAHVKAERDVLAESDSPWVVSLYYSFQDAQ- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 kTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS----- 542
Cdd:cd05629  75 -YLYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhk 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 -------KRL--QTICMSGTGMR------------------------------SVTGTPYWMSPEVISGEGYGRKADVWS 583
Cdd:cd05629 154 qhdsayyQKLlqGKSNKNRIDNRnsvavdsinltmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQQGYGQECDWWS 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 584 LGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS--HISEHGRDFLRRIFVEARQ---RPSAEELLTHHF 652
Cdd:cd05629 234 LGAIMFECLIGWPPFCSENSHETYRKIINWRETLYFPDdiHLSVEAEDLIRRLITNAENrlgRGGAHEIKSHPF 307
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
399-654 1.81e-29

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: 118.69  E-value: 1.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06615   9 LGAGNGGVVTKVLHRPSGLIMARKLIHLEI-KPAIRNQIIR---ELKVLHECNSPYIVGFYGAFYSDGE--ISICMEHMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSGTGMR 556
Cdd:cd06615  83 GGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLiDSMANSFVGTR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SvtgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTEK-----PPWAEYEAM--------------------------- 604
Cdd:cd06615 163 S------YMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRypippPDAKELEAMfgrpvsegeakeshrpvsghppdsprp 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 605 AAIFK----IATQPTnPQLPS-HISEHGRDFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd06615 237 MAIFElldyIVNEPP-PKLPSgAFSDEFQDFVDKCLKkNPKERADLKELTKHPFIK 291
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
397-652 2.21e-29

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: 119.05  E-value: 2.21e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDV---DTGRELASKQ------VQFDPDSPETSKEVSALECeiqllknLQHERIVQ-YYgclrdrA 466
Cdd:cd05584   2 KVLGKGGYGKVFQVRKTtgsDKGKIFAMKVlkkasiVRNQKDTAHTKAERNILEA-------VKHPFIVDlHY------A 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKT---LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd05584  69 FQTggkLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 -RLQTICMSGTgmrsVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNpqLPSH 622
Cdd:cd05584 149 eSIHDGTVTHT----FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLN--LPPY 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42794767 623 ISEHGRDFLRRIFVeaRQRPS--------AEELLTHHF 652
Cdd:cd05584 223 LTNEARDLLKKLLK--RNVSSrlgsgpgdAEEIKAHPF 258
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
397-652 2.31e-29

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: 119.79  E-value: 2.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGR----ELASKQvqfdpdspETSK--EVSALECEIQLLKNLQHERIVQYYGCLRDraEKTL 470
Cdd:cd05596  32 KVIGRGAFGEVQLVRHKSTKKvyamKLLSKF--------EMIKrsDSAFFWEERDIMAHANSEWIVQLHYAFQD--DKYL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticM 550
Cdd:cd05596 102 YMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK-----M 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGM-RSVT--GTPYWMSPEVISGEG----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS-- 621
Cdd:cd05596 176 DKDGLvRSDTavGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFPDdv 255
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 622 HISEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05596 256 EISKDAKSLICAFLTDREVRlgrNGIEEIKAHPF 289
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
399-654 2.54e-29

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: 118.62  E-value: 2.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdspeTSKE---VSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFME 475
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVRMD-----NERDgipISSLR-EITLLLNLRHPNIVELKEVVVGKHLDSIFLVME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPG--GSVKDQLKAygALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSgt 553
Cdd:cd07845  89 YCEQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKP-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 gMRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKP--------------------P----WAEYEAMAAI- 607
Cdd:cd07845 165 -MTPKVVTLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKPllpgkseieqldliiqllgtPnesiWPGFSDLPLVg 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 608 -FKIATQPTN---PQLPShISEHGRDFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd07845 244 kFTLPKQPYNnlkHKFPW-LSEAGLRLLNFLLMyDPKKRATAEEALESSYFK 294
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
396-651 2.73e-29

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: 117.00  E-value: 2.73e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVsalecEIQLLKNlQHERIVQ----YYGCLRDRaeKTLT 471
Cdd:cd14089   6 KQVLGLGINGKVLECFHKKTGEKFALKVLR---DNPKARREV-----ELHWRAS-GCPHIVRiidvYENTYQGR--KCLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKR-- 544
Cdd:cd14089  75 VVMECMEGGELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKEtt 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 ----LQTICMsgtgmrsvtgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMaAIF-----KIATQ-- 613
Cdd:cd14089 155 tkksLQTPCY----------TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL-AISpgmkkRIRNGqy 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42794767 614 --PtNPQLpSHISEHGRDFLRRIF-VEARQRPSAEELLTHH 651
Cdd:cd14089 224 efP-NPEW-SNVSEEAKDLIRGLLkTDPSERLTIEEVMNHP 262
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
399-650 2.75e-29

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: 117.73  E-value: 2.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASK---QVQFDPDSpetskevsalECEIqLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd14091   8 IGKGSYSVCKRCIHKATGKEYAVKiidKSKRDPSE----------EIEI-LLRYGQHPNIITLRDVYDD--GNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN---VKLGDFGASKRLqticms 551
Cdd:cd14091  75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyADESGDpesLRICDFGFAKQL------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gtgmRSVTG---TP-Y---WMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA--EYEAMAAIFKiatQPTNPQLP-- 620
Cdd:cd14091 149 ----RAENGllmTPcYtanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgPNDTPEVILA---RIGSGKIDls 221
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42794767 621 ----SHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14091 222 ggnwDHVSDSAKDLVRKMLhVDPSQRPTAAQVLQH 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
397-650 2.78e-29

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: 117.13  E-value: 2.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQV---QFdpdspeTSKEVSALECEIQLLKNLQHERIVqyygCLRDRAEKTLTIF 473
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIdklRF------PTKQESQLRNEVAILQQLSHPGVV----NLECMFETPERVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 --MEYMPGgsvkDQLK-----AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASK 543
Cdd:cd14082  79 vvMEKLHG----DMLEmilssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFAR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 rlqtICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTNPQlpS 621
Cdd:cd14082 155 ----IIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAfmYPPNPW--K 228
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 622 HISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14082 229 EISPDAIDLINNLLqVKMRKRYSVDKSLSH 258
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
396-650 3.33e-29

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: 116.59  E-value: 3.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFME 475
Cdd:cd14185   5 GRTIGDGNFAVVKECRHWNENQEYAMKII----DKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYE--TEKEIYLILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDqlkaygALTESVtrKYTRQ--------ILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFG--- 540
Cdd:cd14185  79 YVRGGDLFD------AIIESV--KFTEHdaalmiidLCEALVYIHSKHIVHRDLKPENLLvqhnPDKSTTLKLADFGlak 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 -ASKRLQTICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEA-MAAIFKIATQPTNPQ 618
Cdd:cd14185 151 yVTGPIFTVC----------GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERdQEELFQIIQLGHYEF 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42794767 619 LP---SHISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14185 221 LPpywDNISEAAKDLISRLLVvDPEKRYTAKQVLQH 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
395-652 4.19e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 118.77  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetskEVSALEC-EIQLLKNLQHERIVQYYGCLRDRAEktLTIF 473
Cdd:PLN00034  78 RVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHED-----TVRRQICrEIEILRDVNHPNVVKCHDMFDHNGE--IQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  474 MEYMPGGSVKDQLKAYGALTESVTRkytrQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTI--CM 550
Cdd:PLN00034 151 LEFMDGGSLEGTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILaQTMdpCN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  551 SgtgmrSVtGTPYWMSPEVIS-----GEGYGRKADVWSLGCTVVEMLTEKPP--------WAEYeaMAAIfkIATQPtnP 617
Cdd:PLN00034 227 S-----SV-GTIAYMSPERINtdlnhGAYDGYAGDIWSLGVSILEFYLGRFPfgvgrqgdWASL--MCAI--CMSQP--P 294
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 42794767  618 QLPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:PLN00034 295 EAPATASREFRHFISCCLQrEPAKRWSAMQLLQHPF 330
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
399-652 4.34e-29

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: 117.26  E-value: 4.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetsKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMP 478
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEIRLELDE----SKFNQIIMELDILHKAVSPYIVDFYGAFF--IEGAVYMCMEYMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVkDQLKAYGALT----ESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSG 552
Cdd:cd06622  83 AGSL-DKLYAGGVATegipEDVLRRITYAVVKGLKFLKEEHnIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLvASLAKTN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSvtgtpyWMSPEVISGEG------YGRKADVWSLGCTVVEMLTEKPPWAEyEAMAAIF---KIATQPTNPQLPSHI 623
Cdd:cd06622 162 IGCQS------YMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYPP-ETYANIFaqlSAIVDGDPPTLPSGY 234
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 624 SEHGRDFLRRIFVE-ARQRPSAEELLTHHF 652
Cdd:cd06622 235 SDDAQDFVAKCLNKiPNRRPTYAQLLEHPW 264
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
392-650 5.07e-29

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: 116.17  E-value: 5.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLt 471
Cdd:cd14193   5 NVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIK-----ARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 iFMEYMPGGSVKDQL--KAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQt 547
Cdd:cd14193  79 -VMEYVDGGELFDRIidENYN-LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcvSREANQVKIIDFGLARRYK- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 icmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLpSHIS 624
Cdd:cd14193 156 ---PREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLgedDNETLNNILACQWDFEDEEF-ADIS 231
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIFVEARQ-RPSAEELLTH 650
Cdd:cd14193 232 EEAKDFISKLLIKEKSwRMSASEALKH 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
399-585 5.15e-29

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: 116.21  E-value: 5.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDvDTGRELASKQVQFDPDSPEtsKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd14161  11 LGKGTYGRVKKARD-SSGRLVAIKSIRKDRIKDE--QDLLHIRREIEIMSSLNHPHIISVYEVFENSSK--IVIVMEYAS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS------KRLQTICmsg 552
Cdd:cd14161  86 RGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSnlynqdKFLQTYC--- 162
                       170       180       190
                ....*....|....*....|....*....|....
gi 42794767 553 tgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLG 585
Cdd:cd14161 163 -------GSPLYASPEIVNGRPYiGPEVDSWSLG 189
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
399-655 5.40e-29

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: 116.75  E-value: 5.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEiqlLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06617   9 LGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDIS---MRSVDCPYTVTFYGALFREGD--VWICMEVMD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLqTICMSGT- 553
Cdd:cd06617  84 TSLDKFYKKVYDkglTIPEDILGKIAVSIVKALEYLHSKLsVIHRDVKPSNVLINRNGQVKLCDFGISGYL-VDSVAKTi 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 --GMRsvtgtPYwMSPEVISGE----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH-ISEH 626
Cdd:cd06617 163 daGCK-----PY-MAPERINPElnqkGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEEPSPQLPAEkFSPE 236
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTHHFAQL 655
Cdd:cd06617 237 FQDFVNKCLKkNYKERPNYPELLQHPFFEL 266
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
396-600 5.50e-29

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: 116.83  E-value: 5.50e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTgrELASKQVqFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFME 475
Cdd:cd14158  20 GNKLGEGGFGVVFKGYINDK--NVAVKKL-AAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQ--LCLVYT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticmSG 552
Cdd:cd14158  95 YMPNGSLLDRLACLNdtpPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARA------SE 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794767 553 TGMRS-----VTGTPYWMSPEVISGEgYGRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd14158 169 KFSQTimterIVGTTAYMAPEALRGE-ITPKSDIFSFGVVLLEIITGLPPVDE 220
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
399-635 5.69e-29

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: 116.97  E-value: 5.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASK---------QVQFDPDSP---------ETSKEVSALE---CEIQLLKNLQHERIVQ 457
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKvlskkkllkQYGFPRRPPprgskaaqgEQAKPLAPLErvyQEIAILKKLDHVNIVK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 458 YYGCLRDRAEKTLTIFMEYMPGGSVKdQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLG 537
Cdd:cd14200  88 LIEVLDDPAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 538 DFGASKRLQTicmSGTGMRSVTGTPYWMSPEVIS--GEGYGRKA-DVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQP 614
Cdd:cd14200 167 DFGVSNQFEG---NDALLSSTAGTPAFMAPETLSdsGQSFSGKAlDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKP 243
                       250       260
                ....*....|....*....|..
gi 42794767 615 TN-PQLPShISEHGRDFLRRIF 635
Cdd:cd14200 244 VEfPEEPE-ISEELKDLILKML 264
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
399-642 6.15e-29

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: 116.99  E-value: 6.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDspETSKEVSALEcEIQLLKNLQH------ERIVQYYGCLRDRAEKTLTI 472
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSVRVQTN--EDGLPLSTVR-EVALLKRLEAfdhpniVRLMDVCATSRTDRETKVTL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYmpggsVKDQLKAY-------GALTESVtRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRL 545
Cdd:cd07863  85 VFEH-----VDQDLRTYldkvpppGLPAETI-KDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA-RI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSgtgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLPSH 622
Cdd:cd07863 158 YSCQMA---LTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFcgnSEADQLGKIFDLIGLPPEDDWPRD 234
                       250       260
                ....*....|....*....|
gi 42794767 623 ISehgrdFLRRIFVEARQRP 642
Cdd:cd07863 235 VT-----LPRGAFSPRGPRP 249
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
396-650 7.98e-29

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: 115.50  E-value: 7.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFME 475
Cdd:cd14095   5 GRVIGDGNFAVVKECRDKATDKEYALKII----DKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTE--LYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAG--NVKLGDFG----ASKRLQT 547
Cdd:cd14095  79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLvvEHEDGskSLKLADFGlateVKEPLFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 ICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA-----EYEAMAAIFKIATQPTNPQLpSH 622
Cdd:cd14095 159 VC----------GTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspdrdQEELFDLILAGEFEFLSPYW-DN 227
                       250       260
                ....*....|....*....|....*....
gi 42794767 623 ISEHGRDFLRR-IFVEARQRPSAEELLTH 650
Cdd:cd14095 228 ISDSAKDLISRmLVVDPEKRYSAGQVLDH 256
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
399-652 8.01e-29

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: 116.66  E-value: 8.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKMDL-----RKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG----ASKRLQTicmsgtg 554
Cdd:cd06657 101 GGALTD-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGfcaqVSKEVPR------- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIfKIATQPTNPQLPS--HISEHGRDFLR 632
Cdd:cd06657 173 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM-KMIRDNLPPKLKNlhKVSPSLKGFLD 251
                       250       260
                ....*....|....*....|.
gi 42794767 633 RIFV-EARQRPSAEELLTHHF 652
Cdd:cd06657 252 RLLVrDPAQRATAAELLKHPF 272
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
397-652 8.89e-29

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: 117.07  E-value: 8.89e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELA----SKQVQFDPDspetskEVSALECEIQLLKNLQHERIVQ--YYGCLRDRaektL 470
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAikilKKEVIIAKD------EVAHTLTENRVLQNTRHPFLTSlkYSFQTNDR----L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcm 550
Cdd:cd05571  71 CFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISY-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 sGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDF 630
Cdd:cd05571 149 -GATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEV--RFPSTLSPEAKSL 225
                       250       260
                ....*....|....*....|....*...
gi 42794767 631 LRRIFV-EARQR----PS-AEELLTHHF 652
Cdd:cd05571 226 LAGLLKkDPKKRlgggPRdAKEIMEHPF 253
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
398-625 1.04e-28

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: 115.52  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCydVDTGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFMEY 476
Cdd:cd14146   1 IIGVGGFGKVYRA--TWKGQEVAVKAARQDPDEDIKATAESVRQ-EAKLFSMLRHPNIIKLEGvCLE---EPNLCLVMEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAY-GALTESVTRK--------YTRQILEGMSYLHSNMIV---HRDIKGANIL------RDSAGN--VKL 536
Cdd:cd14146  75 ARGGTLNRALAAAnAAPGPRRARRipphilvnWAVQIARGMLYLHEEAVVpilHRDLKSSNILllekieHDDICNktLKI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 537 GDFGASKRLQTicmsgTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTN 616
Cdd:cd14146 155 TDFGLAREWHR-----TTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLT 229

                ....*....
gi 42794767 617 PQLPSHISE 625
Cdd:cd14146 230 LPIPSTCPE 238
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
398-625 1.13e-28

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: 115.08  E-value: 1.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYlcYDVDTGRELASKQVQFDPDSpETSKEVSALECEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFMEY 476
Cdd:cd14148   1 IIGVGGFGKVY--KGLWRGEEVAVKAARQDPDE-DIAVTAENVRQEARLFWMLQHPNIIALRGvCLN---PPHLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLkAYGALTESVTRKYTRQILEGMSYLHSNMIV---HRDIKGANIL------RDSAGN--VKLGDFGASKRL 545
Cdd:cd14148  75 ARGGALNRAL-AGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILilepieNDDLSGktLKITDFGLAREW 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTicmsgTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISE 625
Cdd:cd14148 154 HK-----TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPE 228
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
392-650 1.40e-28

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: 115.66  E-value: 1.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQYYGCLRdrAEKTLT 471
Cdd:cd07836   1 NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIR----EISLMKELKHENIVRLHDVIH--TENKLM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGgsvkdQLKAY-------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkR 544
Cdd:cd07836  75 LVFEYMDK-----DLKKYmdthgvrGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA-R 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTICMSGTGMRSVtgTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLP 620
Cdd:cd07836 149 AFGIPVNTFSNEVV--TLWYRAPDVLLGsRTYSTSIDIWSVGCIMAEMITGRPLFPgtnNEDQLLKIFRIMGTPTESTWP 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 621 S------------------------HISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd07836 227 GisqlpeykptfpryppqdlqqlfpHADPLGIDLLHRLLqLNPELRISAHDALQH 281
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
392-631 1.77e-28

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: 115.51  E-value: 1.77e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQ-FDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEktL 470
Cdd:cd08229  25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQiFDLMDAKARADCIK---EIDLLKQLNHPNVIKYYASFIEDNE--L 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGA----LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ 546
Cdd:cd08229 100 NIVLELADAGDLSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TicmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIATQPTNPQLPS-HIS 624
Cdd:cd08229 180 S---KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAAlQSPFYGDKMNLYSLCKKIEQCDYPPLPSdHYS 256

                ....*..
gi 42794767 625 EHGRDFL 631
Cdd:cd08229 257 EELRQLV 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
397-650 1.82e-28

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: 114.74  E-value: 1.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEVSaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd14167   9 EVLGTGAFSEVVLAEEKRTQKLVAIKCI---AKKALEGKETS-IENEIAVLHKIKHPNIVALDDIYESGGH--LYLIMQL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR---DSAGNVKLGDFGASKrlqtICMSGT 553
Cdd:cd14167  83 VSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYyslDEDSKIMISDFGLSK----IEGSGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP-WAEYEA--MAAIFKIATQPTNPQLpSHISEHGRDF 630
Cdd:cd14167 159 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPfYDENDAklFEQILKAEYEFDSPYW-DDISDSAKDF 237
                       250       260
                ....*....|....*....|.
gi 42794767 631 LRRIF-VEARQRPSAEELLTH 650
Cdd:cd14167 238 IQHLMeKDPEKRFTCEQALQH 258
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
397-652 2.00e-28

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: 116.26  E-value: 2.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPEtSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 476
Cdd:cd05598   7 KTIGVGAFGEVSLVRKKDTNALYAMKTLR-KKDVLK-RNQVAHVKAERDILAEADNEWVVKLYYSFQDKE--NLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtICmsgTGMR 556
Cdd:cd05598  83 IPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG-------LC---TGFR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 -----------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHI 623
Cdd:cd05598 153 wthdskyylahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPheANL 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 624 SEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05598 233 SPEAKDLILRLCCDAEDRlgrNGADEIKAHPF 264
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
396-650 2.19e-28

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: 114.43  E-value: 2.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpdspETSK--EVSA--LECEIQLLKNLQHERIVQYYGCLrDRAEKtLT 471
Cdd:cd14074   8 EETLGRGHFAVVKLARHVFTGEKVAVKVI-------DKTKldDVSKahLFQEVRCMKLVQHPNVVRLYEVI-DTQTK-LY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQ-LKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGNVKLGDFGASKRLqtic 549
Cdd:cd14074  79 LILELGDGGDMYDYiMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKF---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQPTNPQLPSHISEHGR 628
Cdd:cd14074 155 QPGEKLETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI--MDCKYTVPAHVSPECK 232
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14074 233 DLIRRMLIrDPKKRASLEEIENH 255
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
399-617 2.96e-28

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: 114.40  E-value: 2.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAE--KTLTIFMEY 476
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCELQ---DRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkRCIVLVTEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGaskrLQTIcMSGT 553
Cdd:cd14032  86 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIfITGPTGSVKIGDLG----LATL-KRAS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 554 GMRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP 617
Cdd:cd14032 161 FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKP 223
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
392-632 3.30e-28

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: 114.14  E-value: 3.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLT 471
Cdd:cd14070   3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVID-KKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILE--TENSYY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMS 551
Cdd:cd14070  80 LVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA--EYEAMAAIFKIATQPTNPqLPSHISEHGRD 629
Cdd:cd14070 160 -DPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTvePFSLRALHQKMVDKEMNP-LPTDLSPGAIS 237

                ...
gi 42794767 630 FLR 632
Cdd:cd14070 238 FLR 240
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
399-647 3.83e-28

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: 113.69  E-value: 3.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCydVDTGRELASKQVQFDpdspetsKEVSALECEIQLLKNLQHERIVQYYGclRDRAEKTLTIFMEYMP 478
Cdd:cd14058   1 VGRGSFGVVCKA--RWRNQIVAVKIIESE-------SEKKAFEVEVRQLSRVDHPNIIKLYG--ACSNQKPVCLVMEYAE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSV------KDQLKAYgalTESVTRKYTRQILEGMSYLHS---NMIVHRDIKGANILRDSAG-NVKLGDFGaskrlqTI 548
Cdd:cd14058  70 GGSLynvlhgKEPKPIY---TAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGtVLKICDFG------TA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQP-TNPQLPSHISEHG 627
Cdd:cd14058 141 CDISTHMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNgERPPLIKNCPKPI 220
                       250       260
                ....*....|....*....|.
gi 42794767 628 RDFLRRIF-VEARQRPSAEEL 647
Cdd:cd14058 221 ESLMTRCWsKDPEKRPSMKEI 241
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
367-619 4.59e-28

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 117.44  E-value: 4.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  367 RSADSENALSVQerNVPTKSPSApiNWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETskevsalecEIQL 446
Cdd:PTZ00036  46 AGEDEDEEKMID--NDINRSPNK--SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNR---------ELLI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  447 LKNLQHERIV---QYY--GCLRdRAEKT--LTIFMEYMPGgSVKDQLKAYG----ALTESVTRKYTRQILEGMSYLHSNM 515
Cdd:PTZ00036 113 MKNLNHINIIflkDYYytECFK-KNEKNifLNVVMEFIPQ-TVHKYMKHYArnnhALPLFLVKLYSYQLCRALAYIHSKF 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  516 IVHRDIKGANILRD-SAGNVKLGDFGASKRLQticmsgTGMRSVT--GTPYWMSPEVISGE-GYGRKADVWSLGCTVVEM 591
Cdd:PTZ00036 191 ICHRDLKPQNLLIDpNTHTLKLCDFGSAKNLL------AGQRSVSyiCSRFYRAPELMLGAtNYTTHIDLWSLGCIIAEM 264
                        250       260       270
                 ....*....|....*....|....*....|.
gi 42794767  592 LTEKPPW---AEYEAMAAIFKIATQPTNPQL 619
Cdd:PTZ00036 265 ILGYPIFsgqSSVDQLVRIIQVLGTPTEDQL 295
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
392-650 4.85e-28

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: 113.25  E-value: 4.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQ--VQFDPDSPETSK--EVSALEceiqLLKnlQHERIVQYYgclRDRAE 467
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKskKPFRGPKERARAlrEVEAHA----ALG--QHPNIVRYY---SSWEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 -KTLTIFMEYMPGGSVKDQLKAYGALT---ESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd13997  72 gGHLYIQMELCENGSLQDALEELSPISklsEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RLqticmsGTGMRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEM-----LTEKPPWAEyeamaaifkiatQPTNP 617
Cdd:cd13997 152 RL------ETSGDVEEGDSRYLAPELLNENyTHLPKADIFSLGVTVYEAatgepLPRNGQQWQ------------QLRQG 213
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42794767 618 QLPSHISEHGRDFLRRIFV-----EARQRPSAEELLTH 650
Cdd:cd13997 214 KLPLPPGLVLSQELTRLLKvmldpDPTRRPTADQLLAH 251
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
397-585 5.44e-28

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: 113.26  E-value: 5.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQV---QFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF 473
Cdd:cd14071   6 RTIGKGNFAVVKLARHRITKTEVAIKIIdksQLDEENLKKIYR------EVQIMKMLNHPHIIKLYQVME--TKDMLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSGT 553
Cdd:cd14071  78 TEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK----PGE 153
                       170       180       190
                ....*....|....*....|....*....|...
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGY-GRKADVWSLG 585
Cdd:cd14071 154 LLKTWCGSPPYAAPEVFEGKEYeGPQLDIWSLG 186
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
396-650 6.97e-28

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: 113.35  E-value: 6.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVS--ALECEIQLLKNLQHERIVQYYGCLRDRAEKTLtiF 473
Cdd:cd14105  10 GEELGSGQFAVVKKCREKSTGLEYAAKFIK-KRRSKASRRGVSreDIEREVSILRQVLHPNIITLHDVFENKTDVVL--I 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDS---AGNVKLGDFGASKRLQtic 549
Cdd:cd14105  87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKnvpIPRIKLIDFGLAHKIE--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 mSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHISEH 626
Cdd:cd14105 164 -DGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgdTKQETLANITAVNYD-FDDEYFSNTSEL 241
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14105 242 AKDFIRQLLVkDPRKRMTIQESLRH 266
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
397-641 7.02e-28

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: 114.72  E-value: 7.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQ-LLKNLQHERIVQYYGCLRDRaEKtLTIFME 475
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQ--KKAILKRNEVKHIMAERNvLLKNVKHPFLVGLHYSFQTK-DK-LYFVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICMSGTgM 555
Cdd:cd05575  77 YVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCK--EGIEPSDT-T 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-----AE-YEamaaifKIATQPTnpQLPSHISEHGRD 629
Cdd:cd05575 154 STFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFysrdtAEmYD------NILHKPL--RLRTNVSPSARD 225
                       250
                ....*....|..
gi 42794767 630 FLRRIFVEARQR 641
Cdd:cd05575 226 LLEGLLQKDRTK 237
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
397-650 9.05e-28

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: 113.09  E-value: 9.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlqHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKS--NPRVVNLHEVYETTSE--IILILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQticmS 551
Cdd:cd14198  90 AAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIG----H 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLpSHISEHGR 628
Cdd:cd14198 166 ACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVgedNQETFLNISQVNVDYSEETF-SSVSQLAT 244
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIFVEA-RQRPSAEELLTH 650
Cdd:cd14198 245 DFIQKLLVKNpEKRPTAEICLSH 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
393-650 9.26e-28

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: 112.79  E-value: 9.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQ---FDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDRAEkt 469
Cdd:cd14195   7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKkrrLSSSRRGVSRE--EIEREVNILREIQHPNIITLHDIFENKTD-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI--LRDSAGN--VKLGDFGASKRL 545
Cdd:cd14195  83 VVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImlLDKNVPNprIKLIDFGIAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QticmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIaTQPTNPQLPSH 622
Cdd:cd14195 163 E----AGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFlgeTKQETLTNISAV-NYDFDEEYFSN 237
                       250       260
                ....*....|....*....|....*....
gi 42794767 623 ISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14195 238 TSELAKDFIRRLLVkDPKKRMTIAQSLEH 266
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
397-652 9.87e-28

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: 113.01  E-value: 9.87e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSKEvsalEC----EIQLLKNLQ-HERIVQYYGCLRDRaeKTLT 471
Cdd:cd07830   5 KQLGDGTFGSVYLARNKETGELVAIKKMK----KKFYSWE----ECmnlrEVKSLRKLNeHPNIVKLKEVFREN--DELY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPG---GSVKDQlkAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqti 548
Cdd:cd07830  75 FVFEYMEGnlyQLMKDR--KGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cmsgtGMRSV-TGTPY----WM-SPEVI--SGEgYGRKADVWSLGCTVVEMLTEKP------------------------ 596
Cdd:cd07830 148 -----EIRSRpPYTDYvstrWYrAPEILlrSTS-YSSPVDIWALGCIMAELYTLRPlfpgsseidqlykicsvlgtptkq 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 597 PWAEYEAMAAIFKIATQPTNPQLPSHI----SEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07830 222 DWPEGYKLASKLGFRFPQFAPTSLHQLipnaSPEAIDLIKDMLRwDPKKRPTASQALQHPY 282
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
399-592 9.99e-28

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: 112.99  E-value: 9.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQ-VQFDPDSPETS-KEVSALECeiqllknLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKElIRFDEEAQRNFlKEVKVMRS-------LDHPNVLKFIGVLYK--DKKLNLITEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK-----RLQTICM 550
Cdd:cd14154  72 IPGGTLKDVLKDMARPLPWAQRvRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARliveeRLPSGNM 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 551 SGTGMRS------------VTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd14154 152 SPSETLRhlkspdrkkrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
398-649 1.05e-27

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: 112.60  E-value: 1.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVY-LCYDVDTGRELASKQVQ-----FDPDSPETSKEVSALECEIQLLK-NLQHERIVQYYGCLRDraEKTL 470
Cdd:cd08528   7 LLGSGAFGCVYkVRKKSNGQTLLALKEINmtnpaFGRTEQERDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLE--NDRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKA----YGALTESVTRKYTRQILEGMSYLH-SNMIVHRDIKGANILRDSAGNVKLGDFGASKRL 545
Cdd:cd08528  85 YIVMELIEGAPLGEHFSSlkekNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICmsgTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPqLPSHI-S 624
Cdd:cd08528 165 GPES---SKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEP-LPEGMyS 240
                       250       260
                ....*....|....*....|....*.
gi 42794767 625 EHGRDFLRR-IFVEARQRPSAEELLT 649
Cdd:cd08528 241 DDITFVIRScLTPDPEARPDIVEVSS 266
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
399-650 1.77e-27

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: 111.91  E-value: 1.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdsPETSKEVSALECEIQLLKNLQHERIVqyygCLRDRAE--KTLTIFMEY 476
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFI------PLRSSTRARAFQERDILARLSHRRLT----CLLDQFEtrKTLILILEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGASKRLQticmSGTG 554
Cdd:cd14107  80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTreDIKICDFGFAQEIT----PSEH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHGRDFLR 632
Cdd:cd14107 156 QFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPeiTHLSEDAKDFIK 235
                       250
                ....*....|....*....
gi 42794767 633 RIFVEARQ-RPSAEELLTH 650
Cdd:cd14107 236 RVLQPDPEkRPSASECLSH 254
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
398-650 2.17e-27

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: 111.81  E-value: 2.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALeceiqllKNLQHERIVQYYGCLRD------------- 464
Cdd:cd14047  13 LIGSGGFGQVFKAKHRIDGKTYAIKRVKLN--NEKAEREVKAL-------AKLDHPNIVRYNGCWDGfdydpetsssnss 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 -RAEKTLTIFMEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGa 541
Cdd:cd14047  84 rSKTKCLFIQMEFCEKGTLESWIekRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFG- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 skrLQTiCMSGTGMRSVT-GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLtekppWAEYEAMAAIfKIATQPTNPQLP 620
Cdd:cd14047 163 ---LVT-SLKNDGKRTKSkGTLSYMSPEQISSQDYGKEVDIYALGLILFELL-----HVCDSAFEKS-KFWTDLRNGILP 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 621 SHISEHGR---DFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14047 233 DIFDKRYKiekTIIKKMLsKKPEDRPNASEILRT 266
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
399-652 2.37e-27

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: 112.14  E-value: 2.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevSALEcEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMp 478
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPS--SALR-EICLLKELKHKNIVRLYDVLH--SDKKLTLVFEYC- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 ggsvkDQ-LKAY-----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmsG 552
Cdd:cd07839  82 -----DQdLKKYfdscnGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF------G 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTE-KP--PWAEYE-AMAAIFKIATQPTNPQLPS--- 621
Cdd:cd07839 151 IPVRCYSAevvTLWYRPPDVLFGaKLYSTSIDMWSAGCIFAELANAgRPlfPGNDVDdQLKRIFRLLGTPTEESWPGvsk 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794767 622 ---------------------HISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07839 231 lpdykpypmypattslvnvvpKLNSTGRDLLQNLLVcNPVQRISAEEALQHPY 283
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
399-597 2.46e-27

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: 111.60  E-value: 2.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYdVDTGRELASKQVqfDPDSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEKTLtIFmEYMP 478
Cdd:cd14066   1 IGSGGFGTVYKGV-LENGTVVAVKRL--NEMNCAASKKE--FLTELEMLGRLRHPNLVRLLGYCLESDEKLL-VY-EYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGA---LTESVTRKYTRQILEGMSYLHSNM---IVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcMSG 552
Cdd:cd14066  74 NGSLEDRLHCHKGsppLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPS-ESV 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd14066 153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPA 197
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
399-599 2.83e-27

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: 114.36  E-value: 2.83e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELA----SKQVQFDPDspetskEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFM 474
Cdd:cd05600  19 VGQGGYGSVFLARKKDTGEICAlkimKKKVLFKLN------EVNHVLTERDILTTTNSPWLVKLLYAFQDP--ENVYLAM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK----------- 543
Cdd:cd05600  91 EYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesm 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 544 --RLQ----------TICMSGTGMR-----------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA 599
Cdd:cd05600 171 kiRLEevkntaflelTAKERRNIYRamrkedqnyanSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS 249
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
396-652 3.01e-27

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 112.93  E-value: 3.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdspETSKEVSAL-----EC--------EIQLLKNLQHERIVQyygcL 462
Cdd:PTZ00024  14 GAHLGEGTYGKVEKAYDTLTGKIVAIKKVKII----EISNDVTKDrqlvgMCgihfttlrELKIMNEIKHENIMG----L 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  463 RDR--AEKTLTIFMEYMpGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:PTZ00024  86 VDVyvEGDFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  541 ASKRLQTICMSGTG-----------MRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKP--PWA-EYEAMA 605
Cdd:PTZ00024 165 LARRYGYPPYSDTLskdetmqrreeMTSKVVTLWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPlfPGEnEIDQLG 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767  606 AIFKIATQPTN---PQ---LPS-----------------HISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:PTZ00024 245 RIFELLGTPNEdnwPQakkLPLyteftprkpkdlktifpNASDDAIDLLQSLLkLNPLERISAKEALKHEY 315
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
397-652 3.04e-27

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: 112.79  E-value: 3.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQ-FDPDSPEtskEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd05601   7 NVIGRGHFGEVQVVKEKATGDIYAMKVLKkSETLAQE---EVSFFEEERDIMAKANSPWITKLQYAFQD--SENLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmSGTG 554
Cdd:cd05601  82 YHPGGDLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKL-----SSDK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 M---RSVTGTPYWMSPEVI------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH--I 623
Cdd:cd05601 157 TvtsKMPVGTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDpkV 236
                       250       260
                ....*....|....*....|....*....
gi 42794767 624 SEHGRDFLRRIFVEARQRPSAEELLTHHF 652
Cdd:cd05601 237 SESAVDLIKGLLTDAKERLGYEGLCCHPF 265
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
397-598 3.08e-27

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: 111.73  E-value: 3.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdpdspetSKEVSALECEIQ-------LLKNLQHERIVQYYGCLRDRaeKT 469
Cdd:cd05609   6 KLISNGAYGAVYLVRHRETRQRFAMKKI---------NKQNLILRNQIQqvfverdILTFAENPFVVSMYCSFETK--RH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK----RL 545
Cdd:cd05609  75 LCMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmSL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 546 QTICMSGT--------GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05609 155 TTNLYEGHiekdtrefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 215
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
399-650 3.50e-27

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: 111.52  E-value: 3.50e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEvSALECEIQLLKNLQHERIVQyygcLRDRAEKT--LTIFMEY 476
Cdd:cd14169  11 LGEGAFSEVVLAQERGSQRLVALKCI---PKKALRGKE-AMVENEIAVLRRINHENIVS----LEDIYESPthLYLAMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKrlqticMSGT 553
Cdd:cd14169  83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfedSKIMISDFGLSK------IEAQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVT-GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLpSHISEHGRD 629
Cdd:cd14169 157 GMLSTAcGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFydeNDSELFNQILKAEYEFDSPYW-DDISESAKD 235
                       250       260
                ....*....|....*....|..
gi 42794767 630 FLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14169 236 FIRHLLErDPEKRFTCEQALQH 257
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
397-652 3.90e-27

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: 112.25  E-value: 3.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEvsALeCEIQLLKNLQH------ERIVQYYGCLRDRAEktL 470
Cdd:cd14210  19 SVLGKGSFGQVVKCLDHKTGQLVAIKIIR---NKKRFHQQ--AL-VEVKILKHLNDndpddkHNIVRYKDSFIFRGH--L 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEyMPGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASkrlq 546
Cdd:cd14210  91 CIVFE-LLSINLYELLKSnnFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILlkQPSKSSIKVIDFGSS---- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 tiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPT-------- 615
Cdd:cd14210 166 --CFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPgenEEEQLACIMEVLGVPPkslidkas 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 616 ----------NPQLPshISEHGR---------------------DFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14210 244 rrkkffdsngKPRPT--TNSKGKkrrpgskslaqvlkcddpsflDFLKKCLRwDPSERMTPEEALQHPW 310
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
393-650 4.26e-27

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: 110.89  E-value: 4.26e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTGKEFALKII----DKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAE--LYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGaskrLQTI 548
Cdd:cd14184  77 VMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvceyPDGTKSLKLGDFG----LATV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cMSGTgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPS----HIS 624
Cdd:cd14184 153 -VEGP-LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGKLEFPSpywdNIT 230
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14184 231 DSAKELISHMLqVNVEARYTAEQILSH 257
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
394-652 4.61e-27

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: 111.95  E-value: 4.61e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIF 473
Cdd:cd05574   4 KKIKLLGKGDVGRVYLVRLKGTGKLFAMKVL--DKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASF---QTSTHLCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 -MEYMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT--- 547
Cdd:cd05574  79 vMDYCPGGELFRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVtpp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 -----------------------ICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAM 604
Cdd:cd05574 159 pvrkslrkgsrrssvksieketfVAEPSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 605 AAIFKIATQPTN-PQLPsHISEHGRDFLRRIFV-EARQR----PSAEELLTHHF 652
Cdd:cd05574 239 ETFSNILKKELTfPESP-PVSSEAKDLIRKLLVkDPSKRlgskRGASEIKRHPF 291
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
401-650 4.62e-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: 111.55  E-value: 4.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 401 QGAFGRVYLCYDVDTGRELASKQVQFDPdspetSKE---VSALEcEIQLLKNLQHERIVQyygcLR-----DRAEKtltI 472
Cdd:cd07843  15 EGTYGVVYRARDKKTGEIVALKKLKMEK-----EKEgfpITSLR-EINILLKLQHPNIVT----VKevvvgSNLDK---I 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 F--MEYMPGgSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd07843  82 YmvMEYVEH-DLKSLMETMkQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTgmrSVTGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--------------------P----WAEYEAM 604
Cdd:cd07843 161 KPYT---QLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPlfpgkseidqlnkifkllgtPtekiWPGFSEL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 605 AAI--FKIATQPTNpQLPSH-----ISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd07843 238 PGAkkKTFTKYPYN-QLRKKfpalsLSDNGFDLLNRLLtYDPAKRISAEDALKH 290
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
396-650 4.97e-27

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: 111.35  E-value: 4.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKevSALECEIQLLKNLQ-HERIVQYYGCLRDRaEKTLTIFm 474
Cdd:cd14090   7 GELLGEGAYASVQTCINLYTGKEYAVKIIE---KHPGHSR--SRVFREVETLHQCQgHPNILQLIEYFEDD-ERFYLVF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFG-ASKrlqtICM 550
Cdd:cd14090  80 EKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDlGSG----IKL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVT--------GTPYWMSPEVI---SGEG--YGRKADVWSLGCTVVEMLTEKPP----------WAEYEAMAA- 606
Cdd:cd14090 156 SSTSMTPVTtpelltpvGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPfygrcgedcgWDRGEACQDc 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 607 ---IFKiATQPTNPQLP----SHISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14090 236 qelLFH-SIQEGEYEFPekewSHISAEAKDLISHLLVrDASQRYTAEQVLQH 286
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
399-652 6.36e-27

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: 110.56  E-value: 6.36e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDV---DTGRELASKQ------VQFDPDSPETSKEVSALECEIQ--LLKNLqherivqYYGClrdRAE 467
Cdd:cd05583   2 LGTGAYGKVFLVRKVgghDAGKLYAMKVlkkatiVQKAKTAEHTMTERQVLEAVRQspFLVTL-------HYAF---QTD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqt 547
Cdd:cd05583  72 AKLHLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEF-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 icMSGTGMR--SVTGTPYWMSPEVISG--EGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiATQPTNPQLP 620
Cdd:cd05583 150 --LPGENDRaySFCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTvdgERNSQSEISK-RILKSHPPIP 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42794767 621 SHISEHGRDFLRRIFVEARQR------PSAEELLTHHF 652
Cdd:cd05583 227 KTFSAEAKDFILKLLEKDPKKrlgagpRGAHEIKEHPF 264
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
400-652 9.35e-27

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: 111.22  E-value: 9.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 400 GQGAFGRVYLCY--DVDTGRELASKQvqFDPDsPETSKEVSALEC-EIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEY 476
Cdd:cd07842   9 GRGTYGRVYKAKrkNGKDGKEYAIKK--FKGD-KEQYTGISQSACrEIALLRELKHENVVSLVEVFLEHADKSVYLLFDY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MP---GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGASKRLQTI 548
Cdd:cd07842  86 AEhdlWQIIKFHRQAKRvSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILvmgeGPERGVVKIGDLGLARLFNAP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPWA------------EYEAMAAIFKIATQPT 615
Cdd:cd07842 166 LKPLADLDPVVVTIWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTLEPIFKgreakikksnpfQRDQLERIFEVLGTPT 245
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 616 N------------PQLPSHISE--------------------HGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd07842 246 EkdwpdikkmpeyDTLKSDTKAstypnsllakwmhkhkkpdsQGFDLLRKLLeYDPTKRITAEEALEHPY 315
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
399-652 1.02e-26

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: 110.05  E-value: 1.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskEVSALEcEIQLLKNLQ-HERIVQYYGCLRDRAEKTLTIFMEYM 477
Cdd:cd07831   7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLE---QVNNLR-EIQALRRLSpHPNILRLIEVLFDRKTGRLALVFELM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGgSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFG-----ASKRLQTICMS 551
Cdd:cd07831  83 DM-NLYELIKGRkRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGscrgiYSKPPYTEYIS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 gtgmrsvtgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--PWA-EYEAMAAIFKIATQPT------------ 615
Cdd:cd07831 161 ---------TRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPlfPGTnELDQIAKIHDVLGTPDaevlkkfrksrh 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 616 -NPQLPS-----------HISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07831 232 mNYNFPSkkgtglrkllpNASAEGLDLLKKLLAyDPDERITAKQALRHPY 281
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
397-625 1.50e-26

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: 109.36  E-value: 1.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCydVDTGRELASKQVQFDPDSpETSKEVSALECEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFME 475
Cdd:cd14145  12 EIIGIGGFGKVYRA--IWIGDEVAVKAARHDPDE-DISQTIENVRQEAKLFAMLKHPNIIALRGvCLK---EPNLCLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIV---HRDIKGANIL------RDSAGN--VKLGDFGASKR 544
Cdd:cd14145  86 FARGGPLNRVLSG-KRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILilekveNGDLSNkiLKITDFGLARE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTicmsgTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHIS 624
Cdd:cd14145 165 WHR-----TTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLPIPSTCP 239

                .
gi 42794767 625 E 625
Cdd:cd14145 240 E 240
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
398-655 1.60e-26

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: 109.76  E-value: 1.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetsKEVSALECEIQLLKNLQH-ERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd06616  13 EIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDE----KEQKRLLMDLDVVMRSSDcPYIVKFYGALFR--EGDCWICMEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAY----GALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmS 551
Cdd:cd06616  87 MDISLDKFYKYVYevldSVIPEEILGKIAVATVKALNYLKEELkIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD---S 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYwMSPEVI----SGEGYGRKADVWSLGCTVVEMLTEKPPwaeYEAMAAIFKIATQPTN---PQL-PSHI 623
Cdd:cd06616 164 IAKTRDAGCRPY-MAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFP---YPKWNSVFDQLTQVVKgdpPILsNSEE 239
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 42794767 624 SEHGRDFLRriFV------EARQRPSAEELLTHHFAQL 655
Cdd:cd06616 240 REFSPSFVN--FVnlclikDESKRPKYKELLKHPFIKM 275
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
397-650 1.63e-26

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: 109.24  E-value: 1.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVIN-----KQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNE--IVLFMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQL--KAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQticmSG 552
Cdd:cd14190  83 VEGGELFERIvdEDY-HLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcvNRTGHQVKIIDFGLARRYN----PR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFkIATQPTNPQLPSHISEHGRD 629
Cdd:cd14190 158 EKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLgddDTETLNNVL-MGNWYFDEETFEHVSDEAKD 236
                       250       260
                ....*....|....*....|..
gi 42794767 630 FLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14190 237 FVSNLIIkERSARMSATQCLKH 258
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
399-598 1.78e-26

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: 109.77  E-value: 1.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMp 478
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKK--IALR-EIRMLKQLKHPNLVNLIEVFRRK--RKLHLVFEYC- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTgmrS 557
Cdd:cd07847  83 DHTVLNELEKNpRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYT---D 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42794767 558 VTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd07847 160 YVATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLW 201
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
397-650 2.09e-26

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: 109.75  E-value: 2.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdPDSPETSKEvSALECEIQLLKNLQHERIVqyygCLRDRAEKT--LTIFM 474
Cdd:cd14168  16 EVLGTGAFSEVVLAEERATGKLFAVKCI---PKKALKGKE-SSIENEIAVLRKIKHENIV----ALEDIYESPnhLYLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKrlqticMS 551
Cdd:cd14168  88 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyfsQDEESKIMISDFGLSK------ME 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTG--MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLpSHISEH 626
Cdd:cd14168 162 GKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFydeNDSKLFEQILKADYEFDSPYW-DDISDS 240
                       250       260
                ....*....|....*....|....*
gi 42794767 627 GRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14168 241 AKDFIRNLMeKDPNKRYTCEQALRH 265
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
399-592 2.15e-26

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: 108.89  E-value: 2.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQ-VQFDPDSPETS-KEVSALECeiqllknLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKElIRFDEETQRTFlKEVKVMRC-------LEHPNVLKFIGVLYK--DKRLNFITEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGM 555
Cdd:cd14221  72 IKGGTLRGIIKSMDSHYPWSQRvSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGL 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 556 RS-----------VTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd14221 152 RSlkkpdrkkrytVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
397-636 2.19e-26

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: 110.17  E-value: 2.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELA----SKQVQFDPDSPETS---KEVSALECeiqllknlQHERIVQYYGCLRdrAEKT 469
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAikalKKDVVLEDDDVECTmieRRVLALAS--------QHPFLTHLFCTFQ--TESH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTIC 549
Cdd:cd05592  71 LFFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCK--ENIY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGmRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiatqpTNPQLPSHISEH 626
Cdd:cd05592 149 GENKA-STFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHgedEDELFWSICN-----DTPHYPRWLTKE 222
                       250
                ....*....|
gi 42794767 627 GRDFLRRIFV 636
Cdd:cd05592 223 AASCLSLLLE 232
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
390-652 2.53e-26

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: 111.24  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCydvdtgRELASKQVQfdpdspeTSKEVSALEC-----------EIQLLKNLQHERIVQY 458
Cdd:cd05621  51 AEDYDVVKVIGRGAFGEVQLV------RHKASQKVY-------AMKLLSKFEMikrsdsaffweERDIMAFANSPWVVQL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 459 YGCLRDraEKTLTIFMEYMPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGD 538
Cdd:cd05621 118 FCAFQD--DKYLYMVMEYMPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLAD 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 539 FGASKRlqticMSGTGM---RSVTGTPYWMSPEVISGEG----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIA 611
Cdd:cd05621 195 FGTCMK-----MDETGMvhcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIM 269
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42794767 612 TQPTNPQLPS--HISEHGRDFLrRIFVEARQ----RPSAEELLTHHF 652
Cdd:cd05621 270 DHKNSLNFPDdvEISKHAKNLI-CAFLTDREvrlgRNGVEEIKQHPF 315
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
397-652 2.86e-26

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: 110.56  E-value: 2.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERI--VQYYGCLRDRaektLTIFM 474
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYAMKILK--KEVIIAKDEVAHTLTESRVLKNTRHPFLtsLKYSFQTKDR----LCFVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTG 554
Cdd:cd05593  95 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT---DAAT 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEyEAMAAIFKIATQpTNPQLPSHISEHGRDFLRRI 634
Cdd:cd05593 172 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILM-EDIKFPRTLSADAKSLLSGL 249
                       250       260
                ....*....|....*....|....
gi 42794767 635 FVEARQR------PSAEELLTHHF 652
Cdd:cd05593 250 LIKDPNKrlgggpDDAKEIMRHSF 273
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
398-652 2.92e-26

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: 109.39  E-value: 2.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECeiqLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYM 477
Cdd:cd06618  22 EIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDV---VLKSHDCPYIVKCYGYFI--TDSDVFICMELM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 pgGSVKDQLK--AYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLqTICMSGTg 554
Cdd:cd06618  97 --STCLDKLLkrIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISGRL-VDSKAKT- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 mRSvTGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWA----EYEAMAaifKIATQPTnPQLPSH--ISE 625
Cdd:cd06618 173 -RS-AGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRncktEFEVLT---KILNEEP-PSLPPNegFSP 246
                       250       260
                ....*....|....*....|....*...
gi 42794767 626 HGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd06618 247 DFCSFVDLCLTkDHRYRPKYRELLQHPF 274
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
397-650 3.30e-26

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: 108.54  E-value: 3.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVsalECEIQLLKNLQHERIVQYYGCLRdRAEKTLTIFMEY 476
Cdd:cd14172  10 QVLGLGVNGKVLECFHRRTGQKCALKLLY---DSPKARREV---EHHWRASGGPHIVHILDVYENMH-HGKRCLLIIMEC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKR------L 545
Cdd:cd14172  83 MEGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLytsKEKDAVLKLTDFGFAKEttvqnaL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMsgtgmrsvtgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEY--EAMAAIFKIATQPTNPQLP--- 620
Cdd:cd14172 163 QTPCY----------TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNtgQAISPGMKRRIRMGQYGFPnpe 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 621 -SHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14172 233 wAEVSEEAKQLIRHLLkTDPTERMTITQFMNH 264
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
399-617 3.90e-26

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: 108.60  E-value: 3.90e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIFMEY 476
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQ---DRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvKGKKCIVLVTEL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANI-LRDSAGNVKLGDFGaskrLQTICMSGT 553
Cdd:cd14030 110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIfITGPTGSVKIGDLG----LATLKRASF 185
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 554 GmRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP 617
Cdd:cd14030 186 A-KSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKP 247
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
391-650 3.97e-26

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: 108.68  E-value: 3.97e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 391 INWRRGKLLGQGAFGRVYLCYDV-DTGRELASKQV---QFDPDSPETSKEVSALEcEIQLLKNLQHERIVQyygcLRDRA 466
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYKAVPLrNTGKPVAIKVVrkaDLSSDNLKGSSRANILK-EVQIMKRLSHPNIVK----LLDFQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 E--KTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS-------------- 530
Cdd:cd14096  76 EsdEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkad 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 531 -------------------AGNVKLGDFGASKRL-----QTICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGC 586
Cdd:cd14096 156 ddetkvdegefipgvggggIGIVKLADFGLSKQVwdsntKTPC----------GTVGYTAPEVVKDERYSKKVDMWALGC 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 587 TVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14096 226 VLYTLLCGFPPFYDESIETLTEKISRGDYTFLSPwwDEISKSAKDLISHLLtVDPAKRYDIDEFLAH 292
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
399-650 4.24e-26

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: 108.66  E-value: 4.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLtIFmEYMP 478
Cdd:cd14086   9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLS---ARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYL-VF-DLVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASkrlqtICMSGTGM 555
Cdd:cd14086  84 GGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLlasKSKGAAVKLADFGLA-----IEVQGDQQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 R--SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP-WAE--YEAMAAIFKIATQPTNPQLPShISEHGRDF 630
Cdd:cd14086 159 AwfGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPfWDEdqHRLYAQIKAGAYDYPSPEWDT-VTPEAKDL 237
                       250       260
                ....*....|....*....|.
gi 42794767 631 LRRIF-VEARQRPSAEELLTH 650
Cdd:cd14086 238 INQMLtVNPAKRITAAEALKH 258
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
399-620 4.63e-26

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: 108.28  E-value: 4.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDS---PETSKEvsalecEIQLLKNLQHERIVqyygCLRD--RAEKTLTIF 473
Cdd:cd07861   8 IGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEegvPSTAIR------EISLLKELQHPNIV----CLEDvlMQENRLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVK--DQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticms 551
Cdd:cd07861  78 FEFLSMDLKKylDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF------ 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 552 GTGMRSVTG---TPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLP 620
Cdd:cd07861 152 GIPVRVYTHevvTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFhgdSEIDQLFRIFRILGTPTEDIWP 227
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
400-650 4.99e-26

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: 107.60  E-value: 4.99e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 400 GQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMPG 479
Cdd:cd14111  12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQ------EYEILKSLHHERIMALHEAYI--TPRYLVLIAEFCSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 480 GSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRsvT 559
Cdd:cd14111  84 KELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRR--T 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 560 GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP-QLPSHISEHGRDFLRRIF-VE 637
Cdd:cd14111 162 GTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAfKLYPNVSQSASLFLKKVLsSY 241
                       250
                ....*....|...
gi 42794767 638 ARQRPSAEELLTH 650
Cdd:cd14111 242 PWSRPTTKDCFAH 254
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
399-601 5.04e-26

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: 107.58  E-value: 5.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVsaleceiQLLKNLQHERIVQYYG-CLRDraeKTLTIFMEYM 477
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEV-------KLMRRLSHPNILRFIGvCVKD---NKLNFITEYV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN--VKLGDFGASkRLQTICMSGT 553
Cdd:cd14065  71 NGGTLEELLKsMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLvREANRGrnAVVADFGLA-REMPDEKTKK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 554 GMR----SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEY 601
Cdd:cd14065 150 PDRkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPADPDY 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-656 5.69e-26

N-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: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 109.24  E-value: 5.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDV---DTGRELASKQ------VQFDPDSPETSKEVSALEceiqllknlqHERIVQYYGCLRD--R 465
Cdd:cd05614   6 KVLGTGAYGKVFLVRKVsghDANKLYAMKVlrkaalVQKAKTVEHTRTERNVLE----------HVRQSPFLVTLHYafQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 AEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL 545
Cdd:cd05614  76 TDAKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTgmRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPW-------AEYEAMAAIFKIatqptNP 617
Cdd:cd05614 156 LTEEKERT--YSFCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFtlegeknTQSEVSRRILKC-----DP 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42794767 618 QLPSHISEHGRDFLRRIFVEARQR------PSAEELLTHHFAQLM 656
Cdd:cd05614 229 PFPSFIGPVARDLLQKLLCKDPKKrlgagpQGAQEIKEHPFFKGL 273
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
397-652 7.82e-26

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: 107.09  E-value: 7.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQV---QFDPDSPETSKEVSALECEIQLLKNLQ---HERIVQyygcLRDRAEKTL 470
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIfkeRILVDTWVRDRKLGTVPLEIHILDTLNkrsHPNIVK----LLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGS---VKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQt 547
Cdd:cd14004  82 FYYLVMEKHGSgmdLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIK- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 icmSGTgMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEY-EAMAAIFKIatqptnpqlPSHISE 625
Cdd:cd14004 161 ---SGP-FDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIeEILEADLRI---------PYAVSE 227
                       250       260
                ....*....|....*....|....*...
gi 42794767 626 HGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd14004 228 DLIDLISRMLNrDVGDRPTIEELLTDPW 255
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
399-601 1.36e-25

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: 106.78  E-value: 1.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL--CYDVDTGRE--LASKQVQFDPDSPETSKEvsaLECEIQLLKNLQHERIVQYYGCLRDrAEKTLTIFm 474
Cdd:cd05049  13 LGEGAFGKVFLgeCYNLEPEQDkmLVAVKTLKDASSPDARKD---FEREAELLTNLQHENIVKFYGVCTE-GDPLLMVF- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGA--------------LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd05049  88 EYMEHGDLNKFLRSHGPdaaflasedsapgeLTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFG 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 541 ASKRLQTI---CMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEY 601
Cdd:cd05049 168 MSRDIYSTdyyRVGGHTMLPIR----WMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQL 228
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
399-629 2.17e-25

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: 107.45  E-value: 2.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEI-KPAIRNQIIR---ELQVLHECNSPYIVGFYGAFYSDGE--ISICMEHMD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYL-HSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSGTGMR 556
Cdd:cd06650  87 GGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLiDSMANSFVGTR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SvtgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEA--MAAIF------KIATQPTNPQLPSH-ISEHG 627
Cdd:cd06650 167 S------YMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAkeLELMFgcqvegDAAETPPRPRTPGRpLSSYG 240

                ..
gi 42794767 628 RD 629
Cdd:cd06650 241 MD 242
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
397-652 2.30e-25

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: 107.36  E-value: 2.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQ-LLKNLQHERIVQYYGCLRDrAEKtLTIFME 475
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQ--KKTILKKKEQNHIMAERNvLLKNLKHPFLVGLHYSFQT-SEK-LYFVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtICMSGTGM 555
Cdd:cd05603  77 YVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFG-------LCKEGMEP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRDFL 631
Cdd:cd05603 150 EETTstfcGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPL--HLPGGKTVAACDLL 227
                       250       260
                ....*....|....*....|....*.
gi 42794767 632 RRIF-VEARQRPSAE----ELLTHHF 652
Cdd:cd05603 228 QGLLhKDQRRRLGAKadflEIKNHVF 253
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
397-650 2.77e-25

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: 105.45  E-value: 2.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd14665   6 KDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQR------EIINHRSLRHPNIVRFKEVILTPTH--LAIVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD--SAGNVKLGDFGASKrlQTICMSGTg 554
Cdd:cd14665  78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSK--SSVLHSQP- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 mRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQ--LPS--HISEHGRD 629
Cdd:cd14665 155 -KSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQysIPDyvHISPECRH 233
                       250       260
                ....*....|....*....|..
gi 42794767 630 FLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14665 234 LISRIFVaDPATRITIPEIRNH 255
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
396-650 2.84e-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: 106.45  E-value: 2.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDspetsKEVsaLECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFME 475
Cdd:cd14085   8 ESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVD-----KKI--VRTEIGVLLRLSHPNIIKLKEIFETPTE--ISLVLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFGASKRLQTICMsg 552
Cdd:cd14085  79 LVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVT-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 tgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFK-IATQPTNPQLP--SHISEHGRD 629
Cdd:cd14085 157 --MKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKrILNCDYDFVSPwwDDVSLNAKD 234
                       250       260
                ....*....|....*....|..
gi 42794767 630 FLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14085 235 LVKKLIVlDPKKRLTTQQALQH 256
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
396-652 3.27e-25

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: 105.25  E-value: 3.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSKEV--SALECEIQLLKNLQHERIVQYYGCLrDRAEKTLTIF 473
Cdd:cd14165   6 GINLGEGSYAKVKSAYSERLKCNVAIKII----DKKKAPDDFveKFLPRELEILARLNHKSIIKTYEIF-ETSDGKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcMSGT 553
Cdd:cd14165  81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRD-ENGR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVT--GTPYWMSPEVISGEGYG-RKADVWSLGCTVVEMLTEKPPWAEYEaMAAIFKIATQpTNPQLPS--HISEHGR 628
Cdd:cd14165 160 IVLSKTfcGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSN-VKKMLKIQKE-HRVRFPRskNLTSECK 237
                       250       260
                ....*....|....*....|....*
gi 42794767 629 DFLRR-IFVEARQRPSAEELLTHHF 652
Cdd:cd14165 238 DLIYRlLQPDVSQRLCIDEVLSHPW 262
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
399-653 3.99e-25

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: 105.89  E-value: 3.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDV-DTGRELASKQVQFDPDSP----ETSKEVSALeceiQLLKNLQHERIVQYYG-CLRDRA--EKTL 470
Cdd:cd07862   9 IGEGAYGKVFKARDLkNGGRFVALKRVRVQTGEEgmplSTIREVAVL----RHLETFEHPNVVRLFDvCTVSRTdrETKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYmpggsVKDQLKAY-------GALTESVtRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASk 543
Cdd:cd07862  85 TLVFEH-----VDQDLTTYldkvpepGVPTETI-KDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RLQTICMSGTgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKI---------- 610
Cdd:cd07862 158 RIYSFQMALT---SVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFrgsSDVDQLGKILDViglpgeedwp 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 611 ----------ATQPTNP--QLPSHISEHGRDFLRRIF-VEARQRPSAEELLTHHFA 653
Cdd:cd07862 235 rdvalprqafHSKSAQPieKFVTDIDELGKDLLLKCLtFNPAKRISAYSALSHPYF 290
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
399-650 4.65e-25

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: 104.70  E-value: 4.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSALECEIQLLKNLQHERIVQyygCLRDRAEKT-LTIFMEYM 477
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGKFFK-----AYSAKEKENIRQEISIMNCLHHPKLVQ---CVDAFEEKAnIVMVLEMV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRLQticmSGTG 554
Cdd:cd14191  82 SGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvNKTGTKIKLIDFGLARRLE----NAGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiATQPTNPQLPSHISEHGRDFL 631
Cdd:cd14191 158 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgdnDNETLANVTS-ATWDFDDEAFDEISDDAKDFI 236
                       250       260
                ....*....|....*....|
gi 42794767 632 RRIF-VEARQRPSAEELLTH 650
Cdd:cd14191 237 SNLLkKDMKARLTCTQCLQH 256
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
399-648 5.07e-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: 104.52  E-value: 5.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSaleceiqLLKNLQHERIVQYYG-CLRDraEKTLTIfMEYM 477
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVREIS-------LLQKLSHPNIVRYLGiCVKD--EKLHPI-LEYV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQL---------KAYGALTESVTRkytrqileGMSYLHSNMIVHRDIKGANILRDSAGNVK---LGDFGASKRL 545
Cdd:cd14156  71 SGGCLEELLareelplswREKVELACDISR--------GMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 qtICM---SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI---ATQPTNPQL 619
Cdd:cd14156 143 --GEMpanDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLdvqAFKEMVPGC 220
                       250       260
                ....*....|....*....|....*....
gi 42794767 620 PSHISEHGRDFLRrifVEARQRPSAEELL 648
Cdd:cd14156 221 PEPFLDLAASCCR---MDAFKRPSFAELL 246
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
399-652 5.58e-25

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: 104.92  E-value: 5.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSK---EVSALEcEIQLLKNLQHERIVqyygCLRDRAE-KT-LTIF 473
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKL----DKKRIKKkkgETMALN-EKIILEKVSSPFIV----SLAYAFEtKDkLCLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmS 551
Cdd:cd05577  72 LTLMNGGDLKYHIYNVGtrGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFK----G 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIA--TQPTNPQLPSHISEHGR 628
Cdd:cd05577 148 GKKIKGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKrrTLEMAVEYPDSFSPEAR 227
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 629 DFLRRIF---VEAR---QRPSAEELLTHHF 652
Cdd:cd05577 228 SLCEGLLqkdPERRlgcRGGSADEVKEHPF 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
472-598 6.01e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 109.50  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG---Askrlqti 548
Cdd:NF033483  84 IVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiarA------- 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 42794767  549 cMSGTGM---RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:NF033483 157 -LSSTTMtqtNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
393-650 6.28e-25

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: 104.30  E-value: 6.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEvSALECEIQLLKNLQHERIVQYYGCLrDRAEKTLTI 472
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIID-KSGGPEEFIQ-RFLPRELQIVERLDHKNIIHVYEML-ESADGKIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAgNVKLGDFGASKRL------- 545
Cdd:cd14163  79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLpkggrel 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 -QTICmsgtgmrsvtGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKiatQPTNPQLPSH- 622
Cdd:cd14163 158 sQTFC----------GSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQ---QQKGVSLPGHl 224
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 623 -ISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14163 225 gVSRTCQDLLKRLLePDMVLRPSIEEVSWH 254
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
399-649 6.78e-25

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: 105.16  E-value: 6.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPD--SPETS-KEVSaleceiqLLKNLQHERIVqyygCLRD--RAEKTLTIF 473
Cdd:cd07844   8 LGEGSYATVYKGRSKLTGQLVALKEIRLEHEegAPFTAiREAS-------LLKDLKHANIV----TLHDiiHTKKTLTLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMpggsVKDqLKAY-----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTI 548
Cdd:cd07844  77 FEYL----DTD-LKQYmddcgGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA-RAKSV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cMSGTGMRSVTgTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPW----AEYEAMAAIFKI------ATQPTNP 617
Cdd:cd07844 151 -PSKTYSNEVV-TLWYRPPDVLLGStEYSTSLDMWGVGCIFYEMATGRPLFpgstDVEDQLHKIFRVlgtpteETWPGVS 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42794767 618 QLPSHISEHGRDFLRRIFVEARQR----PSAEELLT 649
Cdd:cd07844 229 SNPEFKPYSFPFYPPRPLINHAPRldriPHGEELAL 264
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
397-641 7.18e-25

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: 106.16  E-value: 7.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKnLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd05619  11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLA-WEHPFLTHLFCTFQTK--ENLFFVMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtiCMSGTGMR 556
Cdd:cd05619  88 LNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE----NMLGDAKT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SV-TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQptNPQLPSHISEHGRDFLRRIF 635
Cdd:cd05619 164 STfCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMD--NPFYPRWLEKEAKDILVKLF 241

                ....*.
gi 42794767 636 VEARQR 641
Cdd:cd05619 242 VREPER 247
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
399-593 7.48e-25

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: 104.84  E-value: 7.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALEceIQLLKNLQHERIVQYYGC---LRDRAEKTLTIF-M 474
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLE--VQIMKKLNHPNVVSARDVppeLEKLSPNDLPLLaM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGS---VKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAGNV--KLGDFGASKRL--Q 546
Cdd:cd13989  79 EYCSGGDlrkVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRViyKLIDLGYAKELdqG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42794767 547 TICMsgtgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd13989 159 SLCT------SFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT 199
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
399-649 7.86e-25

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: 104.35  E-value: 7.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQV-QFDPDSpetsKEVSALEC-----EIQLLKNL-QHERIVQYYGCLRDraEKTLT 471
Cdd:cd13993   8 IGEGAYGVVYLAVDLRTGRKYAIKCLyKSGPNS----KDGNDFQKlpqlrEIDLHRRVsRHPNIITLHDVFET--EVAIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKA---YGALTESVTRKYTrQILEGMSYLHSNMIVHRDIKGANIL-RDSAGNVKLGDFGASkrlqt 547
Cdd:cd13993  82 IVLEYCPNGDLFEAITEnriYVGKTELIKNVFL-QLIDAVKHCHSLGIYHRDIKPENILlSQDEGTVKLCDFGLA----- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 iCMSGTGMRSVTGTPYWMSPEVI-----SGEGYG-RKADVWSLGCTVVEMLTEKPPWaeyeamaaifKIATQPTN----- 616
Cdd:cd13993 156 -TTEKISMDFGVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPW----------KIASESDPifydy 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42794767 617 ----PQLPSHISEHGRDF---LRRIF-VEARQRPSAEELLT 649
Cdd:cd13993 225 ylnsPNLFDVILPMSDDFynlLRQIFtVNPNNRILLPELQL 265
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
399-592 8.02e-25

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: 104.64  E-value: 8.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQ-VQFDPDSPETskevsaLECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEYM 477
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQKT------FLTEVKVMRSLDHPNVLKFIGVLYK--DKRLNLLTEFI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK-------------- 543
Cdd:cd14222  73 EGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRliveekkkpppdkp 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 544 --RLQTICMSGTGMR-SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd14222 153 ttKKRTLRKNDRKKRyTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
399-650 8.44e-25

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: 103.71  E-value: 8.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVsaleceiQLLKNLQHERIVQYYG-CLRDRAEKTLTifmEYM 477
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREV-------QLMNRLSHPNILRFMGvCVHQGQLHALT---EYI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAG-NVKLGDFGASKRLQTICMSGTG 554
Cdd:cd14155  71 NGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLikRDENGyTAVVGDFGLAEKIPDYSDGKEK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI---ATQPTNPQLPShisehgrDFL 631
Cdd:cd14155 151 L-AVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLdydAFQHMVGDCPP-------DFL 222
                       250       260
                ....*....|....*....|...
gi 42794767 632 RRIF----VEARQRPSAEELLTH 650
Cdd:cd14155 223 QLAFnccnMDPKSRPSFHDIVKT 245
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
396-652 9.18e-25

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 105.45  E-value: 9.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCydVDTGRELASKQVQFDPDSpetSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFME 475
Cdd:cd08216   7 GKCFKGGGVVHLAKH--KPTNTLVAVKKINLESDS---KEDLKFLQQEILTSRQLQHPNILPYVTSFVVDND--LYVVTP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDF-------GASKRLQ 546
Cdd:cd08216  80 LMAYGSCRDLLKTHfpEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLryaysmvKHGKRQR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TICMSGtgmRSVTGTPYWMSPEVI--SGEGYGRKADVWSLGCTVVE---------------MLTEK----PP-------W 598
Cdd:cd08216 160 VVHDFP---KSSEKNLPWLSPEVLqqNLLGYNEKSDIYSVGITACElangvvpfsdmpatqMLLEKvrgtTPqlldcstY 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 599 AEYE-AMAAIFKIATQPTNPQLPSHI------SEHGRDF----LRRifvEARQRPSAEELLTHHF 652
Cdd:cd08216 237 PLEEdSMSQSEDSSTEHPNNRDTRDIpyqrtfSEAFHQFvelcLQR---DPELRPSASQLLAHSF 298
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
396-643 1.08e-24

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: 104.18  E-value: 1.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKqVQFDPDSPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFME 475
Cdd:cd14117  11 GRPLGKGKFGNVYLAREKQSKFIVALK-VLFKSQIEKEGVE-HQLRREIEIQSHLRHPNILRLYNYFHDR--KRIYLILE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-----ASKRLQTICm 550
Cdd:cd14117  87 YAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGwsvhaPSLRRRTMC- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 sgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATqpTNPQLPSHISEHGRDF 630
Cdd:cd14117 166 ---------GTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVK--VDLKFPPFLSDGSRDL 234
                       250
                ....*....|...
gi 42794767 631 LRRIFveaRQRPS 643
Cdd:cd14117 235 ISKLL---RYHPS 244
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
397-650 1.17e-24

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: 103.70  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYygclrdrAEKTLT----- 471
Cdd:cd14662   6 KDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQR------EIINHRSLRHPNIIRF-------KEVVLTpthla 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS--AGNVKLGDFGASKrlQTIC 549
Cdd:cd14662  73 IVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGspAPRLKICDFGYSK--SSVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTgmRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQ--LPS--HIS 624
Cdd:cd14662 151 HSQP--KSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSVQykIPDyvRVS 228
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14662 229 QDCRHLLSRIFVaNPAKRITIPEIKNH 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
396-652 1.23e-24

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized 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: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 103.57  E-value: 1.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFME 475
Cdd:cd14088   6 GQVIKTEEFCEIFRAKDKTTGKLYTCKKFL----KRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKE--YFIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKrlqticMSG 552
Cdd:cd14088  80 LATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynRLKNSKIVISDFHLAK------LEN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAM-AAIF-KIATQPTNPQLP--SH 622
Cdd:cd14088 154 GLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddYENHdKNLFrKILAGDYEFDSPywDD 233
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 623 ISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14088 234 ISQAAKDLVTRLMeVEQDQRITAEEAISHEW 264
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
397-625 1.46e-24

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: 103.57  E-value: 1.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYlcYDVDTGRELASKQVQFDPDSpETSKEVSALECEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFME 475
Cdd:cd14147   9 EVIGIGGFGKVY--RGSWRGELVAVKAARQDPDE-DISVTAESVRQEARLFAMLAHPNIIALKAvCLE---EPNLCLVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLkAYGALTESVTRKYTRQILEGMSYLHSNMIV---HRDIKGANILRDSAG--------NVKLGDFGASKR 544
Cdd:cd14147  83 YAAGGPLSRAL-AGRRVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIenddmehkTLKITDFGLARE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTicmsgTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHIS 624
Cdd:cd14147 162 WHK-----TTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCP 236

                .
gi 42794767 625 E 625
Cdd:cd14147 237 E 237
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
397-652 2.23e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 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: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 105.48  E-value: 2.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd05626   7 KTLGIGAFGEVCLACKVDTHALYAMKTLR--KKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDK--DNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG---------------- 540
Cdd:cd05626  83 IPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGlctgfrwthnskyyqk 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ----------------------ASKRLQTICMSGTGM------RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd05626 163 gshirqdsmepsdlwddvsncrCGDRLKTLEQRATKQhqrclaHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEML 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 593 TEKPPWAEYEAMAAIFKIATQPTNPQLPSHI--SEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05626 243 VGQPPFLAPTPTETQLKVINWENTLHIPPQVklSPEAVDLITKLCCSAEERlgrNGADDIKAHPF 307
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
399-654 3.37e-24

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: 103.12  E-value: 3.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASK---------QVQFDPDSPETSKEVSALEC------------EIQLLKNLQHERIVQ 457
Cdd:cd14199  10 IGKGSYGVVKLAYNEDDNTYYAMKvlskkklmrQAGFPRRPPPRGARAAPEGCtqprgpiervyqEIAILKKLDHPNVVK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 458 YYGCLRDRAEKTLTIFMEYMPGGSVKDqLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLG 537
Cdd:cd14199  90 LVEVLDDPSEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 538 DFGASKRLQTicmSGTGMRSVTGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQP 614
Cdd:cd14199 169 DFGVSNEFEG---SDALLTNTVGTPAFMAPETLSETRkifSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQP 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42794767 615 TN-PQLPShISEHGRDFLRRIFVE-ARQRPSAEELLTHHFAQ 654
Cdd:cd14199 246 LEfPDQPD-ISDDLKDLLFRMLDKnPESRISVPEIKLHPWVT 286
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
396-650 3.74e-24

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: 101.93  E-value: 3.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpeTSKEVSALE---CEIQLLK---NLQHERIVQyygcLRDRAEKT 469
Cdd:cd14005   5 GDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVT--EWAMINGPVpvpLEIALLLkasKPGVPGVIR----LLDWYERP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 --LTIFMEYmPGGSVK--DQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFGASKR 544
Cdd:cd14005  79 dgFLLIMER-PEPCQDlfDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTicmsgTGMRSVTGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEamaaifKIATQptNPQLPSHI 623
Cdd:cd14005 158 LKD-----SVYTDFDGTRVYSPPEWIRhGRYHGRPATVWSLGILLYDMLCGDIPFENDE------QILRG--NVLFRPRL 224
                       250       260
                ....*....|....*....|....*...
gi 42794767 624 SEHGRDFLRRIFVE-ARQRPSAEELLTH 650
Cdd:cd14005 225 SKECCDLISRCLQFdPSKRPSLEQILSH 252
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
397-648 4.55e-24

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 106.11  E-value: 4.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQyygCLRDRAEK-------- 468
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQA---EVCCLLNCDFFSIVK---CHEDFAKKdprnpenv 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  469 -TLTIFMEYMPGG----SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:PTZ00283 112 lMIALVLDYANAGdlrqEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  544 rLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKIATQPTNPQLPSHI 623
Cdd:PTZ00283 192 -MYAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPF-DGENMEEVMHKTLAGRYDPLPPSI 269
                        250       260
                 ....*....|....*....|....*.
gi 42794767  624 SEHGRDFLRRIFV-EARQRPSAEELL 648
Cdd:PTZ00283 270 SPEMQEIVTALLSsDPKRRPSSSKLL 295
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
397-598 4.79e-24

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: 103.24  E-value: 4.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELA----SKQVQFDPDSPE---TSKEVSALECEIQLLknlqheriVQYYGCLR--DRae 467
Cdd:cd05587   2 MVLGKGSFGKVMLAERKGTDELYAikilKKDVIIQDDDVEctmVEKRVLALSGKPPFL--------TQLHSCFQtmDR-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 ktLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQT 547
Cdd:cd05587  72 --LYFVMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK--EG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42794767 548 IcMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05587 148 I-FGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
393-654 4.86e-24

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; 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 three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 101.85  E-value: 4.86e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpETSKEVSALEC--EIQLLKNL----QHE---RIVQYYgclr 463
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQ-QWSKLPGVNPVpnEVALLQSVgggpGHRgviRLLDWF---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 464 DRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS-AGNVKLGDFGAS 542
Cdd:cd14101  77 EIPEGFLLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFGSG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 KRLQTICMSgtgmrSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAifkiatqpTNPQLPS 621
Cdd:cd14101 157 ATLKDSMYT-----DFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDTDILK--------AKPSFNK 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 622 HISEHGRDFLRR-IFVEARQRPSAEELLTHHFAQ 654
Cdd:cd14101 224 RVSNDCRSLIRScLAYNPSDRPSLEQILLHPWMM 257
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
392-654 6.09e-24

N-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: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 102.39  E-value: 6.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDV---DTGRELASKQVQfDPDSPETSKEVSALECEIQLLKNLQHER--IVQYYGClrdRA 466
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVsghDAGKLYAMKVLK-KATIVQKAKTAEHTRTERQVLEHIRQSPflVTLHYAF---QT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLq 546
Cdd:cd05613  77 DTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 tICMSGTGMRSVTGTPYWMSPEVISG--EGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPS 621
Cdd:cd05613 156 -LLDENERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILK-SEPPYPQ 233
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 622 HISEHGRDFLRRIFVEARQR-----PS-AEELLTHHFAQ 654
Cdd:cd05613 234 EMSALAKDIIQRLLMKDPKKrlgcgPNgADEIKKHPFFQ 272
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
383-641 8.27e-24

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: 103.17  E-value: 8.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 383 PTKSPSapiNWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQ-LLKNLQHERIVQYYGC 461
Cdd:cd05602   2 PHAKPS---DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQ--KKAILKKKEEKHIMSERNvLLKNVKHPFLVGLHFS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 462 LRDRAEktLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd05602  77 FQTTDK--LYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 SKrlQTICMSGTgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPS 621
Cdd:cd05602 155 CK--ENIEPNGT-TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPL--QLKP 229
                       250       260
                ....*....|....*....|
gi 42794767 622 HISEHGRDFLRRIFVEARQR 641
Cdd:cd05602 230 NITNSARHLLEGLLQKDRTK 249
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
393-650 8.32e-24

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: 101.22  E-value: 8.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 472
Cdd:cd14183   8 YKVGRTIGDGNFAVVKECVERSTGREYALKIIN---KSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTE--LYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGaskrLQTI 548
Cdd:cd14183  82 VMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLvyehQDGSKSLKLGDFG----LATV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cMSGTgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYEAMAAIF-KIATQPTNPQLP--SHIS 624
Cdd:cd14183 158 -VDGP-LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrGSGDDQEVLFdQILMGQVDFPSPywDNVS 235
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14183 236 DSAKELITMMLqVDVDQRYSALQVLEH 262
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
397-598 1.03e-23

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: 102.38  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlQHERIVQYYGCLR--DRaektLTIFM 474
Cdd:cd05616   6 MVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQtmDR----LYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTIcMSGTG 554
Cdd:cd05616  81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK--ENI-WDGVT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05616 158 TKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
397-652 1.10e-23

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: 103.94  E-value: 1.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSK--EVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 474
Cdd:cd05624  78 KVIGRGAFGEVAVVKMKNTERIYAMKIL----NKWEMLKraETACFREERNVLVNGDCQWITTLHYAFQD--ENYLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 553
Cdd:cd05624 152 DYYVGGDLLTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMND---DGT 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVT-GTPYWMSPEVIS----GEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHI---S 624
Cdd:cd05624 229 VQSSVAvGTPDYISPEILQamedGMGkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVtdvS 308
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 625 EHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05624 309 EEAKDLIQRLICSRERRlgqNGIEDFKKHAF 339
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
399-607 1.13e-23

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: 101.20  E-value: 1.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL--CYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDrAEKTLTIFmEY 476
Cdd:cd05092  13 LGEGAFGKVFLaeCHNLLPEQDKMLVAVKALKEATESARQ--DFQREAELLTVLQHQHIVRFYGVCTE-GEPLIMVF-EY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSV---------------KDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd05092  89 MRHGDLnrflrshgpdakildGGEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGM 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 542 SKRLQTICMSGTGMRsvTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAMAAI 607
Cdd:cd05092 169 SRDIYSTDYYRVGGR--TMLPIrWMPPESILYRKFTTESDIWSFGVVLWEIFTYgKQPWYQLSNTEAI 234
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
399-598 1.24e-23

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: 100.41  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTgRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMP 478
Cdd:cd05112  12 IGSGQFGLVHLGYWLNK-DKVAIKTIREGAMSEEDFIE------EAEVMMKLSHPKLVQLYGVCLEQA--PICLVFEFME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqtiCMSGTGMRS 557
Cdd:cd05112  83 HGCLSDYLRTQrGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR-----FVLDDQYTS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 558 VTGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPW 598
Cdd:cd05112 158 STGTKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEgKIPY 202
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
397-652 1.53e-23

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. 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 NDR1 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: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 102.81  E-value: 1.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPEtSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 476
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTGHVYAMKILR-KADMLE-KEQVGHIRAERDILVEADSLWVVKMFYSFQDKL--NLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS-------------- 542
Cdd:cd05628  83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCtglkkahrtefyrn 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 -----------KRLQTICMSGTGMR-------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAM 604
Cdd:cd05628 163 lnhslpsdftfQNMNSKRKAETWKRnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQ 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 605 AAIFKI----ATQPTNPQLPshISEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05628 243 ETYKKVmnwkETLIFPPEVP--ISEKAKDLILRFCCEWEHRigaPGVEEIKTNPF 295
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
397-652 1.57e-23

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. 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 NDR2 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: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 102.83  E-value: 1.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPEtSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd05627   8 KVIGRGAFGEVRLVQKKDTGHIYAMKILR-KADMLE-KEQVAHIRAERDILVEADGAWVVKMFYSFQDK--RNLYLIMEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC------- 549
Cdd:cd05627  84 LPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHrtefyrn 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 --------MSGTGMR-----------------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAM 604
Cdd:cd05627 164 lthnppsdFSFQNMNskrkaetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQ 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 605 AAIFKI----ATQPTNPQLPshISEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05627 244 ETYRKVmnwkETLVFPPEVP--ISEKAKDLILRFCTDAENRigsNGVEEIKSHPF 296
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
399-597 1.68e-23

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: 101.99  E-value: 1.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdspetsK-------EVSALECE---IQLLKNLQHERIVQYYGCLRdrAEK 468
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKALK---------KgdiiardEVESLMCEkriFETVNSARHPFLVNLFACFQ--TPE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtI 548
Cdd:cd05589  76 HVCFVMEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFG-------L 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794767 549 CMSGTGM--RSVT--GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd05589 148 CKEGMGFgdRTSTfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESP 200
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
399-623 1.76e-23

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: 101.42  E-value: 1.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpdspeTSKE---VSALEcEIQLLKNLQHERIVQYYGCLRDRAEKT------ 469
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGELVALKKVRLD-----NEKEgfpITAIR-EIKILRQLNHRSVVNLKEIVTDKQDALdfkkdk 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 --LTIFMEYMPG---GSVKDQLKAYgalTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkR 544
Cdd:cd07864  89 gaFYLVFEYMDHdlmGLLESGLVHF---SEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLA-R 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LqticMSGTGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNP 617
Cdd:cd07864 165 L----YNSEESRPYTNkviTLWYRPPELLLGeERYGPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRLCGSPCPA 240

                ....*.
gi 42794767 618 QLPSHI 623
Cdd:cd07864 241 VWPDVI 246
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
398-598 2.66e-23

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: 101.61  E-value: 2.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlQHERIVQYYGCLR--DRaektLTIFME 475
Cdd:cd05615  17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQD-KPPFLTQLHSCFQtvDR----LYFVME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticMSGTGM 555
Cdd:cd05615  92 YVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHM---VEGVTT 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05615 169 RTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPF 211
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
398-657 3.77e-23

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: 100.84  E-value: 3.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQ-FDpdspetsKEVSALEC--EIQLLKNLQHERIVQYYGCLRDRAEKTLT--- 471
Cdd:cd07849  12 YIGEGAYGMVCSAVHKPTGQKVAIKKISpFE-------HQTYCLRTlrEIKILLRFKHENIIGILDIQRPPTFESFKdvy 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGG---SVKDQlkaygALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTI 548
Cdd:cd07849  85 IVQELMETDlykLIKTQ-----HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLA-RIADP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTG-MRSVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQPTNPQLPSHI 623
Cdd:cd07849 159 EHDHTGfLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPlfPGKDYlHQLNLILGILGTPSQEDLNCII 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 624 SEHGRDFLR-----------RIFVEA----------------RQRPSAEELLTHHFAQLMY 657
Cdd:cd07849 239 SLKARNYIKslpfkpkvpwnKLFPNAdpkaldlldkmltfnpHKRITVEEALAHPYLEQYH 299
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
399-602 4.27e-23

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: 100.26  E-value: 4.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQvqFDPDSPETSKEVSALECEIqlLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMP 478
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKV--FNNLSFMRPLDVQMREFEV--LKKLNHKNIVKLFAIEEELTTRHKVLVMELCP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLK----AYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR----DSAGNVKLGDFGASKRLqticM 550
Cdd:cd13988  77 CGSLYTVLEepsnAYG-LPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAAREL----E 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVI--------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd13988 152 DDEQFVSLYGTEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPFRPFE 211
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
397-652 4.30e-23

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: 102.01  E-value: 4.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlqHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd05622  79 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFAN--SPWVVQLFYAFQD--DRYLYMVMEY 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqticMSGTGM- 555
Cdd:cd05622 155 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMK-----MNKEGMv 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 --RSVTGTPYWMSPEVISGEG----YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHG 627
Cdd:cd05622 229 rcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPddNDISKEA 308
                       250       260
                ....*....|....*....|....*....
gi 42794767 628 RDFLrRIFVEARQ----RPSAEELLTHHF 652
Cdd:cd05622 309 KNLI-CAFLTDREvrlgRNGVEEIKRHLF 336
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
397-598 4.94e-23

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: 101.26  E-value: 4.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERI--VQYYGCLRDRaektLTIFM 474
Cdd:cd05594  31 KLLGKGTFGKVILVKEKATGRYYAMKILK--KEVIVAKDEVAHTLTENRVLQNSRHPFLtaLKYSFQTHDR----LCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLqtiCMSGT 553
Cdd:cd05594 105 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEG---IKDGA 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05594 182 TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 226
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
399-596 5.62e-23

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: 100.14  E-value: 5.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKE---VSALEcEIQLLKNLQHERIVQYYGCLRDRAEK------T 469
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKVLM-----ENEKEgfpITALR-EIKILQLLKHENVVNLIEICRTKATPynrykgS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEY----MPGGSVKDQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG----- 540
Cdd:cd07865  94 IYLVFEFcehdLAGLLSNKNVK----FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGlaraf 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 541 -ASKRLQTICMSGtgmRSVtgTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07865 170 sLAKNSQPNRYTN---RVV--TLWYRPPELLLGErDYGPPIDMWGAGCIMAEMWTRSP 222
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
397-593 6.27e-23

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: 98.81  E-value: 6.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYdVDTGRELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEY 476
Cdd:cd05067  13 ERLGAGQFGEVWMGY-YNGHTKVAIKSLK------QGSMSPDAFLAEANLMKQLQHQRLVRLYAVV---TQEPIYIITEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTR--KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd05067  83 MENGSLVDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED--NEYTA 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05067 161 REGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVT 199
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
397-652 6.51e-23

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: 100.11  E-value: 6.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSK--EVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 474
Cdd:cd05597   7 KVIGRGAFGEVAVVKLKSTEKVYAMKIL----NKWEMLKraETACFREERDVLVNGDRRWITKLHYAFQD--ENYLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 553
Cdd:cd05597  81 DYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLRE---DGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVT-GTPYWMSPEVI----SGEG-YGRKADVWSLGCTVVEML-TEKPPWAeyEAMAAIF-KIATQPTNPQLPSH--- 622
Cdd:cd05597 158 VQSSVAvGTPDYISPEILqameDGKGrYGPECDWWSLGVCMYEMLyGETPFYA--ESLVETYgKIMNHKEHFSFPDDedd 235
                       250       260       270
                ....*....|....*....|....*....|...
gi 42794767 623 ISEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05597 236 VSEEAKDLIRRLICSRERRlgqNGIDDFKKHPF 268
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
397-598 6.80e-23

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: 100.04  E-value: 6.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQ-LLKNLQHERIVQYYGCLRdrAEKTLTIFME 475
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQ--KKVILNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQ--TTDKLYFVLD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICMSGTGM 555
Cdd:cd05604  78 FVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCK--EGISNSDTTT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 556 rSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05604 156 -TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
397-602 7.12e-23

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: 99.98  E-value: 7.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlQHERIVQYYGCLR--DRaektLTIFM 474
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLAR-NHPFLTQLYCCFQtpDR----LFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICmSGTG 554
Cdd:cd05590  76 EFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK--EGIF-NGKT 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW-AEYE 602
Cdd:cd05590 153 TSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFeAENE 201
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
398-652 1.25e-22

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: 99.18  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSK-EVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEY 476
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIR---KAHIVSRsEVTHTLAERTVLAQVDCPFIVPLKFSFQ--SPEKLYLVLAF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK-------RLQTIC 549
Cdd:cd05585  76 INGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlnmkdddKTNTFC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 msgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnpQLPSHISEHGRD 629
Cdd:cd05585 156 ----------GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPL--RFPDGFDRDAKD 223
                       250       260
                ....*....|....*....|....*..
gi 42794767 630 FLRRIFVEA-RQR---PSAEELLTHHF 652
Cdd:cd05585 224 LLIGLLNRDpTKRlgyNGAQEIKNHPF 250
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
397-654 1.38e-22

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: 98.18  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETS--KEVSAL-ECeiQLLKNLQHerIVQYYgclrdRAEKTLTIF 473
Cdd:cd14174   8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRvfREVETLyQC--QGNKNILE--LIEFF-----EDDTRFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDF--GASKRLQTI 548
Cdd:cd14174  79 FEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILcesPDKVSPVKICDFdlGSGVKLNSA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVT--GTPYWMSPEVI-----SGEGYGRKADVWSLGCTVVEMLTEKPP----------WAEYEAMAA----I 607
Cdd:cd14174 159 CTPITTPELTTpcGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPfvghcgtdcgWDRGEVCRVcqnkL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 608 FKiATQPTNPQLP----SHISEHGRDFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd14174 239 FE-SIQEGKYEFPdkdwSHISSEAKDLISKLLVrDAKERLSAAQVLQHPWVQ 289
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
399-598 1.48e-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: 98.19  E-value: 1.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL--CYDVDTGRELASKQVQFDPDSPETSKevSALECEIQLLKNLQHERIVQYYG-CLRDraeKTLTIFME 475
Cdd:cd05093  13 LGEGAFGKVFLaeCYNLCPEQDKILVAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGvCVEG---DPLIMVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGA-------------LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 542
Cdd:cd05093  88 YMKHGDLNKFLRAHGPdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 543 KRLQTICMSGTGMRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPW 598
Cdd:cd05093 168 RDVYSTDYYRVGGHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPW 223
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
398-610 1.79e-22

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: 98.14  E-value: 1.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALEceIQLLKNLQHERIVQYYGCLRDRA---------EK 468
Cdd:cd07848   8 VVGEGAYGVVLKCRHKETKEIVAIKKFK-DSEENEEVKETTLRE--LKMLRTLKQENIVELKEAFRRRGklylvfeyvEK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLkaygaltesvtRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTi 548
Cdd:cd07848  85 NMLELLEEMPNGVPPEKV-----------RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSE- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794767 549 cMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI 610
Cdd:cd07848 153 -GSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTI 213
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
397-598 1.85e-22

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: 98.03  E-value: 1.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd05608   7 RVLGKGGFGEVSACQMRATGKLYACKKL--NKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTD--LCLVMTI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQL----KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSG 552
Cdd:cd05608  83 MNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKD---GQ 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 553 TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05608 160 TKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPF 205
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
399-649 1.97e-22

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: 97.21  E-value: 1.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDvdTGRELASKQvqFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAEktLTIFMEYM 477
Cdd:cd14064   1 IGSGSFGKVYKGRC--RNKIVAIKR--YRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGaCLDDPSQ--FAIVTQYV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLH--SNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd14064  75 SGGSLFSLLHEQKRVIDLQSKlIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQS--LDEDN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRR 633
Cdd:cd14064 153 MTKQPGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIRPPIGYSIPKPISSLLMR 232
                       250
                ....*....|....*..
gi 42794767 634 IF-VEARQRPSAEELLT 649
Cdd:cd14064 233 GWnAEPESRPSFVEIVA 249
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
394-597 1.98e-22

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: 97.81  E-value: 1.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSK---EVSALEcEIQLLKNLQHERIVQ--YYGCLRDRAEK 468
Cdd:cd05605   3 RQYRVLGKGGFGEVCACQVRATGKMYACKKLE----KKRIKKrkgEAMALN-EKQILEKVNSRFVVSlaYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIfmeyMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ 546
Cdd:cd05605  78 VLTI----MNGGDLKFHIYNMGnpGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42794767 547 ticmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd05605 154 ----EGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAP 200
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
399-650 2.43e-22

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: 96.89  E-value: 2.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 478
Cdd:cd14108  10 IGRGAFSYLRRVKEKSSDLSFAAKFI-----PVRAKKKTSARR-ELALLAELDHKSIVRFHDAFEKR--RVVIIVTELCH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN--VKLGDFGASKRLQticmSGTGMR 556
Cdd:cd14108  82 EELLERITKR-PTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELT----PNEPQY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAI--FKIATQPTNPQlpsHISEHGRDFL 631
Cdd:cd14108 157 CKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVgenDRTTLMNIrnYNVAFEESMFK---DLCREAKGFI 233
                       250
                ....*....|....*....
gi 42794767 632 RRIFVEARQRPSAEELLTH 650
Cdd:cd14108 234 IKVLVSDRLRPDAEETLEH 252
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
382-640 2.49e-22

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: 98.60  E-value: 2.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 382 VPTK-SPSAPInwrrgkllGQGAFGRVYLCYDVDTGRELASKQVQ--FDP--DSPETSKEvsaleceIQLLKNLQHERIV 456
Cdd:cd07858   3 VDTKyVPIKPI--------GRGAYGIVCSAKNSETNEKVAIKKIAnaFDNriDAKRTLRE-------IKLLRHLDHENVI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 457 QYYGCLR---DRAEKTLTIFMEYMpGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN 533
Cdd:cd07858  68 AIKDIMPpphREAFNDVYIVYELM-DTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 534 VKLGDFGASKrlqTICMSGTGMRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFK 609
Cdd:cd07858 147 LKICDFGLAR---TTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPlfPGKDYvHQLKLITE 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 610 IATQPTNPQLPSHISEHGRDFLRRIFVEARQ 640
Cdd:cd07858 224 LLGSPSEEDLGFIRNEKARRYIRSLPYTPRQ 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
395-650 3.11e-22

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: 97.76  E-value: 3.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpdspetSKEVSAlECEIQLLKNLQ-HERIVQYYGCLRDRAEktLTIF 473
Cdd:cd14092  10 REEALGDGSFSVCRKCVHKKTGQEFAVKIV---------SRRLDT-SREVQLLRLCQgHPNIVKLHEVFQDELH--TYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFG------ASKR 544
Cdd:cd14092  78 MELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDdaeIKIVDFGfarlkpENQP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTICMSgtgmrsvtgTPYwMSPEVI----SGEGYGRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAifKIATQPTNPQ 618
Cdd:cd14092 158 LKTPCFT---------LPY-AAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqsPSRNESAA--EIMKRIKSGD 225
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 619 LP------SHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14092 226 FSfdgeewKNVSSEAKSLIQGLLtVDPSKRLTMSELRNH 264
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
397-651 3.48e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 101.74  E-value: 3.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEY 476
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHKRTQEFFCWKAISY---RGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANQKLYILMEF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   477 MPGGSVKDQL----KAYGALTESVTRKYTRQILEGMSYLHS-------NMIVHRDIKGANILRDS-----------AGNV 534
Cdd:PTZ00266   96 CDAGDLSRNIqkcyKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgirhigkitaqANNL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767   535 ------KLGDFGASKRLQTICMSgtgmRSVTGTPYWMSPEVISGE--GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA 606
Cdd:PTZ00266  176 ngrpiaKIGDFGLSKNIGIESMA----HSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKANNFSQ 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 42794767   607 IfkIATQPTNPQLPSHISEHGRDFLRR--IFVEARQRPSAEELLTHH 651
Cdd:PTZ00266  252 L--ISELKRGPDLPIKGKSKELNILIKnlLNLSAKERPSALQCLGYQ 296
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
399-654 3.59e-22

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: 97.38  E-value: 3.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMp 478
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDNLVALKEIRLEH---EEGAPCTAIR-EVSLLKDLKHANIVTLHDIIH--TEKSLTLVFEYL- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRK-YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTICMSGTGMRS 557
Cdd:cd07873  83 DKDLKQYLDDCGNSINMHNVKlFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSIPTKTYSNEV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 558 VtgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQPTNPQLPSHISEH------- 626
Cdd:cd07873 162 V--TLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPlfPGSTVeEQLHFIFRILGTPTEETWPGILSNEefksyny 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42794767 627 ------------------GRDFLRRIF-VEARQRPSAEELLTHHFAQ 654
Cdd:cd07873 240 pkyradalhnhaprldsdGADLLSKLLqFEGRKRISAEEAMKHPYFH 286
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
399-654 4.21e-22

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: 97.93  E-value: 4.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQF-DPDSPEtskevSALEcEIQLLKNLQHERIVQYYGCLRDRAEK--------- 468
Cdd:cd07854  13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLtDPQSVK-----HALR-EIKIIRRLDHDNIVKVYEVLGPSGSDltedvgslt 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 ---TLTIFMEYMPG--GSVKDQlkayGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV-KLGDFGAS 542
Cdd:cd07854  87 elnSVYIVQEYMETdlANVLEQ----GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 kRLQTICMSGTGMRSVTGTPYWM-SPE-VISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiaTQPTNP 617
Cdd:cd07854 163 -RIVDPHYSHKGYLSEGLVTKWYrSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAgahELEQMQLILE--SVPVVR 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 618 Q---------LPSHISEHGR------------------DFLRRIFV-EARQRPSAEELLTHHFAQ 654
Cdd:cd07854 240 EedrnellnvIPSFVRNDGGeprrplrdllpgvnpealDFLEQILTfNPMDRLTAEEALMHPYMS 304
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
394-593 4.29e-22

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: 96.71  E-value: 4.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGR----ELASKqVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYG-CLrdraEK 468
Cdd:cd05057  10 EKGKVLGSGAFGTVYKGVWIPEGEkvkiPVAIK-VLREETGPKANEEILD---EAYVMASVDHPHLVRLLGiCL----SS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-- 545
Cdd:cd05057  82 QVQLITQLMPLGCLLDYVRNHrDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLdv 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 -QTICMSGTGMrsvtgTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05057 162 dEKEYHAEGGK-----VPIkWMALESIQYRIYTHKSDVWSYGVTVWELMT 206
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
397-635 4.37e-22

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: 97.47  E-value: 4.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDV---DTGRELASKQVQfdpdspETSKEV-----SALECEIqlLKNLQHERIVQYYGCLrdRAEK 468
Cdd:cd05582   1 KVLGQGSFGKVFLVRKItgpDAGTLYAMKVLK------KATLKVrdrvrTKMERDI--LADVNHPFIVKLHYAF--QTEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTI 548
Cdd:cd05582  71 KLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSK--ESI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiatqpTNPQLPSHISE 625
Cdd:cd05582 149 -DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQgkdRKETMTMILK-----AKLGMPQFLSP 222
                       250
                ....*....|
gi 42794767 626 HGRDFLRRIF 635
Cdd:cd05582 223 EAQSLLRALF 232
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
397-635 4.66e-22

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: 97.32  E-value: 4.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFD----PDSPETS---KEVSALECEIQLLKNLQherivqyygCLRDRAEKt 469
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDvvliDDDVECTmveKRVLALAWENPFLTHLY---------CTFQTKEH- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK------ 543
Cdd:cd05620  71 LFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKenvfgd 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 -RLQTICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIfkiatQPTNPQL 619
Cdd:cd05620 151 nRASTFC----------GTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHgddEDELFESI-----RVDTPHY 215
                       250
                ....*....|....*.
gi 42794767 620 PSHISEHGRDFLRRIF 635
Cdd:cd05620 216 PRWITKESKDILEKLF 231
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
396-598 4.91e-22

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: 95.98  E-value: 4.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYG-CLRDRAektLTIFM 474
Cdd:cd05059   9 LKELGSGQFGVVHL------GKWRGKIDVAIKMIKEGSMSEDDFIE-EAKVMMKLSHPKLVQLYGvCTKQRP---IFIVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL---QTICM 550
Cdd:cd05059  79 EYMANGCLLNYLRERrGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVlddEYTSS 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMrsvtgtPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPW 598
Cdd:cd05059 159 VGTKF------PVkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEgKMPY 202
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
399-620 4.95e-22

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 96.81  E-value: 4.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  399 LGQGAFGRVYLCYDVDTGRELASKQV---QFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFME 475
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETIALKKIrleQEDEGVPSTAIR------EISLLKEMQHGNIVRLQDVVH--SEKRLYLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  476 YMpGGSVKDQLKAYGALTES--VTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-VKLGDFGASKRLqticmsG 552
Cdd:PLN00009  82 YL-DLDLKKHMDSSPDFAKNprLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAF------G 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767  553 TGMRSVTG---TPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLP 620
Cdd:PLN00009 155 IPVRTFTHevvTLWYRAPEILLGsRHYSTPVDIWSVGCIFAEMVNQKPLFpgdSEIDELFKIFRILGTPNEETWP 229
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
397-650 6.24e-22

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: 95.66  E-value: 6.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPdspetskevsALECEIQLLKNLQHERIVQYYGCLRDRaEKTLTIFMEY 476
Cdd:cd14109  10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDP----------FLMREVDIHNSLDHPNIVQMHDAYDDE-KLAVTVIDNL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGS-VKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRdSAGNVKLGDFGASKRLQTICMSGtg 554
Cdd:cd14109  79 ASTIElVRDNLlPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTT-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 mrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQLpSHISEHGRDFL 631
Cdd:cd14109 156 --LIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLgdnDRETLTNVRSGKWSFDSSPL-GNISDDARDFI 232
                       250       260
                ....*....|....*....|
gi 42794767 632 RRIFVEA-RQRPSAEELLTH 650
Cdd:cd14109 233 KKLLVYIpESRLTVDEALNH 252
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
399-652 7.12e-22

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: 96.23  E-value: 7.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPD--SPETSKEvsalecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEY 476
Cdd:cd07871  13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEegAPCTAIR------EVSLLKNLKHANIVTLHDIIH--TERCLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGgSVKDQLKAYGALTESVTRK-YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTICMSGTGM 555
Cdd:cd07871  85 LDS-DLKQYLDNCGNLMSMHNVKiFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA-RAKSVPTKTYSN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVtgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQPTN--------------- 616
Cdd:cd07871 163 EVV--TLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPmfPGSTVkEELHLIFRLLGTPTEetwpgvtsneefrsy 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42794767 617 --PQ-LPSHISEH-------GRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07871 241 lfPQyRAQPLINHaprldtdGIDLLSSLLLyETKSRISAEAALRHSY 287
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
398-650 7.61e-22

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: 95.29  E-value: 7.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskevsALECEIQLLKNLQHERIVQYYGCLrDRAEKtLTIFMEYM 477
Cdd:cd14087   8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRE------VCESELNVLRRVRHTNIIQLIEVF-ETKER-VYMVMELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFG-ASKRLQTI-CMsg 552
Cdd:cd14087  80 TGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGlASTRKKGPnCL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 tgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI--ATQPTNPQLPSHISEHGRDF 630
Cdd:cd14087 158 --MKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQIlrAKYSYSGEPWPSVSNLAKDF 235
                       250       260
                ....*....|....*....|.
gi 42794767 631 LRRIF-VEARQRPSAEELLTH 650
Cdd:cd14087 236 IDRLLtVNPGERLSATQALKH 256
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
435-652 8.26e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.94  E-value: 8.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  435 KEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMPGG----SVKDQLKAYGALTESVTRKYTRQILEGMSY 510
Cdd:PTZ00267 107 RQAAYARSELHCLAACDHFGIVKHFDDFK--SDDKLLLIMEYGSGGdlnkQIKQRLKEHLPFQEYEVGLLFYQIVLALDE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  511 LHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVE 590
Cdd:PTZ00267 185 VHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQY-SDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYE 263
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767  591 MLTEKPPW---AEYEAMAAIFKIATQPtnpqLPSHISEHGRDFLRRIFVE-ARQRPSAEELLTHHF 652
Cdd:PTZ00267 264 LLTLHRPFkgpSQREIMQQVLYGKYDP----FPCPVSSGMKALLDPLLSKnPALRPTTQQLLHTEF 325
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
391-650 8.65e-22

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: 95.99  E-value: 8.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 391 INWRRGklLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSA-LECEiqllknlQHERIVQYYGCLRDR---- 465
Cdd:cd14171   8 VNWTQK--LGTGISGPVRVCVKKSTGERFALKILL---DRPKARTEVRLhMMCS-------GHPNIVQIYDVYANSvqfp 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 ----AEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN--VKLGD 538
Cdd:cd14171  76 gessPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLlKDNSEDapIKLCD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 539 FGASKrlqticMSGTGMRSVTGTPYWMSPEVISGEGYGRKA-----------------DVWSLGCTVVEMLTEKPP-WAE 600
Cdd:cd14171 156 FGFAK------VDQGDLMTPQFTPYYVAPQVLEAQRRHRKErsgiptsptpytydkscDMWSLGVIIYIMLCGYPPfYSE 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794767 601 YEA-----------MAAIFKIatqPTNPQlpSHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14171 230 HPSrtitkdmkrkiMTGSYEF---PEEEW--SQISEMAKDIVRKLLcVDPEERMTIEEVLHH 286
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
397-598 9.49e-22

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL 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: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 97.26  E-value: 9.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKE-VSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFME 475
Cdd:cd05610  10 KPISRGAFGKVYLGRKKNNSKLYAVKVVK---KADMINKNmVHQVQAERDALALSKSPFIVHLYYSLQ--SANNVYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL--QTICM--- 550
Cdd:cd05610  85 YLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTlnRELNMmdi 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 ------------------------SGTGMRSVT---------------------GTPYWMSPEVISGEGYGRKADVWSLG 585
Cdd:cd05610 165 lttpsmakpkndysrtpgqvlsliSSLGFNTPTpyrtpksvrrgaarvegerilGTPDYLAPELLLGKPHGPAVDWWALG 244
                       250
                ....*....|...
gi 42794767 586 CTVVEMLTEKPPW 598
Cdd:cd05610 245 VCLFEFLTGIPPF 257
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
443-629 1.14e-21

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: 96.66  E-value: 1.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 443 EIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYL-HSNMIVHRDI 521
Cdd:cd06649  53 ELQVLHECNSPYIVGFYGAFYSDGE--ISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDV 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 522 KGANILRDSAGNVKLGDFGASKRLqticmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEY 601
Cdd:cd06649 131 KPSNILVNSRGEIKLCDFGVSGQL-----IDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPP 205
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 602 EA--MAAIF-------------KIATQPTNPQLPshISEHGRD 629
Cdd:cd06649 206 DAkeLEAIFgrpvvdgeegephSISPRPRPPGRP--VSGHGMD 246
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
397-641 1.21e-21

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: 97.78  E-value: 1.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETSK--EVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 474
Cdd:cd05623  78 KVIGRGAFGEVAVVKLKNADKVFAMKIL----NKWEMLKraETACFREERDVLVNGDSQWITTLHYAFQD--DNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 553
Cdd:cd05623 152 DYYVGGDLLTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLME---DGT 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSV-TGTPYWMSPEVIS----GEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH---IS 624
Cdd:cd05623 229 VQSSVaVGTPDYISPEILQamedGKGkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQvtdVS 308
                       250
                ....*....|....*..
gi 42794767 625 EHGRDFLRRIFVEARQR 641
Cdd:cd05623 309 ENAKDLIRRLICSREHR 325
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
397-650 1.30e-21

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: 95.48  E-value: 1.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPEtskevSALECEIQLLKNLQHER----IVQYYgclrdRAEKTLTI 472
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSR-----SRVFREVEMLYQCQGHRnvleLIEFF-----EEEDKFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDF--GASKRLQT 547
Cdd:cd14173  78 VFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILcehPNQVSPVKICDFdlGSGIKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 IC--MSGTGMRSVTGTPYWMSPEVISGEG-----YGRKADVWSLGCTVVEMLTEKPP----------WAEYEAMAA---I 607
Cdd:cd14173 158 DCspISTPELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPfvgrcgsdcgWDRGEACPAcqnM 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 608 FKIATQPTNPQLP----SHISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd14173 238 LFESIQEGKYEFPekdwAHISCAAKDLISKLLVrDAKQRLSAAQVLQH 285
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
397-647 1.40e-21

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: 95.11  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYdVDTGRELASKQVQfdpdsPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd05072  13 KKLGAGQFGEVWMGY-YNNSTKVAVKTLK-----PGTMSVQAFLE-EANLMKTLQHDKLVRLYAVVTK--EEPIYIITEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK--AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd05072  84 MAKGSLLDFLKsdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIED--NEYTA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT----EKPPWAEYEAMAAIFKIATQPTNPQLPSHIsehgRDF 630
Cdd:cd05072 162 REGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTygkiPYPGMSNSDVMSALQRGYRMPRMENCPDEL----YDI 237
                       250
                ....*....|....*...
gi 42794767 631 LRRIFVE-ARQRPSAEEL 647
Cdd:cd05072 238 MKTCWKEkAEERPTFDYL 255
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
397-651 1.93e-21

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: 93.91  E-value: 1.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsaleceiQLLKNLQHERIVQYYGCLR-DRA---EKTLTI 472
Cdd:cd14050   7 SKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKR--------KLEEVERHEKLGEHPNCVRfIKAweeKGILYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMpGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAskrlqTICMSG 552
Cdd:cd14050  79 QTELC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL-----VVELDK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVT-GTPYWMSPEVISGEgYGRKADVWSLGCTVVEMLT------EKPPWaeyeamaaifkiaTQPTNPQLPSHISE 625
Cdd:cd14050 153 EDIHDAQeGDPRYMAPELLQGS-FTKAADIFSLGITILELACnlelpsGGDGW-------------HQLRQGYLPEEFTA 218
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 626 HGRDFLRRIFV-----EARQRPSAEELLTHH 651
Cdd:cd14050 219 GLSPELRSIIKlmmdpDPERRPTAEDLLALP 249
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
399-593 2.09e-21

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: 94.72  E-value: 2.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL-----CYDVDTGRELASKQVQFDPdspeTSKEVSALECEIQLLKNLQHERIVQYYGcLRDRAEKTLTIf 473
Cdd:cd05032  14 LGQGSFGMVYEglakgVVKGEPETRVAIKTVNENA----SMRERIEFLNEASVMKEFNCHHVVRLLG-VVSTGQPTLVV- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKA----------YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd05032  88 MELMAKGDLKSYLRSrrpeaennpgLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTR 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794767 544 RL---QTICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05032 168 DIyetDYYRKGGKGLLPVR----WMAPESLKDGVFTTKSDVWSFGVVLWEMAT 216
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
399-599 2.16e-21

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: 94.00  E-value: 2.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCY---DVdtgrelASKQVQFDPDSPETSKevsALECEIQLLKNLQHERIVQYYGCLRdraEKTLTIFME 475
Cdd:cd14062   1 IGSGSFGTVYKGRwhgDV------AVKKLNVTDPTPSQLQ---AFKNEVAVLRKTRHVNILLFMGYMT---KPQLAIVTQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrLQTICMSGTG 554
Cdd:cd14062  69 WCEGSSLYKHLHVLETKFEMLQLiDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT-VKTRWSGSQQ 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 555 MRSVTGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWA 599
Cdd:cd14062 148 FEQPTGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYS 195
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
397-593 3.90e-21

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: 93.12  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYlcYDVDTGR-ELASKQVQfdpdsPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFME 475
Cdd:cd05034   1 KKLGAGQFGEVW--MGVWNGTtKVAVKTLK-----PGTMSPEAFLQ-EAQIMKKLRHDKLVQLYAVCSDE--EPIYIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLK--AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT-ICMSG 552
Cdd:cd05034  71 LMSKGSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDdEYTAR 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 553 TGMRsvtgTPY-WMSPEVISgegYGR---KADVWSLGCTVVEMLT 593
Cdd:cd05034 151 EGAK----FPIkWTAPEAAL---YGRftiKSDVWSFGILLYEIVT 188
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
399-650 4.90e-21

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: 94.55  E-value: 4.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqFDP-----DSPETSKEVSALeceiQLLKNlqHERIVQYYGCLRdrAEKTLTIF 473
Cdd:cd07852  15 LGKGAYGIVWKAIDKKTGEVVALKKI-FDAfrnatDAQRTFREIMFL----QELND--HPNIIKLLNVIR--AENDKDIY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 M--EYMPGG--SVkdqLKAygALTESVTRKY-TRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd07852  86 LvfEYMETDlhAV---IRA--NILEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 --CMSGTGMRSVTGTPYWMSPEVISGEGYGRKA-DVWSLGCTVVEMLTEKP--------------------PWAE----- 600
Cdd:cd07852 161 eeDDENPVLTDYVATRWYRAPEILLGSTRYTKGvDMWSVGCILGEMLLGKPlfpgtstlnqlekiievigrPSAEdiesi 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 601 --YEAMAAIFKIAT--QPTNPQLPSHISEHGRDFLRRIFV-EARQRPSAEELLTH 650
Cdd:cd07852 241 qsPFAATMLESLPPsrPKSLDELFPKASPDALDLLKKLLVfNPNKRLTAEEALRH 295
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
397-650 5.08e-21

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: 93.95  E-value: 5.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVsalECEIQLLKNLQHERIVQYYGCLRdRAEKTLTIFMEY 476
Cdd:cd14170   8 QVLGLGINGKVLQIFNKRTQEKFALKMLQ---DCPKARREV---ELHWRASQCPHIVRIVDVYENLY-AGRKCLLIVMEC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA---GNVKLGDFGASKRLQTicms 551
Cdd:cd14170  81 LDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTS---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA-------IFKIATQPTNPQLpSHIS 624
Cdd:cd14170 157 HNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgmktrIRMGQYEFPNPEW-SEVS 235
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14170 236 EEVKMLIRNLLkTEPTQRMTITEFMNH 262
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
372-610 6.56e-21

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 94.28  E-value: 6.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  372 ENALSVQERNVPTKSPSAPINWRRgkLLGQGAFGRVYLC-YDVDTGRELASKQvqFDPDSPETSKEVSALECEIQLLKNL 450
Cdd:PTZ00426  13 KDSDSTKEPKRKNKMKYEDFNFIR--TLGTGSFGRVILAtYKNEDFPPVAIKR--FEKSKIIKQKQVDHVFSERKILNYI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  451 QHERIVQYYGCLRDraEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS 530
Cdd:PTZ00426  89 NHPFCVNLYGSFKD--ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  531 AGNVKLGDFGASK----RLQTICmsgtgmrsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA 606
Cdd:PTZ00426 167 DGFIKMTDFGFAKvvdtRTYTLC----------GTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLI 236

                 ....
gi 42794767  607 IFKI 610
Cdd:PTZ00426 237 YQKI 240
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
399-650 7.32e-21

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: 93.00  E-value: 7.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdspETSKEVsALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 478
Cdd:cd14104   8 LGRGQFGIVHRCVETSSKKTYMAKFVKV-----KGADQV-LVKKEISILNIARHRNILRLHESFESHEE--LVMIFEFIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS--AGNVKLGDFGASKRLQticmSGTGM 555
Cdd:cd14104  80 GVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTrrGSYIKIIEFGQSRQLK----PGDKF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW--------------AEYEAMAAIFKiatqptnpqlps 621
Cdd:cd14104 156 RLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFeaetnqqtienirnAEYAFDDEAFK------------ 223
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 622 HISEHGRDFLRRIFVEARQ-RPSAEELLTH 650
Cdd:cd14104 224 NISIEALDFVDRLLVKERKsRMTAQEALNH 253
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
397-598 7.95e-21

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. 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-epsilon 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: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 93.71  E-value: 7.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNlQHERIVQYYGCL--RDRaektLTIFM 474
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAA-KHPFLTALHSCFqtKDR----LFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtICMSGT- 553
Cdd:cd05591  76 EYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFG-------MCKEGIl 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 554 -GMRSVT--GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05591 149 nGKTTTTfcGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPF 196
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
397-586 8.03e-21

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: 92.73  E-value: 8.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqFDPDSPEtskeVSALECEIQLLKNLQ-HERIVQYYG----CLRDRAEKTLt 471
Cdd:cd14037   9 KYLAEGGFAHVYLVKTSNGGNRAALKRV-YVNDEHD----LNVCKREIEIMKRLSgHKNIVGYIDssanRSGNGVYEVL- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHS--NMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 547
Cdd:cd14037  83 LLMEYCKGGGVIDLMnqRLQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSATTKIL 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 548 ICMSGTGMRSVT------GTPYWMSPEVI---SGEGYGRKADVWSLGC 586
Cdd:cd14037 163 PPQTKQGVTYVEedikkyTTLQYRAPEMIdlyRGKPITEKSDIWALGC 210
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
397-649 1.32e-20

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: 92.00  E-value: 1.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYlcydvdTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEY 476
Cdd:cd14150   6 KRIGTGSFGTVF------RGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFM---TRPNFAIITQW 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTGM 555
Cdd:cd14150  77 CEGSSLYRHLHVTETRFDTMQLiDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFG----LATVKTRWSGS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSV---TGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWAEYEAM-AAIFKIATQPTNPQLpSHISEHGR 628
Cdd:cd14150 153 QQVeqpSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNINNRdQIIFMVGRGYLSPDL-SKLSSNCP 231
                       250       260
                ....*....|....*....|....*.
gi 42794767 629 DFLRRIFVEA-----RQRPSAEELLT 649
Cdd:cd14150 232 KAMKRLLIDClkfkrEERPLFPQILV 257
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
399-593 1.43e-20

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: 91.73  E-value: 1.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYlcydvdTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAektLTIFMEYM 477
Cdd:cd05148  14 LGSGYFGEVW------EGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAvCSVGEP---VYIITELM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLK-AYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGtgm 555
Cdd:cd05148  85 EKGSLLAFLRsPEGqVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLS--- 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42794767 556 rSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05148 162 -SDKKIPYkWTAPEAASHGTFSTKSDVWSFGILLYEMFT 199
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
397-647 1.57e-20

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It 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 PFTAIRE-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: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 92.33  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPdspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd07870   6 EKLGEGSYATVYKGISRINGQLVALKVISMKT---EEGVPFTAIR-EASLLKGLKHANIVLLHDIIHTK--ETLTFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTgmr 556
Cdd:cd07870  80 MHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYS--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 557 SVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPWA-------EYEAMAAIFKIATQPTNP---QLPSHISE 625
Cdd:cd07870 157 SEVVTLWYRPPDVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPgvsdvfeQLEKIWTVLGVPTEDTWPgvsKLPNYKPE 236
                       250       260
                ....*....|....*....|....*.
gi 42794767 626 HGR----DFLRRIFVEARQRPSAEEL 647
Cdd:cd07870 237 WFLpckpQQLRVVWKRLSRPPKAEDL 262
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
399-648 2.04e-20

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: 91.80  E-value: 2.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdspeTSKEVSALEC-----EIQLLKNLQHERIVQYYGCLRDRAEKTLTIF 473
Cdd:cd14049  14 LGKGGYGKVYKVRNKLDGQYYAIKKI--------LIKKVTKRDCmkvlrEVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEyMPGGSVKDQL--------------KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAGNVKLGD 538
Cdd:cd14049  86 MQ-LCELSLWDWIvernkrpceeefksAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIfLHGSDIHVRIGD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 539 FG---------ASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLteKPPWAEYEAMAAIfk 609
Cdd:cd14049 165 FGlacpdilqdGNDSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF--QPFGTEMERAEVL-- 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42794767 610 iaTQPTNPQLPSHISEHGRDFLRRIFV----EARQRPSAEELL 648
Cdd:cd14049 241 --TQLRNGQIPKSLCKRWPVQAKYIKLltstEPSERPSASQLL 281
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
393-602 2.70e-20

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: 91.59  E-value: 2.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALEcEIQLLKNLQHERIVQ--YYGCLRDRAEKTL 470
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRKGEAMALN-EKRILEKVNSRFVVSlaYAYETKDALCLVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIfmeyMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTI 548
Cdd:cd05631  80 TI----MNGGDLKFHIYNMGnpGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLG----LAVQ 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 549 CMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd05631 152 IPEGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRK 205
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
396-610 3.02e-20

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: 90.94  E-value: 3.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRE---LASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDraeKTLTI 472
Cdd:cd05056  11 GRCIGEGQFGDVYQGVYMSPENEkiaVAVKTCKNCTSPSVREKFLQ----EAYIMRQFDHPHIVKLIGVITE---NPVWI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmS 551
Cdd:cd05056  84 VMELAPLGELRSYLQVNKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED---E 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 552 GTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAMAAIFKI 610
Cdd:cd05056 161 SYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMLgVKPFQGVKNNDVIGRI 221
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
399-596 3.11e-20

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: 92.25  E-value: 3.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVqyygCLRDRAEKTL--TIFMEY 476
Cdd:cd07856  18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYR---ELKLLKHLRHENII----SLSDIFISPLedIYFVTE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTICMSGtgmr 556
Cdd:cd07856  91 LLGTDLHRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA-RIQDPQMTG---- 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42794767 557 sVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07856 165 -YVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKP 204
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
399-598 3.12e-20

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: 91.23  E-value: 3.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL--CYDVDTGRELASKQVQFDPDSPETSKEvsALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd05094  13 LGEGAFGKVFLaeCYNLSPTKDKMLVAVKTLKDPTLAARK--DFQREAELLTNLQHDHIVKFYGVCGD--GDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGA----------------LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd05094  89 MKHGDLNKFLRAHGPdamilvdgqprqakgeLGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFG 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 541 ASKRLQTICMSGTGMRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPW 598
Cdd:cd05094 169 MSRDVYSTDYYRVGGHTMLPI-RWMPPESIMYRKFTTESDVWSFGVILWEIFTYgKQPW 226
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
397-610 3.32e-20

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: 90.48  E-value: 3.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLC-YDVDTGREL--ASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTif 473
Cdd:cd05040   1 EKLGDGSFGVVRRGeWTTPSGKVIqvAVKCLK--SDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVT-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 mEYMPGGSVKDQL-KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmsG 552
Cdd:cd05040  77 -ELAPLGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAL------P 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 553 TG-----MRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAMAAIFKI 610
Cdd:cd05040 150 QNedhyvMQEHRKVPFaWCAPESLKTRKFSHASDVWMFGVTLWEMFTYgEEPWLGLNGSQILEKI 214
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
397-652 3.36e-20

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: 92.24  E-value: 3.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevsaleCEIQLLKNLQHE------RIVQYYGCLRDRaeKTL 470
Cdd:cd14134  18 RLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAK------IEIDVLETLAEKdpngksHCVQLRDWFDYR--GHM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMpGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKlgdFGASKRLQTI 548
Cdd:cd14134  90 CIVFELL-GPSLYDFLKKnnYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVK---VYNPKKKRQI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMS-GTGMR---------------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT-----------------EK 595
Cdd:cd14134 166 RVPkSTDIKlidfgsatfddeyhsSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTgellfqthdnlehlammER 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 596 ----PP----------------------WAEYEAMAAIFKIATQPTNPQLPSHISEHGR--DFLRRIFV-EARQRPSAEE 646
Cdd:cd14134 246 ilgpLPkrmirrakkgakyfyfyhgrldWPEGSSSGRSIKRVCKPLKRLMLLVDPEHRLlfDLIRKMLEyDPSKRITAKE 325

                ....*.
gi 42794767 647 LLTHHF 652
Cdd:cd14134 326 ALKHPF 331
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
397-652 3.42e-20

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 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: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 93.19  E-value: 3.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 476
Cdd:cd05625   7 KTLGIGAFGEVCLARKVDTKALYATKTLR--KKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDK--DNLYFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA---------SKRLQT 547
Cdd:cd05625  83 IPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 -------------------ICMSGTGMR----------------SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd05625 163 gdhlrqdsmdfsnewgdpeNCRCGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEML 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 593 TEKPPWAEYEAMAAIFKIATQPTNPQLPSH--ISEHGRDFLRRIFVEARQR---PSAEELLTHHF 652
Cdd:cd05625 243 VGQPPFLAQTPLETQMKVINWQTSLHIPPQakLSPEASDLIIKLCRGPEDRlgkNGADEIKAHPF 307
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
393-650 3.43e-20

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; 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 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 90.41  E-value: 3.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDS-----PETSKevsaLECEIQLLKNLQHE-----RIVQYYgcl 462
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSewgelPNGTR----VPMEIVLLKKVGSGfrgviRLLDWF--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 463 rDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFGA 541
Cdd:cd14100  75 -ERPDSFVLVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 SKRLQTicmsgTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAM--AAIFkiatqptnpq 618
Cdd:cd14100 154 GALLKD-----TVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEEIirGQVF---------- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42794767 619 lpshisehgrdFLRRIFVEARQ------------RPSAEELLTH 650
Cdd:cd14100 219 -----------FRQRVSSECQHlikwclalrpsdRPSFEDIQNH 251
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
399-600 3.95e-20

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: 90.46  E-value: 3.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSkevsaleceiqlLKNLQHERIVQYYGCLRDRAEKTLTIF----- 473
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVP----KPSTK------------LKDFLREYNISLELSVHPHIIKTYDVAfeted 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 -----MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRlq 546
Cdd:cd13987  65 yyvfaQEYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLlfDKDCRRVKLCDFGLTRR-- 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 ticmSGTGMRSVTGT-PYwMSPEV---ISGEGY--GRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd13987 143 ----VGSTVKRVSGTiPY-TAPEVceaKKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWEK 197
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
397-602 4.02e-20

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: 91.12  E-value: 4.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIqlLKNLQHERIVQYYGCLRDRAEktLTIFMEY 476
Cdd:cd05607   8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEI--LEKVNSPFIVSLAYAFETKTH--LCLVMSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTR--KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSGTG 554
Cdd:cd05607  84 MNGGDLKYHIYNVGERGIEMERviFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK----EGKP 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 555 MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd05607 160 ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHK 207
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
399-650 4.49e-20

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: 90.02  E-value: 4.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPETSKEVSALEcEIQLLKNLQHERIVqyygCLRDRAEK--TLTIFMEY 476
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFV-----SKKMKKKEQAAH-EAALLQHLQHPQYI----TLHDTYESptSYILVLEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD---SAGNVKLGDFGASKRLqticmsgT 553
Cdd:cd14115  71 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQI-------S 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSV---TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTN--PQLPSHISEHGR 628
Cdd:cd14115 144 GHRHVhhlLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSfpDEYFGDVSQAAR 223
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIFVE-ARQRPSAEELLTH 650
Cdd:cd14115 224 DFINVILQEdPRRRPTAATCLQH 246
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
402-633 4.54e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 90.30  E-value: 4.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  402 GAFGRVYLCYDVDTGRELASKQVqfdpdspeTSKEVSALECEI-QLLKNLQHerIVQYYGCLRdrAEKTLTIFMEYMPGG 480
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKII--------KAKNFNAIEPMVhQLMKDNPN--FIKLYYSVT--TLKGHVLIMDYIKDG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  481 SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA-GNVKLGDFGASKRL-QTICMSGTgmrsv 558
Cdd:PHA03390  95 DLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYGLCKIIgTPSCYDGT----- 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767  559 tgTPYwMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEamAAIFKIAT----QPTNPQLPSHISEHGRDFLRR 633
Cdd:PHA03390 170 --LDY-FSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDE--DEELDLESllkrQQKKLPFIKNVSKNANDFVQS 243
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
393-598 5.56e-20

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: 91.19  E-value: 5.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTI 472
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLE-KKRIKKRKGESMALN-EKQILEKVNSQFVVNLAYAYETK--DALCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticm 550
Cdd:cd05632  80 VLTIMNGGDLKFHIYNMGnpGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIP---- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05632 156 EGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
393-600 7.44e-20

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: 90.08  E-value: 7.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfDPDSPETSKEVSALEcEIQLLKNLQHERIVQYygCLRDRAEKTLTI 472
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLE-KKRIKKRKGEAMALN-EKQILEKVNSRFVVSL--AYAYETKDALCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticm 550
Cdd:cd05630  78 VLTLMNGGDLKFHIYHMGqaGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP---- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd05630 154 EGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQ 203
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
398-644 7.58e-20

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: 89.98  E-value: 7.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLC-YDVD------------TGRELASKQVQFDPDSPETS-KEVSALECEIQLLKNLQHERIVQYYG-CL 462
Cdd:cd14000   1 LLGDGGFGSVYRAsYKGEpvavkifnkhtsSNFANVPADTMLRHLRATDAmKNFRLLRQELTVLSHLHHPSIVYLLGiGI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 463 RDRAektltIFMEYMPGGSVKDQLKAYG----ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-----RDSAGN 533
Cdd:cd14000  81 HPLM-----LVLELAPLGSLDHLLQQDSrsfaSLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtlyPNSAII 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 534 VKLGDFGASKrlQTICMsgtGMRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT 612
Cdd:cd14000 156 IKIADYGISR--QCCRM---GAKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 42794767 613 qptnpQLPSHISEHGRDFLRRIFV--------EARQRPSA 644
Cdd:cd14000 231 -----GLRPPLKQYECAPWPEVEVlmkkcwkeNPQQRPTA 265
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
399-652 8.06e-20

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: 91.27  E-value: 8.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVqyygCLRD--RAEKTLTIF--- 473
Cdd:cd07855  13 IGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLR---ELKILRHFKHDNII----AIRDilRPKVPYADFkdv 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 ---MEYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqtiCM 550
Cdd:cd07855  86 yvvLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMAR-----GL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTG------MRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQPTN---- 616
Cdd:cd07855 160 CTSPeehkyfMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQlfPGKNYvHQLQLILTVLGTPSQavin 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 617 -----------PQLPSH-----------ISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd07855 240 aigadrvrryiQNLPNKqpvpwetlypkADQQALDLLSQMLrFDPSERITVAEALQHPF 298
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
399-598 9.69e-20

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: 89.26  E-value: 9.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQyygcLRDRAE--KTLTIFMEY 476
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVN------KKLMKRDQVTHELGVLQSLQHPQLVG----LLDTFEtpTSYILVLEM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD---SAGNVKLGDFGASKRLQTICMsgt 553
Cdd:cd14113  85 ADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDAVQLNTTYY--- 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 554 gMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd14113 162 -IHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
390-634 1.07e-19

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: 90.78  E-value: 1.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVylCYDVD--TGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRdrAE 467
Cdd:cd07880  14 PDRYRDLKQVGSGAYGTV--CSALDrrTGAKVAIKKLYRPFQSELFAKRAYR---ELRLLKHMKHENVIGLLDVFT--PD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEY---MP-GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd07880  87 LSLDRFHDFylvMPfMGTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RlqticmSGTGMRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPTNPQL 619
Cdd:cd07880 167 Q------TDSEMTGYVVTRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKghdHLDQLMEIMKVTGTPSKEFV 240
                       250
                ....*....|....*
gi 42794767 620 PSHISEHGRDFLRRI 634
Cdd:cd07880 241 QKLQSEDAKNYVKKL 255
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
398-591 1.08e-19

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: 90.77  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEvSALECEIQLLKNLQHE--------RIVQYYGClrdraEKT 469
Cdd:cd14212   6 LLGQGTFGQVVKCQDLKTNKLVAVKVLK---NKPAYFRQ-AMLEIAILTLLNTKYDpedkhhivRLLDHFMH-----HGH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEyMPGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASkrl 545
Cdd:cd14212  77 LCIVFE-LLGVNLYELLKQnqFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILlvNLDSPEIKLIDFGSA--- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 546 qtiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEM 591
Cdd:cd14212 153 ---CFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAEL 195
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
397-641 1.11e-19

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: 91.25  E-value: 1.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdPDSPETSKEVSALECEIQLLKNLQ-HERIVQYYGCLRdrAEKTLTIFME 475
Cdd:cd05618  26 RVIGRGSYAKVLLVRLKKTERIYAMKVVK--KELVNDDEDIDWVQTEKHVFEQASnHPFLVGLHSCFQ--TESRLFFVIE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtICMSGTGM 555
Cdd:cd05618 102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYG-------MCKEGLRP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 556 RSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPwaeyeamaaiFKIATQPTNPqlpshiSEHGRDFL 631
Cdd:cd05618 175 GDTTstfcGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSP----------FDIVGSSDNP------DQNTEDYL 238
                       250
                ....*....|
gi 42794767 632 RRIFVEARQR 641
Cdd:cd05618 239 FQVILEKQIR 248
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
390-652 1.48e-19

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: 90.43  E-value: 1.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVqyygCLRD----- 464
Cdd:cd07851  14 PDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYR---ELRLLKHMKHENVI----GLLDvftpa 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 -RAEK-----TLTIFMEYMPGGSVKDQlkaygALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGD 538
Cdd:cd07851  87 sSLEDfqdvyLVTHLMGADLNNIVKCQ-----KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 539 FGASKrlqticMSGTGMRSVTGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQP 614
Cdd:cd07851 162 FGLAR------HTDDEMTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKTlfPGSDHiDQLKRIMNLVGTP 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 615 TNPQLPSHISEHGRDFLR-----------RIFVEA----------------RQRPSAEELLTHHF 652
Cdd:cd07851 236 DEELLKKISSESARNYIQslpqmpkkdfkEVFSGAnplaidllekmlvldpDKRITAAEALAHPY 300
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
399-598 2.05e-19

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: 88.71  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGReLASKQVQFDPdsPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYMP 478
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGL-VVLKTVYTGP--NCIEHNEALLE-EGKMMNRLRHSRVVKLLGVILEEGKYSLV--MEYME 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA-------------SKRL 545
Cdd:cd14027  75 KGNLMHVLKKV-SVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwskltkeeHNEQ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 546 QTIcmSGTGmRSVTGTPYWMSPE------VISGEgygrKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd14027 154 REV--DGTA-KKNAGTLYYMAPEhlndvnAKPTE----KSDVYSFAIVLWAIFANKEPY 205
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
397-590 2.28e-19

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: 88.63  E-value: 2.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYD-VDTGRELASKQVQFdPDSPETSKEVSALECEI-QLLKNLQHERIVQYYGCLRDRAEktLTIFM 474
Cdd:cd14052   6 ELIGSGEFSQVYKVSErVPTGKVYAVKKLKP-NYAGAKDRLRRLEEVSIlRELTLDGHDNIVQLIDSWEYHGH--LYIQT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcms 551
Cdd:cd14052  83 ELCENGSLDVFLSELGllgRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI--- 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42794767 552 gtGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVE 590
Cdd:cd14052 160 --RGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
396-585 2.44e-19

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: 88.18  E-value: 2.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLcyDVDTGRELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDraeKTLTIFM 474
Cdd:cd05039  11 GELIGKGEFGDVML--GDYRGQKVAVKCLK------DDSTAAQAFLAEASVMTTLRHPNLVQLLGvVLEG---NGLYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmsg 552
Cdd:cd05039  80 EYMAKGSLVDYLRSRGraVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS------ 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42794767 553 tgmRSVTGTPY---WMSPEVISGEGYGRKADVWSLG 585
Cdd:cd05039 154 ---SNQDGGKLpikWTAPEALREKKFSTKSDVWSFG 186
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
399-650 2.84e-19

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: 88.53  E-value: 2.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdspETSKEVSALECEIqLLKNLQHERIVQyygcLRDRAE--KTLTIFMEY 476
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKII-------DKSKRDPSEEIEI-LLRYGQHPNIIT----LKDVYDdgKFVYLVMEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN---VKLGDFGASKRLQticmSG 552
Cdd:cd14178  79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLR----AE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TG-MRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAIFKIATQPTNPQLPShISE 625
Cdd:cd14178 155 NGlLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpddtpEEILARIGSGKYALSGGNWDS-ISD 233
                       250       260
                ....*....|....*....|....*.
gi 42794767 626 HGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14178 234 AAKDIVSKMLhVDPHQRLTAPQVLRH 259
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
399-593 3.67e-19

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: 88.79  E-value: 3.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKevsaleCEIQLLK--------NLQHERIVQYYGCLRDRAEKTL 470
Cdd:cd14136  18 LGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAAL------DEIKLLKcvreadpkDPGREHVVQLLDDFKHTGPNGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFM--EYMpGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANILRdSAGN--VKLGDFGAS- 542
Cdd:cd14136  92 HVCMvfEVL-GPNLLKLIKRYNYrgIPLPLVKKIARQVLQGLDYLHTKCgIIHTDIKPENVLL-CISKieVKIADLGNAc 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 543 -------KRLQTicmsgtgmrsvtgTPYwMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd14136 170 wtdkhftEDIQT-------------RQY-RSPEVILGAGYGTPADIWSTACMAFELAT 213
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
399-647 3.71e-19

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: 88.21  E-value: 3.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEYMP 478
Cdd:cd05071  17 LGQGCFGEVWM------GTWNGTTRVAIKTLKPGTMSPEAFLQ-EAQVMKKLRHEKLVQLYAVV---SEEPIYIVTEYMS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKA----YGALTESVtrKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd05071  87 KGSLLDFLKGemgkYLRLPQLV--DMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIED--NEYTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISgegYGR---KADVWSLGCTVVEMLTEK----PPWAEYEAMAAIFKIATQPTNPQLPSHISEHG 627
Cdd:cd05071 163 RQGAKFPIKWTAPEAAL---YGRftiKSDVWSFGILLTELTTKGrvpyPGMVNREVLDQVERGYRMPCPPECPESLHDLM 239
                       250       260
                ....*....|....*....|
gi 42794767 628 RDFLRRifvEARQRPSAEEL 647
Cdd:cd05071 240 CQCWRK---EPEERPTFEYL 256
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
397-650 3.74e-19

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: 88.12  E-value: 3.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQV--QFDPDSPETSKEVSALeceiqllKNLQHERIVQYYG-CLRDRAEKTLTIF 473
Cdd:cd13986   6 RLLGEGGFSFVYLVEDLSTGRLYALKKIlcHSKEDVKEAMREIENY-------RLFNHPNILRLLDsQIVKEAGGKKEVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 M--EYMPGGSVKDQLKAYGA----LTESVTRKYTRQILEGMSYLHSNMIV---HRDIKGANILRDSAGNVKLGDFGaSKR 544
Cdd:cd13986  79 LllPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLG-SMN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTICMSGT--GMR-----SVTGTPYWMSPE---VISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYE-------AMAai 607
Cdd:cd13986 158 PARIEIEGRreALAlqdwaAEHCTMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF-ERIfqkgdslALA-- 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42794767 608 fkIATQPTNPQLPSHISEHGRDFLRR-IFVEARQRPSAEELLTH 650
Cdd:cd13986 235 --VLSGNYSFPDNSRYSEELHQLVKSmLVVNPAERPSIDDLLSR 276
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
397-647 3.99e-19

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: 87.28  E-value: 3.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEY 476
Cdd:cd14203   1 VKLGQGCFGEVWM------GTWNGTTKVAIKTLKPGTMSPEAFLE-EAQIMKKLRHDKLVQLYAVV---SEEPIYIVTEF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK----AYGALTESVtrKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSG 552
Cdd:cd14203  71 MSKGSLLDFLKdgegKYLKLPQLV--DMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED--NEY 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTGTPYWMSPEVISgegYGR---KADVWSLGCTVVEMLTEK----PPWAEYEAMAAIFKIATQPTNPQLPSHISE 625
Cdd:cd14203 147 TARQGAKFPIKWTAPEAAL---YGRftiKSDVWSFGILLTELVTKGrvpyPGMNNREVLEQVERGYRMPCPPGCPESLHE 223
                       250       260
                ....*....|....*....|..
gi 42794767 626 HGRDFLRRifvEARQRPSAEEL 647
Cdd:cd14203 224 LMCQCWRK---DPEERPTFEYL 242
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
401-597 4.46e-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: 87.28  E-value: 4.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 401 QGAFGRVYLCYDVDTGRELASKQVQFDPdspetsKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMPGG 480
Cdd:cd14110  13 RGRFSVVRQCEEKRSGQMLAAKIIPYKP------EDKQLVLREYQVLRRLSHPRIAQLHSAYL--SPRHLVLIEELCSGP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 481 SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL---QTICMSGTGMRS 557
Cdd:cd14110  85 ELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFnqgKVLMTDKKGDYV 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42794767 558 VTgtpywMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd14110 165 ET-----MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYP 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
399-593 4.96e-19

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: 87.11  E-value: 4.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDpDSPETSKEVsaLEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 478
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKF--LQ-EARILKQYDHPNIVKLIGVCVQK--QPIMIVMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT-ICMSGTGMR 556
Cdd:cd05041  77 GGSLLTFLRKKGArLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDgEYTVSDGLK 156
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42794767 557 SVtgtPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05041 157 QI---PIkWTAPEALNYGRYTSESDVWSFGILLWEIFS 191
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
443-652 5.81e-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: 5.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 443 EIQLL-KNLQHERIVQYYGclRDRAEKTLTIFMEYMPGgSVKD--QLKAYGALTESVTR---KYTRQILEGMSYLHSNMI 516
Cdd:cd13982  44 EVQLLrESDEHPNVIRYFC--TEKDRQFLYIALELCAA-SLQDlvESPRESKLFLRPGLepvRLLRQIASGLAHLHSLNI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 517 VHRDIKGANIL---RDSAGNVK--LGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGR---KADVWSLGCTV 588
Cdd:cd13982 121 VHRDLKPQNIListPNAHGNVRamISDFGLCKKLDVGRSSFSRRSGVAGTSGWIAPEMLSGSTKRRqtrAVDIFSLGCVF 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 589 VEMLT--EKPPWAEYEAMAAIFK-IATQPTNPQLPSHISEhGRDFLRR-IFVEARQRPSAEELLTHHF 652
Cdd:cd13982 201 YYVLSggSHPFGDKLEREANILKgKYSLDKLLSLGEHGPE-AQDLIERmIDFDPEKRPSAEEVLNHPF 267
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
399-596 5.82e-19

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: 87.02  E-value: 5.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYL-CYDVDTGREL--ASKQVQfDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYG-CLrdraEKTLTIFM 474
Cdd:cd05060   3 LGHGNFGSVRKgVYLMKSGKEVevAVKTLK-QEHEKAGKKEFLR---EASVMAQLDHPCIVRLIGvCK----GEPLMLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticmsGTG 554
Cdd:cd05060  75 ELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRAL------GAG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 ---MRSVTGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKP 596
Cdd:cd05060 149 sdyYRATTAGRWplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSygAKP 198
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
390-654 6.06e-19

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: 88.57  E-value: 6.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRA--E 467
Cdd:cd07878  14 PERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYR---ELRLLKHMKHENVIGLLDVFTPATsiE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqt 547
Cdd:cd07878  91 NFNEVYLVTNLMGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ--- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 548 icmSGTGMRSVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEKP--PWAEY-EAMAAIFKIATQPTNPQLPSHI 623
Cdd:cd07878 168 ---ADDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKAlfPGNDYiDQLKRIMEVVGTPSPEVLKKIS 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 624 SEHGR--------------------------DFLRRIFV-EARQRPSAEELLTH-HFAQ 654
Cdd:cd07878 245 SEHARkyiqslphmpqqdlkkifrganplaiDLLEKMLVlDSDKRISASEALAHpYFSQ 303
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
398-652 6.83e-19

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: 87.11  E-value: 6.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSK-EVSALEcEIQLLKNLQHERIVQYYGCLR---DRAEKtLTIF 473
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKCL--DKKRIKMKQgETLALN-ERIMLSLVSTGGDCPFIVCMTyafQTPDK-LCFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA----SKRLQTIC 549
Cdd:cd05606  77 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLacdfSKKKPHAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MsgtgmrsvtGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMA--AIFKIaTQPTNPQLPSHISEH 626
Cdd:cd05606 157 V---------GTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDkhEIDRM-TLTMNVELPDSFSPE 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 627 GRDFLRRIF---VEAR---QRPSAEELLTHHF 652
Cdd:cd05606 227 LKSLLEGLLqrdVSKRlgcLGRGATEVKEHPF 258
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
397-602 9.34e-19

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: 87.80  E-value: 9.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIFM 474
Cdd:cd14223   6 RIIGRGGFGEVYGCRKADTGKMYAMKCLD---KKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYafHTPDKLSFIL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqtiC-MSGT 553
Cdd:cd14223  83 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA------CdFSKK 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd14223 157 KPHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFRQHK 206
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
396-650 1.07e-18

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: 86.07  E-value: 1.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVsaLECEIQLLKNLQHERIVQYYGCLrDRAEKTLTIFME 475
Cdd:cd14164   5 GTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKF--LPRELSILRRVNHPNIVQMFECI-EVANGRLYIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 ympgGSVKDQLKAY---GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG-NVKLGDFGASKRlqticMS 551
Cdd:cd14164  82 ----AAATDLLQKIqevHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARF-----VE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVT--GTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWaeYEAMAAIFKIATQPTNPQLPSHISEHGR 628
Cdd:cd14164 153 DYPELSTTfcGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPF--DETNVRRLRLQQRGVLYPSGVALEEPCR 230
                       250       260
                ....*....|....*....|...
gi 42794767 629 DFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14164 231 ALIRTLLqFNPSTRPSIQQVAGN 253
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
390-654 1.42e-18

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: 87.40  E-value: 1.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIV---QYYGCLRDRA 466
Cdd:cd07877  16 PERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYR---ELRLLKHMKHENVIgllDVFTPARSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKTLTIFMEYMPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlq 546
Cdd:cd07877  93 EFNDVYLVTHLMGADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH-- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 ticmSGTGMRSVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEK---PPWAEYEAMAAIFKIATQPtNPQLPSH 622
Cdd:cd07877 170 ----TDDEMTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRtlfPGTDHIDQLKLILRLVGTP-GAELLKK 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 623 ISEHGR---------------------------DFLRRIFV-EARQRPSAEELLTH-HFAQ 654
Cdd:cd07877 245 ISSESArnyiqsltqmpkmnfanvfiganplavDLLEKMLVlDSDKRITAAQALAHaYFAQ 305
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
399-652 1.64e-18

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: 86.43  E-value: 1.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDS----PETSKEVSALEC---EIQLLKNLQHERIVQyygclrdRAEKTLT 471
Cdd:cd07837   9 IGEGTYGKVYKARDKNTGKLVALKKTRLEMEEegvpSTALREVSLLQMlsqSIYIVRLLDVEHVEE-------NGKPLLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMpGGSVKDQLKAYG-----ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV-KLGDFGASkRL 545
Cdd:cd07837  82 LVFEYL-DTDLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLG-RA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMRSVtgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQPTNPQLPS 621
Cdd:cd07837 160 FTIPIKSYTHEIV--TLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFpgdSELQQLLHIFRLLGTPNEEVWPG 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 622 -------HI----------------SEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07837 238 vsklrdwHEypqwkpqdlsravpdlEPEGVDLLTKMLAyDPAKRISAKAALQHPY 292
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
397-601 2.49e-18

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: 85.30  E-value: 2.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFME 475
Cdd:cd05114  10 KELGSGLFGVVRL------GKWRAQYKVAIKAIREGAMSEEDFIE-EAKVMMKLTHPKLVQLYGvCTQ---QKPIYIVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKA-YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR-LQTICMSGT 553
Cdd:cd05114  80 FMENGCLLNYLRQrRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYvLDDQYTSSS 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 554 GMRSVTGtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEY 601
Cdd:cd05114 160 GAKFPVK---WSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEgKMPFESK 205
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
397-593 2.50e-18

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: 85.46  E-value: 2.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLC-YDVDTgrELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFME 475
Cdd:cd05073  17 KKLGAGQFGEVWMAtYNKHT--KVAVKTMK------PGSMSVEAFLAEANVMKTLQHDKLVKLHAVV---TKEPIYIITE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTR--KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGT 553
Cdd:cd05073  86 FMAKGSLLDFLKSDEGSKQPLPKliDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED---NEY 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42794767 554 GMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05073 163 TAREGAKFPIkWTAPEAINFGSFTIKSDVWSFGILLMEIVT 203
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
399-591 2.84e-18

Catalytic domain of Suppressor of loss of cAMP-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 Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-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: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 86.47  E-value: 2.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdspetSKEVsaleceIQLLKNLQH---ERIVQYYGCLRD----------- 464
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVL---------SKKV------IVAKKEVAHtigERNILVRTALDEspfivglkfsf 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 RAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd05586  66 QTPTDLYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKA 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42794767 545 LQTicmSGTGMRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEM 591
Cdd:cd05586 146 DLT---DNKTTNTFCGTTEYLAPEVLLDEkGYTKMVDFWSLGVLVFEM 190
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
397-602 4.48e-18

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: 86.27  E-value: 4.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVqfdpDSPETS-KEVSALECEIQLLKNLQHERIVQYYGCLRD--RAEKTLTIF 473
Cdd:cd05633  11 RIIGRGGFGEVYGCRKADTGKMYAMKCL----DKKRIKmKQGETLALNERIMLSLVSTGDCPFIVCMTYafHTPDKLCFI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkrlqtiC-MSG 552
Cdd:cd05633  87 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA------CdFSK 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42794767 553 TGMRSVTGTPYWMSPEVIS-GEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd05633 161 KKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 211
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
370-597 4.84e-18

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 85.29  E-value: 4.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 370 DSENAlsvqerNVPTKSPSapiNWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdsPETSKEVSAlecEIQLLKN 449
Cdd:cd14132   6 DYENL------NVEWGSQD---DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLK-----PVKKKKIKR---EIKILQN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 450 LQ-HERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDqlkAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR 528
Cdd:cd14132  69 LRgGPNIVKLLDVVKDPQSKTPSLIFEYVNNTDFKT---LYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 529 DSAGN-VKLGDFGaskrLQTICMSGTGMRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd14132 146 DHEKRkLRLIDWG----LAEFYHPGQEYNVRVASRYYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEP 212
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
399-591 6.14e-18

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: 83.88  E-value: 6.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLcyDVDTGRELASKQVQFDPDSpetskevSALECEIQLLKNLQHERIVQYYGCLRDRaEKTLTIFMEYMP 478
Cdd:cd05082  14 IGKGEFGDVML--GDYRGNKVAVKCIKNDATA-------QAFLAEASVMTQLRHSNLVQLLGVIVEE-KGGLYIVTEYMA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYG--ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcmSGTGMR 556
Cdd:cd05082  84 KGSLVDYLRSRGrsVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASST--QDTGKL 161
                       170       180       190
                ....*....|....*....|....*....|....*
gi 42794767 557 SVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEM 591
Cdd:cd05082 162 PVK----WTAPEALREKKFSTKSDVWSFGILLWEI 192
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
394-585 6.67e-18

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: 84.08  E-value: 6.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPETSKEVSALECEIQLLKNL-QHERIVQYYGCLRDRAektlti 472
Cdd:cd13975   3 KLGRELGRGQYGVVYACDSWGGHFPCALKSV-----VPPDDKHWNDLALEFHYTRSLpKHERIVSLHGSVIDYS------ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 fmeYMPGGS-----VKDQLKA--YGALTESVTRKYTRQI----LEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd13975  72 ---YGGGSSiavllIMERLHRdlYTGIKAGLSLEERLQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGF 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42794767 542 SKrlQTICMSGtgmrSVTGTPYWMSPEVISGEgYGRKADVWSLG 585
Cdd:cd13975 149 CK--PEAMMSG----SIVGTPIHMAPELFSGK-YDNSVDVYAFG 185
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
396-650 6.70e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; 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). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 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: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 83.85  E-value: 6.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHE-----RIVQYYgclrDRAEKTL 470
Cdd:cd14102   5 GSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGSGfrgviKLLDWY----ERPDGFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFGASKRLQTic 549
Cdd:cd14102  81 IVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKD-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 msgTGMRSVTGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAaifkiatqptnpqlpshiseHGR 628
Cdd:cd14102 159 ---TVYTDFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEEIL--------------------RGR 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42794767 629 -DFLRRIFVEARQ------------RPSAEELLTH 650
Cdd:cd14102 216 lYFRRRVSPECQQlikwclslrpsdRPTLEQIFDH 250
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
397-637 7.67e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. 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 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: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 85.16  E-value: 7.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQF-------DPDSPETSKEVsaleceIQLLKNlqHERIVQYYGCLRdrAEKT 469
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKelvnddeDIDWVQTEKHV------FETASN--HPFLVGLHSCFQ--TESR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtIC 549
Cdd:cd05588  71 LFFVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYG-------MC 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPwaeyeamaaiFKIATQPTNPQlpshisE 625
Cdd:cd05588 144 KEGLRPGDTTstfcGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSP----------FDIVGSSDNPD------Q 207
                       250
                ....*....|..
gi 42794767 626 HGRDFLRRIFVE 637
Cdd:cd05588 208 NTEDYLFQVILE 219
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
399-650 9.95e-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: 83.92  E-value: 9.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfDPDSPETSKEVsalecEIqLLKNLQHERIVQyygcLRDRAE--KTLTIFMEY 476
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVI--DKSKRDPSEEI-----EI-LLRYGQHPNIIT----LKDVYDdgKHVYLVTEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR-DSAGN---VKLGDFGASKRLQTicMSG 552
Cdd:cd14175  77 MRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvDESGNpesLRICDFGFAKQLRA--ENG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 TGMRSVTgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAI----FKIATQPTNPqlpsh 622
Cdd:cd14175 155 LLMTPCY-TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsdtpEEILTRIgsgkFTLSGGNWNT----- 228
                       250       260
                ....*....|....*....|....*....
gi 42794767 623 ISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14175 229 VSDAAKDLVSKMLhVDPHQRLTAKQVLQH 257
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
396-610 1.14e-17

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: 83.55  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydvdTGR---ELASKQVQFDPDSPEtskEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTI 472
Cdd:cd14063   5 KEVIGKGRFGRVH------RGRwhgDVAIKLLNIDYLNEE---QLEAFKEEVAAYKNTRHDNLVLFMGACMD--PPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFG--ASKRLQTIC 549
Cdd:cd14063  74 VTSLCKGRTLYSLIHeRKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGlfSLSGLLQPG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 550 MSGTGMRSVTGTPYWMSPEVI----------SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI 610
Cdd:cd14063 153 RREDTLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQV 223
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
399-600 1.20e-17

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: 83.31  E-value: 1.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYdVDTGRELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLtiFMEYMP 478
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLK----GEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLL--VYEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESV---TR-KYTRQILEGMSYLH---SNMIVHRDIKGANILRDSAGNVKLGDFGASKRL---QTI 548
Cdd:cd14664  74 NGSLGELLHSRPESQPPLdweTRqRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMddkDSH 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 549 CMSgtgmrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd14664 154 VMS-----SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDE 200
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
399-598 1.67e-17

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: 83.47  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdSPEtSKEVSALEceIQLLKNLQHERIVQYYGC---LRDRAEKTLTIF-M 474
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQEL-SPK-NRERWCLE--IQIMKRLNHPNVVAARDVpegLQKLAPNDLPLLaM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVK---DQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV---KLGDFGASKRLQti 548
Cdd:cd14038  78 EYCQGGDLRkylNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELD-- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 cmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd14038 156 --QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
455-598 2.17e-17

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: 84.30  E-value: 2.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 455 IVQYYGCLRdrAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV 534
Cdd:cd05617  78 LVGLHSCFQ--TTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHI 155
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 535 KLGDFGaskrlqtICMSGTGMRSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd05617 156 KLTDYG-------MCKEGLGPGDTTstfcGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
396-593 2.38e-17

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: 83.53  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLC----YDVDTGRELASKQVQFDPDSPeTSKEVSALECEIQLLKNL-QHERIVQYYG-CLRDraeKT 469
Cdd:cd05101  29 GKPLGEGCFGQVVMAeavgIDKDKPKEAVTVAVKMLKDDA-TEKDLSDLVSEMEMMKMIgKHKNIINLLGaCTQD---GP 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGAL------------TESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN 533
Cdd:cd05101 105 LYVIVEYASKGNLREYLRARRPPgmeysydinrvpEEQMTFKdlvsCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 534 VKLGDFGASKRLQTI---CMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05101 185 MKIADFGLARDINNIdyyKKTTNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLMWEIFT 243
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
397-650 2.68e-17

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: 82.61  E-value: 2.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFdPDSPETSKEVSAlecEIQLLKNLQHERIVQYY---------GCLRDRAE 467
Cdd:cd14048  12 QCLGRGGFGVVFEAKNKVDDCNYAVKRIRL-PNNELAREKVLR---EVRALAKLDHPGIVRYFnawlerppeGWQEKMDE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAYGALTE---SVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd14048  88 VYLYIQMQLCRKENLKDWMNRRCTMESrelFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 L------QTIcmsGTGMRSV------TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT 612
Cdd:cd14048 168 MdqgepeQTV---LTPMPAYakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQMERIRTLTDVRKLK 244
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 613 QPtnPQLPSHISEHgRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14048 245 FP--ALFTNKYPEE-RDMVQQMLsPSPSERPEAHEVIEH 280
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
395-602 2.68e-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: 83.17  E-value: 2.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpETSKEVSALE-CEiqllknlQHERIVQYYGCLRDRAEKTLTif 473
Cdd:cd14179  11 KDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEA-NTQREIAALKlCE-------GHPNIVKLHEVYHDQLHTFLV-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN--VKLGDFGASK------- 543
Cdd:cd14179  81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLfTDESDNseIKIIDFGFARlkppdnq 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 544 RLQTICMsgtgmrsvtgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYE 602
Cdd:cd14179 161 PLKTPCF----------TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHD 209
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
397-654 2.99e-17

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: 82.77  E-value: 2.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDS-----------PETSKEV-SALECEIQLLKNLQHERIVQYYG-CLR 463
Cdd:cd05051  11 EKLGEGQFGEVHLCEANGLSDLTSDDFIGNDNKDepvlvavkmlrPDASKNArEDFLKEVKIMSQLKDPNIVRLLGvCTR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 464 DraeKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTR------------QILEGMSYLHSNMIVHRDIKGANILRDSA 531
Cdd:cd05051  91 D---EPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKtlsygtllymatQIASGMKYLESLNFVHRDLATRNCLVGPN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 532 GNVKLGDFGASK--------RLQticmsGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT---EKPpwae 600
Cdd:cd05051 168 YTIKIADFGMSRnlysgdyyRIE-----GRAVLPIR----WMAWESILLGKFTTKSDVWAFGVTLWEILTlckEQP---- 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 601 YEAMaaifkiatqpTNPQLPSHISEHGRDFLRRIFV--------------------EARQRPSAEELltHHFAQ 654
Cdd:cd05051 235 YEHL----------TDEQVIENAGEFFRDDGMEVYLsrppncpkeiyelmlecwrrDEEDRPTFREI--HLFLQ 296
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
406-650 3.09e-17

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 81.81  E-value: 3.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 406 RVYLCYDVDTGRELASKQVQFdpdspETSKEVSALECEI-QLLKNL---QHERIVQYYGCLRD-RAEKTLTIFM-EYMPG 479
Cdd:cd13984   9 SAYLAMDTEEGVEVVWNEVQF-----SERKIFKAQEEKIrAVFDNLiqlDHPNIVKFHRYWTDvQEEKARVIFItEYMSS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 480 GSVKDQLKA----YGALTESVTRKYTRQILEGMSYLHS--NMIVHRDIKGANILRDSAGNVKLGdfgaSKRLQTICMSGT 553
Cdd:cd13984  84 GSLKQFLKKtkknHKTMNEKSWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIG----SVAPDAIHNHVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT-------EKPPWAEYEAMAAIFKIatqpTNPQLpshiseh 626
Cdd:cd13984 160 TCREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAAleiqsngEKVSANEEAIIRAIFSL----EDPLQ------- 228
                       250       260
                ....*....|....*....|....*
gi 42794767 627 gRDFLRR-IFVEARQRPSAEELLTH 650
Cdd:cd13984 229 -KDFIRKcLSVAPQDRPSARDLLFH 252
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
390-652 3.69e-17

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: 83.41  E-value: 3.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 390 PINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQyygcLRDRAEKT 469
Cdd:cd07879  14 PERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYR---ELTLLKHMQHENVIG----LLDVFTSA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LT--------IFMEYMpggsVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd07879  87 VSgdefqdfyLVMPYM----QTDLQKIMGHpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRlqticmSGTGMRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKP--------------------PWA 599
Cdd:cd07879 163 LARH------ADAEMTGYVVTRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTlfkgkdyldqltqilkvtgvPGP 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 600 EY----EAMAAIFKIATQPTNP-----QLPSHISEHGRDFLRRIFV-EARQRPSAEELLTHHF 652
Cdd:cd07879 237 EFvqklEDKAAKSYIKSLPKYPrkdfsTLFPKASPQAVDLLEKMLElDVDKRLTATEALEHPY 299
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
393-656 4.29e-17

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: 81.77  E-value: 4.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRgklLGQGAFGRVYLCYDVDTGRELASKqvqFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraekTLTI 472
Cdd:cd14025   1 WEK---VGSGGFGQVYKVRHKHWKTWLAIK---CPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSE----PVGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVKDQLKaygalTESVTRKYTRQILE----GMSYLHS--NMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ 546
Cdd:cd14025  71 VMEYMETGSLEKLLA-----SEPLPWELRFRIIHetavGMNFLHCmkPPLLHLDLKPANILLDAHYHVKISDFGLAKWNG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 547 TICMSGTGMRSVTGTPYWMSPEVI--SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPshis 624
Cdd:cd14025 146 LSHSHDLSRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLS---- 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 42794767 625 ehgrdflrrifVEARQRPSAeellTHHFAQLM 656
Cdd:cd14025 222 -----------PIPRQRPSE----CQQMICLM 238
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
399-650 4.45e-17

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: 83.15  E-value: 4.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVsaleceiqLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 478
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI--------LLRYGQHPNIITLKDVYDD--GKYVYVVTELMK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR-DSAGN---VKLGDFGASKRLQTicMSGTG 554
Cdd:cd14176  97 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFGFAKQLRA--ENGLL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAI----FKIATQPTNPqlpshIS 624
Cdd:cd14176 175 MTPCY-TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpddtpEEILARIgsgkFSLSGGYWNS-----VS 248
                       250       260
                ....*....|....*....|....*..
gi 42794767 625 EHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14176 249 DTAKDLVSKMLhVDPHQRLTAALVLRH 275
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
399-590 4.60e-17

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: 81.89  E-value: 4.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQyyGClrDRAEKTLTIF----- 473
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCH----EIQIMKKLNHPNVVK--AC--DVPEEMNFLVndvpl 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 --MEYMPGGSVKDQL---KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAGNV--KLGDFGASKRL 545
Cdd:cd14039  73 laMEYCSGGDLRKLLnkpENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIvLQEINGKIvhKIIDLGYAKDL 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42794767 546 QticmSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVE 590
Cdd:cd14039 153 D----QGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
395-625 4.90e-17

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: 81.56  E-value: 4.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRE---LASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLT 471
Cdd:cd05063   9 KQKVIGAGEFGEVFRGILKMPGRKevaVAIKTLK----PGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKF--KPAM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcM 550
Cdd:cd05063  83 IITEYMENGALDKYLRDHdGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDD-P 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPW--AEYEAMAAIFKIATQPTNPQLPSHISE 625
Cdd:cd05063 162 EGTYTTSGGKIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfgERPYWdmSNHEVMKAINDGFRLPAPMDCPSAVYQ 241
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
395-598 6.31e-17

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: 81.84  E-value: 6.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 395 RGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSpETSKEVSALE-CEiqllknlQHERIVQYYGCLRDRAEKTLTif 473
Cdd:cd14180  10 EEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEA-NTQREVAALRlCQ-------SHPNIVALHEVLHDQYHTYLV-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---VKLGDFG-------ASK 543
Cdd:cd14180  80 MELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGfarlrpqGSR 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 544 RLQTICMsgtgmrsvtgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd14180 160 PLQTPCF----------TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPF 204
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
396-593 6.49e-17

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: 80.82  E-value: 6.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydVDTGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFME 475
Cdd:cd05085   1 GELLGKGNFGEVY----KGTLKDKTPVAVKTCKEDLPQELKIKFLS-EARILKQYDHPNIVKLIGVCTQR--QPIYIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSV-------KDQLKAYGALtesvtrKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd05085  74 LVPGGDFlsflrkkKDELKTKQLV------KFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDG 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 549 CMSGTGMRSVtgtPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05085 148 VYSSSGLKQI---PIkWTAPEALNYGRYSSESDVWSFGILLWETFS 190
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
398-643 7.73e-17

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: 81.64  E-value: 7.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYL-CYDvdtGRELASKQVqfdpdsPETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAEKTLT--IF 473
Cdd:cd14054   2 LIGQGRYGTVWKgSLD---ERPVAVKVF------PARHRQNFQNEKDIYELPLMEHSNILRFIGaDERPTADGRMEylLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNM---------IVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd14054  73 LEYAPKGSLCSYLREN-TLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLAMV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQ--TICMSGTGMRSVT-----GTPYWMSPEVISG-------EGYGRKADVWSLGCTVVEMLT---------EKPPW-AE 600
Cdd:cd14054 152 LRgsSLVRGRPGAAENAsisevGTLRYMAPEVLEGavnlrdcESALKQVDVYALGLVLWEIAMrcsdlypgeSVPPYqMP 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42794767 601 YEAmaaifKIATQPTNPQLPSHISEHgrdflrrifveaRQRPS 643
Cdd:cd14054 232 YEA-----ELGNHPTFEDMQLLVSRE------------KARPK 257
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
398-593 8.21e-17

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: 80.38  E-value: 8.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCydVDTGRELASKQVqfdpdSPETSKEVsaLECEIQLLKNLQHERIVQYYGC-LRDRAektltIFMEY 476
Cdd:cd14068   1 LLGDGGFGSVYRA--VYRGEDVAVKIF-----NKHTSFRL--LRQELVVLSHLHHPSLVALLAAgTAPRM-----LVMEL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKA-YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-----RDSAGNVKLGDFGASkrlQTICm 550
Cdd:cd14068  67 APKGSLDALLQQdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftlyPNCAIIAKIADYGIA---QYCC- 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42794767 551 sGTGMRSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLT 593
Cdd:cd14068 143 -RMGIKTSEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILT 185
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
392-599 8.32e-17

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK 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: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 80.76  E-value: 8.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKqVQFDpdspETSKEVsaLECEIQLLKNLQHERIV-QYYGClrDRAEKTL 470
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMK-VESK----SQPKQV--LKMEVAVLKKLQGKPHFcRLIGC--GRTERYN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMpGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAG--NVKLGDFGASKR 544
Cdd:cd14017  72 YIVMTLL-GPNLAELRRSQprGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAigRGPSDerTVYILDFGLARQ 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 545 LQTICMSGTGMRSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA 599
Cdd:cd14017 151 YTNKDGEVERPPRNAagfrGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWR 209
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
397-648 9.60e-17

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: 80.31  E-value: 9.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLC-----YDVdtgrelASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAektL 470
Cdd:cd05113  10 KELGTGQFGVVKYGkwrgqYDV------AIKMIK------EGSMSEDEFIEEAKVMMNLSHEKLVQLYGvCTKQRP---I 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqtic 549
Cdd:cd05113  75 FIITEYMANGCLLNYLREMRkRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYV---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVtGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIAtQPTNPQLPSHISE 625
Cdd:cd05113 151 LDDEYTSSV-GSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVS-QGLRLYRPHLASE 228
                       250       260
                ....*....|....*....|....
gi 42794767 626 HGRDFLRRIFVE-ARQRPSAEELL 648
Cdd:cd05113 229 KVYTIMYSCWHEkADERPTFKILL 252
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
399-652 1.09e-16

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: 81.19  E-value: 1.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFDPdspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRdrAEKTLTIFMEYMP 478
Cdd:cd07872  14 LGEGTYATVFKGRSKLTENLVALKEIRLEH---EEGAPCTAIR-EVSLLKDLKHANIVTLHDIVH--TDKSLTLVFEYLD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 ggsvKDqLKAY-----GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTICMSGT 553
Cdd:cd07872  88 ----KD-LKQYmddcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSVPTKTY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 554 GMRSVtgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKP--PWAEYE-AMAAIFKIATQPTNPQLPS-------- 621
Cdd:cd07872 162 SNEVV--TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPlfPGSTVEdELHLIFRLLGTPTEETWPGissndefk 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 622 -----------------HISEHGRDFLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd07872 240 nynfpkykpqplinhapRLDTEGIELLTKFLqYESKKRISAEEAMKHAY 288
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
397-594 1.14e-16

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: 80.50  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEY 476
Cdd:cd05070  15 KRLGNGQFGEVWM------GTWNGNTKVAIKTLKPGTMSPESFLE-EAQIMKKLKHDKLVQLYAVV---SEEPIYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK--AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd05070  85 MSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED--NEYTA 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 555 MRSVTGTPYWMSPEVISgegYGR---KADVWSLGCTVVEMLTE 594
Cdd:cd05070 163 RQGAKFPIKWTAPEAAL---YGRftiKSDVWSFGILLTELVTK 202
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
397-647 1.15e-16

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: 80.42  E-value: 1.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCyDVDTGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQyygCLRDRAEKT-LTIFME 475
Cdd:cd05087   3 KEIGHGWFGKVFLG-EVNSGLSSTQVVVKELKASASVQDQMQFLE-EAQPYRALQHTNLLQ---CLAQCAEVTpYLLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGAlTESVT------RKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqtiC 549
Cdd:cd05087  78 FCPLGDLKGYLRSCRA-AESMApdpltlQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSH-----C 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVTGTPY----WMSPEVISgEGYG--------RKADVWSLGCTVVEMLT-EKPPWAEYEAMAAI-FKIATQP- 614
Cdd:cd05087 152 KYKEDYFVTADQLWvplrWIAPELVD-EVHGnllvvdqtKQSNVWSLGVTIWELFElGNQPYRHYSDRQVLtYTVREQQl 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 42794767 615 --TNPQLPSHISEHGRDFLRRIFVEARQRPSAEEL 647
Cdd:cd05087 231 klPKPQLKLSLAERWYEVMQFCWLQPEQRPTAEEV 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
396-648 1.31e-16

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: 80.49  E-value: 1.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydvdTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGClrdRAEKTLTIFME 475
Cdd:cd14151  13 GQRIGSGSFGTVY------KGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGY---STKPQLAIVTQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTG 554
Cdd:cd14151  84 WCEGSSLYHHLHIIETKFEMIKLiDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG----LATVKSRWSG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 ---MRSVTGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWAEYEAM-AAIFKIATQPTNPQLpSHISEHG 627
Cdd:cd14151 160 shqFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDL-SKVRSNC 238
                       250       260
                ....*....|....*....|....*.
gi 42794767 628 RDFLRRIFVEA-----RQRPSAEELL 648
Cdd:cd14151 239 PKAMKRLMAEClkkkrDERPLFPQIL 264
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
398-633 1.62e-16

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: 80.49  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKE-VSALEC-EIQLLKNLQHERIVQYYGCLRDRAEKTLTIfME 475
Cdd:cd14040  13 LLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnYHKHACrEYRIHKELDHPRIVKLYDYFSLDTDTFCTV-LE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHS--NMIVHRDIKGANILR---DSAGNVKLGDFGASKRLQTICM 550
Cdd:cd14040  92 YCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSY 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVT---GTPYWMSPE--VISGE--GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTNPQLPS 621
Cdd:cd14040 172 GVDGMDLTSqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTilKATEVQFPV 251
                       250
                ....*....|....
gi 42794767 622 H--ISEHGRDFLRR 633
Cdd:cd14040 252 KpvVSNEAKAFIRR 265
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
392-603 1.92e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 79.81  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRELASKqvqFDPdspeTSKEVSALECEIQLLKNLQ-HERI--VQYYGclrdrAEK 468
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK---IEK----KDSKHPQLEYEAKVYKLLQgGPGIprLYWFG-----QEG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIF-MEYMpGGSVKDQLKAYGaltesvtRKYT--------RQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKL 536
Cdd:cd14016  69 DYNVMvMDLL-GPSLEDLFNKCG-------RKFSlktvlmlaDQMISRLEYLHSKGYIHRDIKPENFLmglGKNSNKVYL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 537 GDFGASKRLQTIcMSGTGM-----RSVTGTPYWMSpeVISGEGY--GRKADVWSLGCTVVEMLTEKPPWAEYEA 603
Cdd:cd14016 141 IDFGLAKKYRDP-RTGKHIpyregKSLTGTARYAS--INAHLGIeqSRRDDLESLGYVLIYFLKGSLPWQGLKA 211
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
398-640 1.94e-16

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: 80.49  E-value: 1.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKE-VSALEC-EIQLLKNLQHERIVQYYGCLRDRAEKTLTIfME 475
Cdd:cd14041  13 LLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKEnYHKHACrEYRIHKELDHPRIVKLYDYFSLDTDSFCTV-LE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHS--NMIVHRDIKGANILR---DSAGNVKLGDFGASKRLQTICM 550
Cdd:cd14041  92 YCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGLSKIMDDDSY 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVT----GTPYWMSPE--VISGE--GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTNPQLP 620
Cdd:cd14041 172 NSVDGMELTsqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTilKATEVQFP 251
                       250       260
                ....*....|....*....|..
gi 42794767 621 SH--ISEHGRDFLRRIFVEARQ 640
Cdd:cd14041 252 PKpvVTPEAKAFIRRCLAYRKE 273
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
432-652 2.03e-16

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 79.50  E-value: 2.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 432 ETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYL 511
Cdd:cd14112  39 EVSDEASEAVREFESLRTLQHENVQRLIAAFKPS--NFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 512 HSNMIVHRDIKGANILRDSAGN--VKLGDFGASKRLqticmSGTGMRSVTGTPYWMSPEVISGEGYGR-KADVWSLGCTV 588
Cdd:cd14112 116 HFKGIAHLDVQPDNIMFQSVRSwqVKLVDFGRAQKV-----SKLGKVPVDGDTDWASPEFHNPETPITvQSDIWGLGVLT 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 589 VEMLTEKPPWA-----EYEAMAAIFKIATQPTNpqLPSHISEHGRDFLRRIFVEA-RQRPSAEELLTHHF 652
Cdd:cd14112 191 FCLLSGFHPFTseyddEEETKENVIFVKCRPNL--IFVEATQEALRFATWALKKSpTRRMRTDEALEHRW 258
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
397-628 2.55e-16

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: 80.83  E-value: 2.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSkevsalECEIQLLKNL-QHERIVQYYgclrdrAEKTLTIFM- 474
Cdd:cd14226  19 SLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQA------QIEVRLLELMnKHDTENKYY------IVRLKRHFMf 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 -----------EYmpggSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSN--MIVHRDIKGANIL----RDSAgnVK 535
Cdd:cd14226  87 rnhlclvfellSY----NLYDLLRNtnFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILlcnpKRSA--IK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 536 LGDFGASkrlqtiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIAT 612
Cdd:cd14226 161 IIDFGSS------CQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMNKIVEVLG 234
                       250
                ....*....|....*.
gi 42794767 613 QPtnpqlPSHISEHGR 628
Cdd:cd14226 235 MP-----PVHMLDQAP 245
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
392-596 2.59e-16

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: 80.53  E-value: 2.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 392 NWRRGKLLGQGAFGRVYLCYDVDTGRE--LASKQVqfdpdSPETSKEVSALEC--EIQLLKNLQ-HERIVQYYGC--LRD 464
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETSEEetVAIKKI-----TNVFSKKILAKRAlrELKLLRHFRgHKNITCLYDMdiVFP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 RAEKTLTIFMEYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKR 544
Cdd:cd07857  76 GNFNELYLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 545 LQTICMSGTG-MRSVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07857 155 FSENPGENAGfMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKP 208
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
397-652 2.88e-16

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: 78.80  E-value: 2.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQ-HERIVQYYGCLRDraEKTLTIFME 475
Cdd:cd14019   7 EKIGEGTFSSVYKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILNELECLERLGgSNNVSGLITAFRN--EDQVVAVLP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGaLTEsvTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA-GNVKLGDFGASKRLqticMSGTG 554
Cdd:cd14019  85 YIEHDDFRDFYRKMS-LTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGLAQRE----EDRPE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MR-SVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIFKIATqptnpqlpshI--SEHGRD 629
Cdd:cd14019 158 QRaPRAGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSgRFPFFFSSDDIDALAEIAT----------IfgSDEAYD 227
                       250       260
                ....*....|....*....|....
gi 42794767 630 FLRRIF-VEARQRPSAEELLTHHF 652
Cdd:cd14019 228 LLDKLLeLDPSKRITAEEALKHPF 251
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
399-592 3.29e-16

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-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 PFTAIRE-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: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 79.74  E-value: 3.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFdpdSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEYMP 478
Cdd:cd07869  13 LGEGSYATVYKGKSKVNGKLVALKVIRL---QEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTK--ETLTLVFEYVH 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTIcMSGTGMRSV 558
Cdd:cd07869  87 TDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA-RAKSV-PSHTYSNEV 164
                       170       180       190
                ....*....|....*....|....*....|....*
gi 42794767 559 TgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEML 592
Cdd:cd07869 165 V-TLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMI 198
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
397-649 3.34e-16

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: 79.48  E-value: 3.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSKEVSALEcEIQLLKNLQ-HERIVQYYGCLRDRAEKTLTIFME 475
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVGTGKEYALKRLL----SNEEEKNKAIIQ-EINFMKKLSgHPNIVQFCSAASIGKEESDQGQAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YM-----PGGSVKDQLK---AYGALTESVTRKYTRQILEGMSYLHSNM--IVHRDIKGANILRDSAGNVKLGDFGASkrl 545
Cdd:cd14036  81 YLlltelCKGQLVDFVKkveAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSA--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGT-----GMRSV-------TGTPYWMSPEVI---SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI 610
Cdd:cd14036 158 TTEAHYPDyswsaQKRSLvedeitrNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRIINAK 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 42794767 611 ATQPTNPQLPSHISEHGRDFLRrifVEARQRPSAEELLT 649
Cdd:cd14036 238 YTIPPNDTQYTVFHDLIRSTLK---VNPEERLSITEIVE 273
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
399-645 5.35e-16

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: 78.57  E-value: 5.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLcydvdtGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEYMP 478
Cdd:cd05069  20 LGQGCFGEVWM------GTWNGTTKVAIKTLKPGTMMPEAFLQ-EAQIMKKLRHDKLVPLYAVV---SEEPIYIVTEFMG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLK----AYGALTESVtrKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTicMSGTG 554
Cdd:cd05069  90 KGSLLDFLKegdgKYLKLPQLV--DMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED--NEYTA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 555 MRSVTGTPYWMSPEVISgegYGR---KADVWSLGCTVVEMLTEK----PPWAEYEAMAAIFKIATQPTNPQLPSHISEHG 627
Cdd:cd05069 166 RQGAKFPIKWTAPEAAL---YGRftiKSDVWSFGILLTELVTKGrvpyPGMVNREVLEQVERGYRMPCPQGCPESLHELM 242
                       250
                ....*....|....*...
gi 42794767 628 RDFLRRifvEARQRPSAE 645
Cdd:cd05069 243 KLCWKK---DPDERPTFE 257
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
394-593 5.43e-16

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: 78.84  E-value: 5.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGREL----ASKQVQfDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYG-ClrdrAEK 468
Cdd:cd05111  10 RKLKVLGSGVFGTVHKGIWIPEGDSIkipvAIKVIQ-DRSGRQSFQAVTD---HMLAIGSLDHAYIVRLLGiC----PGA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 547
Cdd:cd05111  82 SLQLVTQLLPLGSLLDHVRQHrGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYP 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42794767 548 icMSGTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05111 162 --DDKKYFYSEAKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMT 206
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
393-655 6.41e-16

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: 78.91  E-value: 6.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGREL----ASKQVQfDPDSPETSKEVsaLEcEIQLLKNLQHERIVQYYG-CLrdraE 467
Cdd:cd05108   9 FKKIKVLGSGAFGTVYKGLWIPEGEKVkipvAIKELR-EATSPKANKEI--LD-EAYVMASVDNPHVCRLLGiCL----T 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 468 KTLTIFMEYMPGGSVKDQLKAYgalTESVTRKYTR----QILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 543
Cdd:cd05108  81 STVQLITQLMPFGCLLDYVREH---KDNIGSQYLLnwcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 544 RL---QTICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPpwaeYEAMAAIfKIATQPTN-- 616
Cdd:cd05108 158 LLgaeEKEYHAEGGKVPIK----WMALESILHRIYTHQSDVWSYGVTVWELMTfgSKP----YDGIPAS-EISSILEKge 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42794767 617 --PQLPSHISEHGRDFLRRIFVEARQRPSAEELLThHFAQL 655
Cdd:cd05108 229 rlPQPPICTIDVYMIMVKCWMIDADSRPKFRELII-EFSKM 268
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
396-593 6.49e-16

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: 77.99  E-value: 6.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcYDVDTGRELASKQVQFDPDSpetskevSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFME 475
Cdd:cd05083  11 GEIIGEGEFGAVL--QGEYMGQKVAVKNIKCDVTA-------QAFLEETAVMTKLQHKNLVRLLGVI---LHNGLYIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYGALTESVTR--KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqticmsgT 553
Cdd:cd05083  79 LMSKGNLVNFLRSRGRALVPVIQllQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK---------V 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 554 GMRSVTGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05083 150 GSMGVDNSRLpvkWTAPEALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
399-600 6.90e-16

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: 78.53  E-value: 6.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYlcydvdTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFMEYMP 478
Cdd:cd14149  20 IGSGSFGTVY------KGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYM---TKDNLAIVTQWCE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGALTESVTR-KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTGMRS 557
Cdd:cd14149  91 GSSLYKHLHVQETKFQMFQLiDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG----LATVKSRWSGSQQ 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 558 V---TGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd14149 167 VeqpTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELPYSH 215
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
397-593 7.28e-16

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: 78.22  E-value: 7.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYlcydvdTGRELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFME 475
Cdd:cd05068  14 RKLGSGQFGEVW------EGLWNNTTPVAVKTLKPGTMDPEDFLR-EAQIMKKLRHPKLIQLYAvCTL---EEPIYIITE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 476 YMPGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTG 554
Cdd:cd05068  84 LMKHGSLLEYLQGKGrSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFG----LARVIKVEDE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42794767 555 MRSVTGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05068 160 YEAREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVT 201
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
399-540 8.13e-16

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: 74.40  E-value: 8.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdSPETSKEVSALECEIQ-LLKNLQHER-IVQYYGCLRDRAEKTLTifMEY 476
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIG-----DDVNNEEGEDLESEMDiLRRLKGLELnIPKVLVTEDVDGPNILL--MEL 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 477 MPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd13968  74 VKGGTLIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
370-592 9.35e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 79.15  E-value: 9.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  370 DSENALSVQERNVPTKSPSAPI----NWRRGKLLGQGAFGRVYLcydvdtgrelASKQVQFDPDSPETSKEVSALeCEIQ 445
Cdd:PHA03209  41 ASESDDDDDDGLIPTKQKAREVvaslGYTVIKTLTPGSEGRVFV----------ATKPGQPDPVVLKIGQKGTTL-IEAM 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  446 LLKNLQHERIVQYYGCLRdRAEKTLTIFMEYmpggsvKDQLKAYgaLTESVTR-------KYTRQILEGMSYLHSNMIVH 518
Cdd:PHA03209 110 LLQNVNHPSVIRMKDTLV-SGAITCMVLPHY------SSDLYTY--LTKRSRPlpidqalIIEKQILEGLRYLHAQRIIH 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767  519 RDIKGANILRDSAGNVKLGDFGASKrlqtICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:PHA03209 181 RDVKTENIFINDVDQVCIGDLGAAQ----FPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
397-596 1.21e-15

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: 78.67  E-value: 1.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQfdpDSPETSKEVSALECEIQLLKNLQHERIVQYYGCL---RDRAEKTLTIF 473
Cdd:cd07859   6 EVIGKGSYGVVCSAIDTHTGEKVAIKKIN---DVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppSRREFKDIYVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMpGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGT 553
Cdd:cd07859  83 FELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAI 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 554 GMRSVTGTPYWMSPEvISGEGYGRKA---DVWSLGCTVVEMLTEKP 596
Cdd:cd07859 162 FWTDYVATRWYRAPE-LCGSFFSKYTpaiDIWSIGCIFAEVLTGKP 206
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
399-594 1.21e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 80.12  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  399 LGQGAFGRVYLCyDV--DTGRELASKQV----QFDPDSPE--------TSKEVSALECEIQLLKNLQHERIVQYYGCLRD 464
Cdd:PHA03210 156 LPAGAFGKIFIC-ALraSTEEAEARRGVnstnQGKPKCERliakrvkaGSRAAIQLENEILALGRLNHENILKIEEILRS 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  465 RAEKTLTI------FMEYMPGGSVkdQLKAYGALTEsvTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGD 538
Cdd:PHA03210 235 EANTYMITqkydfdLYSFMYDEAF--DWKDRPLLKQ--TRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGD 310
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767  539 FGASkrlqticMSGTGMRSV-----TGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE 594
Cdd:PHA03210 311 FGTA-------MPFEKEREAfdygwVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSH 364
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
397-592 1.40e-15

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: 78.22  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF--- 473
Cdd:cd07850   6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYR---ELVLMKLVNHKNIIGLLNVFT--PQKSLEEFqdv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 ---MEYMPGGSVK-DQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd07850  81 ylvMELMDANLCQvIQMD----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42794767 550 MsgtgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd07850 157 M----MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMI 195
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
396-596 1.69e-15

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 77.80  E-value: 1.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTG--RELASKQVQfdpdspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLTIF 473
Cdd:cd07867   7 GCKVGRGTYGHVYKAKRKDGKdeKEYALKQIE------GTGISMSACR-EIALLRELKHPNVIALQKVFLSHSDRKVWLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEY--------MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGA 541
Cdd:cd07867  80 FDYaehdlwhiIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILvmgeGPERGRVKIADMGF 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 542 SKRLQTICMSGTGMRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07867 160 ARLFNSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEP 215
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
396-593 2.05e-15

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: 77.70  E-value: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLC--YDVDTGR--ELASKQVQFDPDSPeTSKEVSALECEIQLLKNL-QHERIVQYYG-CLRDraeKT 469
Cdd:cd05099  17 GKPLGEGCFGQVVRAeaYGIDKSRpdQTVTVAVKMLKDNA-TDKDLADLISEMELMKLIgKHKNIINLLGvCTQE---GP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTR----------------QILEGMSYLHSNMIVHRDIKGANILRDSAGN 533
Cdd:cd05099  93 LYVIVEYAAKGNLREFLRARRPPGPDYTFDITKvpeeqlsfkdlvscayQVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 534 VKLGDFGASKRLQTI---CMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05099 173 MKIADFGLARGVHDIdyyKKTSNGRLPVK----WMAPEALFDRVYTHQSDVWSFGILMWEIFT 231
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
416-625 2.24e-15

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: 76.66  E-value: 2.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 416 GRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMPGGSVKDQLKAYGALTES 495
Cdd:cd13992  25 GRTVAIKHITFSRTEKRTILQ------ELNQLKELVHDNLNKFIGICINPPN--IAVVTEYCTRGSLQDVLLNREIKMDW 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 496 VTR-KYTRQILEGMSYLHSNMI-VHRDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGMRSVTGTPY---WMSPEVI 570
Cdd:cd13992  97 MFKsSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEE---QTNHQLDEDAQHKkllWTAPELL 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 571 SGEGYGR----KADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISE 625
Cdd:cd13992 174 RGSLLEVrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFRPELAVL 232
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
399-585 3.76e-15

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: 76.27  E-value: 3.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVY-------------LCYDVDTGRELASKQVQFDpdspetskevsaLECEIQLLKNLQHERIVQYYG-CLRd 464
Cdd:cd05036  14 LGQGAFGEVYegtvsgmpgdpspLQVAVKTLPELCSEQDEMD------------FLMEALIMSKFNHPNIVRCIGvCFQ- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 465 raEKTLTIFMEYMPGGSVKDQLKAYGALTESVTR-------KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN---V 534
Cdd:cd05036  81 --RLPRFILLELMAGGDLKSFLRENRPRPEQPSSltmldllQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 535 KLGDFGASK---RLQTICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLG 585
Cdd:cd05036 159 KIGDFGMARdiyRADYYRKGGKAMLPVK----WMPPEAFLDGIFTSKTDVWSFG 208
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
399-595 3.96e-15

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: 76.88  E-value: 3.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTG-RELASKQVQfdpdSPETSKEvsALECEIQLLKNLQHERIVQYYGCLR--DRAE--KTLTIF 473
Cdd:cd14135   8 LGKGVFSNVVRARDLARGnQEVAIKIIR----NNELMHK--AGLKELEILKKLNDADPDDKKHCIRllRHFEhkNHLCLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMpGGSVKDQLKAYGA---LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNV-KLGDFGaskrlqtic 549
Cdd:cd14135  82 FESL-SMNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFG--------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42794767 550 mSGTGMRSVTGTPYWMS-----PEVISGEGYGRKADVWSLGCTVVEMLTEK 595
Cdd:cd14135 152 -SASDIGENEITPYLVSrfyraPEIILGLPYDYPIDMWSVGCTLYELYTGK 201
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
399-597 4.06e-15

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: 76.40  E-value: 4.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTgrELASKQVQFDPDSPETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLtIFMeYMP 478
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSELDWSVVKNSFLT-EVEKLSRFRHPNIVDLAGYSAQQGNYCL-IYV-YLP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 479 GGSVKDQLKAYGAlTESVTRKYTRQILEGMS----YLHSNM--IVHRDIKGANILRDSAGNVKLGDFGA---SKRLQTIC 549
Cdd:cd14159  76 NGSLEDRLHCQVS-CPCLSWSQRLHVLLGTAraiqYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLarfSRRPKQPG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMR--SVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd14159 155 MSSTLARtqTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
399-650 4.23e-15

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: 76.21  E-value: 4.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVqfdpdspETSKEVSALECEIqLLKNLQHERIVQyygcLRDRAEKTLTIFM--EY 476
Cdd:cd14177  12 IGVGSYSVCKRCIHRATNMEFAVKII-------DKSKRDPSEEIEI-LMRYGQHPNIIT----LKDVYDDGRYVYLvtEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAGN---VKLGDFGASKRLQticmsg 552
Cdd:cd14177  80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLR------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 553 tGMRSVTGTPYW----MSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAI--FKIATQPTNpqlP 620
Cdd:cd14177 154 -GENGLLLTPCYtanfVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANgpndtpEEILLRIgsGKFSLSGGN---W 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 621 SHISEHGRDFLRRIF-VEARQRPSAEELLTH 650
Cdd:cd14177 230 DTVSDAAKDLLSHMLhVDPHQRYTAEQVLKH 260
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
397-597 4.34e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 77.58  E-value: 4.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  397 KLLGQGAFGRVYLC--YDVDTGRELASKQVQFDPDspetskevsaLECEIQLLKNLQHERIVQYYGCLRDRAektlTIFM 474
Cdd:PHA03207  98 SSLTPGSEGEVFVCtkHGDEQRKKVIVKAVTGGKT----------PGREIDILKTISHRAIINLIHAYRWKS----TVCM 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  475 eYMPggSVKDQLKAYGALTESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqTICM 550
Cdd:PHA03207 164 -VMP--KYKCDLFTYVDRSGPLPLEqaitIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKL-DAHP 239
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 42794767  551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:PHA03207 240 DTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVT 286
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
396-651 5.67e-15

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: 76.60  E-value: 5.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASK----QVQFDPDSPeTSKEVSALECEIQLLKNL-QHERIVQYYG-CLRDraeKT 469
Cdd:cd05100  17 GKPLGEGCFGQVVMAEAIGIDKDKPNKpvtvAVKMLKDDA-TDKDLSDLVSEMEMMKMIgKHKNIINLLGaCTQD---GP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKA-------YGALT-----ESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN 533
Cdd:cd05100  93 LYVLVEYASKGNLREYLRArrppgmdYSFDTcklpeEQLTFKdlvsCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 534 VKLGDFGASKRLQTI---CMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI 610
Cdd:cd05100 173 MKIADFGLARDVHNIdyyKKTTNGRLPVK----WMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKL 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42794767 611 ATQPTNPQLPSHISEHGRDFLRRIF-VEARQRPSAEELLTHH 651
Cdd:cd05100 249 LKEGHRMDKPANCTHELYMIMRECWhAVPSQRPTFKQLVEDL 290
pknD PRK13184
serine/threonine-protein kinase PknD;
397-598 6.19e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 78.66  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQllKNLQHERIVQYYGCLRDRAEKTLTifMEY 476
Cdd:PRK13184   8 RLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIA--ADLIHPGIVPVYSICSDGDPVYYT--MPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  477 MPGGSVKDQLKAYGAlTESVTRKYTRQ------------ILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK- 543
Cdd:PRK13184  84 IEGYTLKSLLKSVWQ-KESLSKELAEKtsvgaflsifhkICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIf 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767  544 -------------RLQTICMSG-TGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:PRK13184 163 kkleeedlldidvDERNICYSSmTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
396-593 7.47e-15

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: 75.53  E-value: 7.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRE------LASKQVQFDpdspETSKEVSALECEIQLLKNL-QHERIVQYYGCLRDraEK 468
Cdd:cd05053  17 GKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKMLKDD----ATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ--DG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTIFMEYMPGGSVKDQLKAY------------GALTESVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAG 532
Cdd:cd05053  91 PLYVVVEYASKGNLREFLRARrppgeeaspddpRVPEEQLTQKdlvsFAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 533 NVKLGDFGASKRLQTI-----CMSGTgmrsvtgTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05053 171 VMKIADFGLARDIHHIdyyrkTTNGR-------LPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFT 230
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
396-596 8.03e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 76.25  E-value: 8.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVD--TGRELASKQVQfdpdspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEKTLTIF 473
Cdd:cd07868  22 GCKVGRGTYGHVYKAKRKDgkDDKDYALKQIE------GTGISMSACR-EIALLRELKHPNVISLQKVFLSHADRKVWLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEY--------MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGA 541
Cdd:cd07868  95 FDYaehdlwhiIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILvmgeGPERGRVKIADMGF 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 542 SKRLQTICMSGTGMRSVTGTPYWMSPEVISG-EGYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd07868 175 ARLFNSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEP 230
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
396-647 1.01e-14

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: 74.95  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRV---YLCYDVDTGRELASKQVQFDPDspeTSKEVSALECEIQLLKNLQHERIVQYYGC-LRDRAEKTLT 471
Cdd:cd05074  14 GRMLGKGEFGSVreaQLKSEDGSFQKVAVKMLKADIF---SSSDIEEFLREAACMKEFDHPNVIKLIGVsLRSRAKGRLP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDqLKAY----------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd05074  91 IPMVILPFMKHGD-LHTFllmsrigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 SKRLqticMSGTGMR--SVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAmAAIFKIATQPTNP 617
Cdd:cd05074 170 SKKI----YSGDYYRqgCASKLPVkWLALESLADNVYTTHSDVWAFGVTMWEIMTRgQTPYAGVEN-SEIYNYLIKGNRL 244
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 618 QLPSHISEHGRDFLRRIFV-EARQRPSAEEL 647
Cdd:cd05074 245 KQPPDCLEDVYELMCQCWSpEPKCRPSFQHL 275
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
396-593 1.21e-14

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: 75.05  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRE-------LASKQVQFDPdspeTSKEVSALECEIQLLKNL-QHERIVQYYG-CLRDra 466
Cdd:cd05098  18 GKPLGEGCFGQVVLAEAIGLDKDkpnrvtkVAVKMLKSDA----TEKDLSDLISEMEMMKMIgKHKNIINLLGaCTQD-- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 eKTLTIFMEYMPGGSVKDQLKA---------YG---------ALTESVTRKYtrQILEGMSYLHSNMIVHRDIKGANILR 528
Cdd:cd05098  92 -GPLYVIVEYASKGNLREYLQArrppgmeycYNpshnpeeqlSSKDLVSCAY--QVARGMEYLASKKCIHRDLAARNVLV 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794767 529 DSAGNVKLGDFGASKRLQTI---CMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05098 169 TEDNVMKIADFGLARDIHHIdyyKKTTNGRLPVK----WMAPEALFDRIYTHQSDVWSFGVLLWEIFT 232
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
427-648 1.22e-14

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: 74.74  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 427 DPDSPETSKEVSALECEIqlLKNLQHERIVQYYGcLRDRAEKTLTIFMEYMpGGSVKDQLKA-----YGALTESVTRKYT 501
Cdd:cd14001  41 DKGQRSLYQERLKEEAKI--LKSLNHPNIVGFRA-FTKSEDGSLCLAMEYG-GKSLNDLIEEryeagLGPFPAATILKVA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 502 RQILEGMSYLHSN-MIVHRDIKGANIL-RDSAGNVKLGDFGASKRL-QTICMSGTGMRSVTGTPYWMSPEVISGEG-YGR 577
Cdd:cd14001 117 LSIARALEYLHNEkKILHGDIKSGNVLiKGDFESVKLCDFGVSLPLtENLEVDSDPKAQYVGTEPWKAKEALEEGGvITD 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 578 KADVWSLGCTVVEMLTEKPPWA--------------EYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFV-----EA 638
Cdd:cd14001 197 KADIFAYGLVLWEMMTLSVPHLnlldiedddedesfDEDEEDEEAYYGTLGTRPALNLGELDDSYQKVIELFYactqeDP 276
                       250
                ....*....|
gi 42794767 639 RQRPSAEELL 648
Cdd:cd14001 277 KDRPSAAHIV 286
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
491-595 1.24e-14

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: 75.94  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 491 ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTICMSGTGMRSVTgTPYWMSPEVI 570
Cdd:cd07853  99 PLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLA-RVEEPDESKHMTQEVV-TQYYRAPEIL 176
                        90       100
                ....*....|....*....|....*.
gi 42794767 571 SG-EGYGRKADVWSLGCTVVEMLTEK 595
Cdd:cd07853 177 MGsRHYTSAVDIWSVGCIFAELLGRR 202
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
399-638 1.25e-14

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: 75.01  E-value: 1.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFD------------PDSPETSKevSALECEIQLLKNLQHERIVQYYG-CLRDr 465
Cdd:cd05097  13 LGEGQFGEVHLCEAEGLAEFLGEGAPEFDgqpvlvavkmlrADVTKTAR--NDFLKEIKIMSRLKNPNIIRLLGvCVSD- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 aeKTLTIFMEYMPGGSVK---DQLKAYGALTE-----SVTRK----YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN 533
Cdd:cd05097  90 --DPLCMITEYMENGDLNqflSQREIESTFTHannipSVSIAnllyMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 534 VKLGDFGASKRLQTICMSGTGMRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLT---EKPpwaeYEAMaaifki 610
Cdd:cd05097 168 IKIADFGMSRNLYSGDYYRIQGRAVLPI-RWMAWESILLGKFTTASDVWAFGVTLWEMFTlckEQP----YSLL------ 236
                       250       260
                ....*....|....*....|....*...
gi 42794767 611 atqpTNPQLPSHISEHGRDFLRRIFVEA 638
Cdd:cd05097 237 ----SDEQVIENTGEFFRNQGRQIYLSQ 260
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
396-593 1.32e-14

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: 74.83  E-value: 1.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPET-SKEVSALECEIQLLKNL-QHERIVQYYG-ClrDRAEKTLTI 472
Cdd:cd05055  40 GKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAhSSEREALMSELKIMSHLgNHENIVNLLGaC--TIGGPILVI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FmEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqticM 550
Cdd:cd05055 118 T-EYCCYGDLLNFLrrKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDI----M 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 551 SGTG--MRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05055 193 NDSNyvVKGNARLPVkWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
399-597 1.42e-14

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: 74.62  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVylCYDVD-TGRELASKQVQFD-----PDSPETS-----------KEVSALECEIQLLKNLQHERIVQYYGC 461
Cdd:cd14067   1 LGQGGSGTV--IYRARyQGQPVAVKRFHIKkckkrTDGSADTmlkhlraadamKNFSEFRQEASMLHSLQHPCIVYLIGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 462 lrdrAEKTLTIFMEYMPGGSVKDQLK------AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDS----- 530
Cdd:cd14067  79 ----SIHPLCFALELAPLGSLNTVLEenhkgsSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVWSldvqe 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 531 AGNVKLGDFGASKRlqticMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 597
Cdd:cd14067 155 HINIKLSDYGISRQ-----SFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRP 216
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
75-151 1.44e-14

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 69.15  E-value: 1.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767     75 DVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFG---QPLDLHYMNNELS-ILLKNQDDLDKAIDILDRSSSmKSLRIL 150
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGldnQSFTLKYQDEDGDlVSLTSDEDLEEAIEEYDSLGS-KKLRLH 79

                   .
gi 42794767    151 L 151
Cdd:smart00666  80 V 80
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
394-606 1.45e-14

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: 74.29  E-value: 1.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGREL---ASKQVQFDPDSPETSKEVsaLEcEIQLLKNLQHERIVQYYG-CLrdraEKT 469
Cdd:cd05109  10 KKVKVLGSGAFGTVYKGIWIPDGENVkipVAIKVLRENTSPKANKEI--LD-EAYVMAGVGSPYVCRLLGiCL----TST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKA-YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL--- 545
Cdd:cd05109  83 VQLVTQLMPYGCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLdid 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 546 QTICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPpwaeYEAMAA 606
Cdd:cd05109 163 ETEYHADGGKVPIK----WMALESILHRRFTHQSDVWSYGVTVWELMTfgAKP----YDGIPA 217
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
397-595 1.63e-14

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: 75.51  E-value: 1.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF--- 473
Cdd:cd07874  23 KPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYR---ELVLMKCVNHKNIISLLNVFT--PQKSLEEFqdv 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 ---MEYMPGGSVK-DQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd07874  98 ylvMELMDANLCQvIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 550 MsgtgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEK 595
Cdd:cd07874 174 M----MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHK 215
PB1 pfam00564
PB1 domain;
75-151 2.81e-14

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 68.47  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    75 DVRIKFEHNGE-RRIIAFSRPVKYEDVEHKVTTVFGQP---LDLHYMNNELS-ILLKNQDDLDKAIDILdRSSSMKSLRI 149
Cdd:pfam00564   1 TVRLKLRYGGGiRRFLSVSRGISFEELRALVEQRFGLDdvdFKLKYPDEDGDlVSLTSDEDLEEALEEA-RSLGSKSLRL 79

                  ..
gi 42794767   150 LL 151
Cdd:pfam00564  80 HV 81
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
396-593 3.16e-14

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: 73.46  E-value: 3.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYLCYDVD-TGR----ELASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAekt 469
Cdd:cd05045   5 GKTLGEGEFGKVVKATAFRlKGRagytTVAVKMLK----ENASSSELRDLLSEFNLLKQVNHPHVIKLYGaCSQDGP--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLK-------AY-----------------GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGAN 525
Cdd:cd05045  78 LLLIVEYAKYGSLRSFLResrkvgpSYlgsdgnrnssyldnpdeRALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARN 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 526 ILRDSAGNVKLGDFGASKRLQTicMSGTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05045 158 VLVAEGRKMKISDFGLSRDVYE--EDSYVKRSKGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 224
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
398-642 3.20e-14

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: 74.35  E-value: 3.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQV----QFDPDSPETSKEVSAL-ECEIQLLKNLQHERIVQYYgclrdraEKTLTI 472
Cdd:cd14225  50 VIGKGSFGQVVKALDHKTNEHVAIKIIrnkkRFHHQALVEVKILDALrRKDRDNSHNVIHMKEYFYF-------RNHLCI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMpGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGASkrlqti 548
Cdd:cd14225 123 TFELL-GMNLYELIKKnnFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVIDFGSS------ 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 549 CMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPtnpqlPSHISE 625
Cdd:cd14225 196 CYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPgenEVEQLACIMEVLGLP-----PPELIE 270
                       250
                ....*....|....*..
gi 42794767 626 HGRDflRRIFVEARQRP 642
Cdd:cd14225 271 NAQR--RRLFFDSKGNP 285
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
397-600 3.99e-14

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: 73.41  E-value: 3.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFMEY 476
Cdd:cd14026   3 RYLSRGAFGTVSRARHADWRVTVAIKCLKLD--SPVGDSERNCLLKEAEILHKARFSYILPILGICNE--PEFLGIVTEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLKA---YGALTESVTRKYTRQILEGMSYLHsNM---IVHRDIKGANILRDSAGNVKLGDFGASKRLQTICM 550
Cdd:cd14026  79 MTNGSLNELLHEkdiYPDVAWPLRLRILYEIALGVNYLH-NMsppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSIS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 551 SGTGMRSVT--GTPYWMSPEVISGEGYGR---KADVWSLGCTVVEMLTEKPPWAE 600
Cdd:cd14026 158 QSRSSKSAPegGTIIYMPPEEYEPSQKRRasvKHDIYSYAIIMWEVLSRKIPFEE 212
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
399-585 6.53e-14

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: 72.41  E-value: 6.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQF----DPDSPETSKEvsaLECEIQLLKNLQHERIVQYYG-CLRDraEKTLTIF 473
Cdd:cd05048  13 LGEGAFGKVYKGELLGPSSEESAISVAIktlkENASPKTQQD---FRREAELMSDLQHPNIVCLLGvCTKE--QPQCMLF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 mEYMP----------------GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLG 537
Cdd:cd05048  88 -EYMAhgdlheflvrhsphsdVGVSSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKIS 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42794767 538 DFGASKRLqticMSGTGMRSVTGTPY---WMSPEVISgegYGR---KADVWSLG 585
Cdd:cd05048 167 DFGLSRDI----YSSDYYRVQSKSLLpvrWMPPEAIL---YGKfttESDVWSFG 213
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
398-655 7.99e-14

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: 72.10  E-value: 7.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYlcYDVDTGRELASKQVQFDPDSPETSK-EVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFmEY 476
Cdd:cd05043  13 LLQEGTFGRIF--HGILRDEKGKEEEVLVKTVKDHASEiQVTMLLQESSLLYGLSHQNLLPILHVCIEDGEKPMVLY-PY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 477 MPGGSVKDQLK--------AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL--- 545
Cdd:cd05043  90 MNWGNLKLFLQqcrlseanNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfpm 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAE---YEAMAAI---FKIAtQPTN-P 617
Cdd:cd05043 170 DYHCLGDNENRPIK----WMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEidpFEMAAYLkdgYRLA-QPINcP 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 618 qlpshisehgrDFLRRIF-----VEARQRPSAEEL---LTHHFAQL 655
Cdd:cd05043 245 -----------DELFAVMaccwaLDPEERPSFQQLvqcLTDFHAQL 279
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
397-651 8.18e-14

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: 72.30  E-value: 8.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDvdTGRELASKQvqFdpdspETSKEVSAL-ECEIQLLKNLQHERIVQYYGC-LRDRAEKT-LTIF 473
Cdd:cd14056   1 KTIGKGRYGEVWLGKY--RGEKVAVKI--F-----SSRDEDSWFrETEIYQTVMLRHENILGFIAAdIKSTGSWTqLWLI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKaYGALTESVTRKYTRQILEGMSYLHSNM--------IVHRDIKGANILRDSAGNVKLGDFG-ASKR 544
Cdd:cd14056  72 TEYHEHGSLYDYLQ-RNTLDTEEALRLAYSAASGLAHLHTEIvgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGlAVRY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 LQTICMSGTGMRSVTGTPYWMSPEVISG-------EGYgRKADVWSLGCTVVEML--TE--------KPPwaeYEAMAai 607
Cdd:cd14056 151 DSDTNTIDIPPNPRVGTKRYMAPEVLDDsinpksfESF-KMADIYSFGLVLWEIArrCEiggiaeeyQLP---YFGMV-- 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42794767 608 fkiatqPTNPQLpshisehgrDFLRRIFVEARQRPSAEELLTHH 651
Cdd:cd14056 225 ------PSDPSF---------EEMRKVVCVEKLRPPIPNRWKSD 253
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
441-642 8.59e-14

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: 72.47  E-value: 8.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 441 ECEIQLLKNLQHERIVQYY-GCLRDRA-EKTLTIFMEYMPGGSVKDQLKAYGALTESVTRkYTRQILEGMSYLHSNM--- 515
Cdd:cd13998  37 EKEIYRTPMLKHENILQFIaADERDTAlRTELWLVTAFHPNGSL*DYLSLHTIDWVSLCR-LALSVARGLAHLHSEIpgc 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 516 ------IVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSGTGMRSV-----TGTPYWMSPEVISG-------EGYgR 577
Cdd:cd13998 116 tqgkpaIAHRDLKSKNILVKNDGTCCIADFGLAVRLS----PSTGEEDNanngqVGTKRYMAPEVLEGainlrdfESF-K 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 578 KADVWSLGCTVVEMLTE----KPPWAEYEAmaaifkiatqPTNPQLPSHISehgRDFLRRIFVEARQRP 642
Cdd:cd13998 191 RVDIYAMGLVLWEMASRctdlFGIVEEYKP----------PFYSEVPNHPS---FEDMQEVVVRDKQRP 246
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
399-596 1.19e-13

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: 71.92  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYlcydvdtgRELASKQVQFDPDSP---ETSKEVSALECEIQLL------KNLQHERIVQYYGCLrDRAEKT 469
Cdd:cd05061  14 LGQGSFGMVY--------EGNARDIIKGEAETRvavKTVNESASLRERIEFLneasvmKGFTCHHVVRLLGVV-SKGQPT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIfMEYMPGGSVKDQLKAYGALTESVTRK----------YTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDF 539
Cdd:cd05061  85 LVV-MELMAHGDLKSYLRSLRPEAENNPGRppptlqemiqMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDF 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794767 540 GASKRLQTICM---SGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEM--LTEKP 596
Cdd:cd05061 164 GMTRDIYETDYyrkGGKGLLPVR----WMAPESLKDGVFTTSSDMWSFGVVLWEItsLAEQP 221
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
396-612 1.24e-13

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: 71.58  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydvdTGR---ELASKQVQFDPDSPEtskEVSALECEIQLLKNLQHERIVQYYG-CLRdraEKTLT 471
Cdd:cd14153   5 GELIGKGRFGQVY------HGRwhgEVAIRLIDIERDNEE---QLKAFKREVMAYRQTRHENVVLFMGaCMS---PPHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGASKrLQTICM 550
Cdd:cd14153  73 IITSLCKGRTLYSVVRdAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFT-ISGVLQ 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794767 551 SGT---GMRSVTGTPYWMSPEVI---SGEG------YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT 612
Cdd:cd14153 151 AGRredKLRIQSGWLCHLAPEIIrqlSPETeedklpFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGS 224
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
480-653 1.42e-13

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 69.35  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    480 GSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVklgdfGASKRLQTIcmsgtgmrsv 558
Cdd:smart00750   1 VSLADILEVRGRpLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKLDGSV-----AFKTPEQSR---------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767    559 tGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKI------ATQPTNPQLPSHISEHG--RDF 630
Cdd:smart00750  66 -PDPYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEIllngmpADDPRDRSNLEGVSAARsfEDF 144
                          170       180
                   ....*....|....*....|....
gi 42794767    631 LRRIFVEARQ-RPSAEELLTHHFA 653
Cdd:smart00750 145 MRLCASRLPQrREAANHYLAHCRA 168
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
397-650 1.57e-13

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: 71.64  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVY---LCYDVDTGRELASKQVqFDPDspetskEVSALECEIQLLK--NLQHERIVQYYGC--LRDRAEKT 469
Cdd:cd14055   1 KLVGKGRFAEVWkakLKQNASGQYETVAVKI-FPYE------EYASWKNEKDIFTdaSLKHENILQFLTAeeRGVGLDRQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYgALTESVTRKYTRQILEGMSYLHSNM---------IVHRDIKGANILRDSAGNVKLGDFG 540
Cdd:cd14055  74 YWLITAYHENGSLQDYLTRH-ILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 541 ASKRL----QTICMSGTGMrsvTGTPYWMSPEVISG-------EGYgRKADVWSLGCTVVEMLTekppwaEYEAMAAIfk 609
Cdd:cd14055 153 LALRLdpslSVDELANSGQ---VGTARYMAPEALESrvnledlESF-KQIDVYSMALVLWEMAS------RCEASGEV-- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42794767 610 iatQPTNPQLPSHISEH-GRDFLRRIFVEARQRPS-AEELLTH 650
Cdd:cd14055 221 ---KPYELPFGSKVRERpCVESMKDLVLRDRGRPEiPDSWLTH 260
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
393-598 1.59e-13

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 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: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 71.24  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVdtgreLASKQVQFDPDSPETSKEVsaLECEIQLLKNLQ-HERIVQYYGCLRDraEKTLT 471
Cdd:cd14129   2 WKVLRKIGGGGFGEIYDALDL-----LTRENVALKVESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--DRFNY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEyMPGGSVKD--QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRL 545
Cdd:cd14129  73 VVMQ-LQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQF 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 546 QTICMSGTGMRSVT---GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd14129 152 TNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 207
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
396-647 1.68e-13

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: 71.03  E-value: 1.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVY---LCYDVDTGRELASKQVQFDPdspETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAEKTLT 471
Cdd:cd05035   4 GKILGEGEFGSVMeaqLKQDDGSQLKVAVKTMKVDI---HTYSEIEEFLSEAACMKDFDHPNVMRLIGvCFTASDLNKPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFM---EYMPGGSVKDQLKA--YGALTESVTR----KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 542
Cdd:cd05035  81 SPMvilPFMKHGDLHSYLLYsrLGGLPEKLPLqtllKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 543 KRLqticMSGTGMRS--VTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAmAAIFKIATQPTNPQ 618
Cdd:cd05035 161 RKI----YSGDYYRQgrISKMPVkWIALESLADNVYTSKSDVWSFGVTMWEIATRgQTPYPGVEN-HEIYDYLRNGNRLK 235
                       250       260       270
                ....*....|....*....|....*....|
gi 42794767 619 LPSHISEHGRDFLRRIF-VEARQRPSAEEL 647
Cdd:cd05035 236 QPEDCLDEVYFLMYFCWtVDPKDRPTFTKL 265
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
397-595 1.75e-13

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: 72.38  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRAE----KTLTI 472
Cdd:cd07875  30 KPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYR---ELVLMKCVNHKNIIGLLNVFTPQKSleefQDVYI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMPGGSVK-DQLKaygaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMs 551
Cdd:cd07875 107 VMELMDANLCQvIQME----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFM- 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42794767 552 gtgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEK 595
Cdd:cd07875 182 ---MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGG 222
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
393-592 1.98e-13

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: 71.98  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYGCLRdrAEKTLTI 472
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYR---ELVLLKCVNHKNIISLLNVFT--PQKSLEE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 F------MEYMPGGSVKdqlKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ 546
Cdd:cd07876  98 FqdvylvMELMDANLCQ---VIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAC 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42794767 547 TICMsgtgMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 592
Cdd:cd07876 175 TNFM----MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELV 216
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
394-593 2.74e-13

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: 70.98  E-value: 2.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRV-----YLCYDVDTGRELASKQVQFDpdspETSKEVSALECEIQLLKNL-QHERIVQYYG-ClrDRA 466
Cdd:cd05054  10 KLGKPLGRGAFGKViqasaFGIDKSATCRTVAVKMLKEG----ATASEHKALMTELKILIHIgHHLNVVNLLGaC--TKP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 467 EKTLTIFMEYMPGGSVKDQLKA----YGALTESVTRK----------------------YTRQILEGMSYLHSNMIVHRD 520
Cdd:cd05054  84 GGPLMVIVEFCKFGNLSNYLRSkreeFVPYRDKGARDveeeedddelykepltledlicYSFQVARGMEFLASRKCIHRD 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 521 IKGANILRDSAGNVKLGDFGASKRLQT---ICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05054 164 LAARNILLSENNVVKICDFGLARDIYKdpdYVRKGDARLPLK----WMAPESIFDKVYTTQSDVWSFGVLLWEIFS 235
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
443-593 2.83e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 71.95  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  443 EIQLLKNLQHERIVQYYGCLrDRAEKTLTIFMEYmpggsvKDQLKAYGALTESVT----RKYTRQILEGMSYLHSNMIVH 518
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTF-TYNKFTCLILPRY------KTDLYCYLAAKRNIAicdiLAIERSVLRAIQYLHENRIIH 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767  519 RDIKGANILRDSAGNVKLGDFGASkrLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:PHA03212 206 RDIKAENIFINHPGDVCLGDFGAA--CFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMAT 278
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
394-593 3.03e-13

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: 70.87  E-value: 3.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 394 RRGKLLGQGAFGRVYLCYDVDTGREL---ASKQVQFDPDSPETSKEVSAlecEIQLLKNLQHERIVQYYG-CLrdraEKT 469
Cdd:cd05110  10 KRVKVLGSGAFGTVYKGIWVPEGETVkipVAIKILNETTGPKANVEFMD---EALIMASMDHPHLVRLLGvCL----SPT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQ-- 546
Cdd:cd05110  83 IQLVTQLMPHGCLLDYVHEHkDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEgd 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794767 547 --TICMSGTGMrsvtgTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05110 163 ekEYNADGGKM-----PIKWMALECIHYRKFTHQSDVWSYGVTIWELMT 206
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
397-648 3.26e-13

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: 70.19  E-value: 3.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDvdTGRELASKQVQFDPDSPETSKE---VSALECEIQLLKNLQHERIVQYYGCLRDrAEKTLTIf 473
Cdd:cd05046  11 TTLGRGEFGEVFLAKA--KGIEEEGGETLVLVKALQKTKDenlQSEFRRELDMFRKLSHKNVVRLLGLCRE-AEPHYMI- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAYGALTESVTRKYTR---------QILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKr 544
Cdd:cd05046  87 LEYTDLGDLKQFLRATKSKDEKLKPPPLStkqkvalctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSK- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 545 lqticmsgtgmrsvtgTPY---------------WMSPEVISGEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEAMAAIF 608
Cdd:cd05046 166 ----------------DVYnseyyklrnaliplrWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLN 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42794767 609 KIATQPTNPQLPSHISEHGRDFLRRIF-VEARQRPSAEELL 648
Cdd:cd05046 230 RLQAGKLELPVPEGCPSRLYKLMTRCWaVNPKDRPSFSELV 270
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
399-593 3.41e-13

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: 70.14  E-value: 3.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYG-CLRdraEKTLTIFMEYM 477
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLK------EDTMEVEEFLKEAAVMKEIKHPNLVQLLGvCTR---EPPFYIITEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 478 PGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLqticMSGTGM 555
Cdd:cd05052  85 PYGNLLDYLREcnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS-RL----MTGDTY 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42794767 556 RSVTGTPY---WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05052 160 TAHAGAKFpikWTAPESLAYNKFSIKSDVWAFGVLLWEIAT 200
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
393-634 5.45e-13

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 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: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 69.29  E-value: 5.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 393 WRRGKLLGQGAFGRVYLCYDVdtgreLASKQVQFDPDSPETSKEVsaLECEIQLLKNLQ-HERIVQYYGCLRDraEKTLT 471
Cdd:cd14130   2 WKVLKKIGGGGFGEIYEAMDL-----LTRENVALKVESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--EKFNY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEyMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRL 545
Cdd:cd14130  73 VVMQ-LQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMRSVT---GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH 622
Cdd:cd14130 152 TNTTGEVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKH 231
                       250
                ....*....|..
gi 42794767 623 ISEHGRDFLRRI 634
Cdd:cd14130 232 MPSEFHLFLDHI 243
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
397-596 5.84e-13

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: 70.93  E-value: 5.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEvsalecEIQLLKNLQHE------RIVQYYGCLRDRAEKTL 470
Cdd:cd14224  71 KVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAE------EIRILEHLKKQdkdntmNVIHMLESFTFRNHICM 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAG--NVKLGDFGAS----KR 544
Cdd:cd14224 145 TFELLSMNLYELIKKNKFQG-FSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGrsGIKVIDFGSScyehQR 223
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42794767 545 LQTICMSgtgmrsvtgtPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKP 596
Cdd:cd14224 224 IYTYIQS----------RFYRAPEVILGARYGMPIDMWSFGCILAELLTGYP 265
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
399-647 7.43e-13

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: 69.64  E-value: 7.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCyDVDTGRELASKQVQFD--PDSPeTSKEVSALEC------------EIQLLKNLQHERIVQYYG-CLr 463
Cdd:cd05095  13 LGEGQFGEVHLC-EAEGMEKFMDKDFALEvsENQP-VLVAVKMLRAdanknarndflkEIKIMSRLKDPNIIRLLAvCI- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 464 drAEKTLTIFMEYMPGGSVKDQLKAY----------GALTESVT--RKYTRQILEGMSYLHSNMIVHRDIKGANILRDSA 531
Cdd:cd05095  90 --TDDPLCMITEYMENGDLNQFLSRQqpegqlalpsNALTVSYSdlRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 532 GNVKLGDFGASKRLqticMSGTGMRsVTGTPY----WMSPEVISGEGYGRKADVWSLGCTVVEMLT---EKPpwaeyeam 604
Cdd:cd05095 168 YTIKIADFGMSRNL----YSGDYYR-IQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETLTfcrEQP-------- 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794767 605 aaifkiATQPTNPQLPSHISEHGRDFLRRIFV--------------------EARQRPSAEEL 647
Cdd:cd05095 235 ------YSQLSDEQVIENTGEFFRDQGRQTYLpqpalcpdsvyklmlscwrrDTKDRPSFQEI 291
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
397-598 9.41e-13

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: 68.94  E-value: 9.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRE---LASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF 473
Cdd:cd05033  10 KVIGGGEFGEVCSGSLKLPGKKeidVAIKTLK----SGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVT--KSRPVMIV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLhSNM-IVHRDIKGANILRDSAGNVKLGDFGASKRLQTIcmS 551
Cdd:cd05033  84 TEYMENGSLDKFLRENdGKFTVTQLVGMLRGIASGMKYL-SEMnYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDS--E 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 552 GTGMRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPW 598
Cdd:cd05033 161 ATYTTKGGKIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEVMSygERPYW 210
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
431-651 1.13e-12

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: 68.89  E-value: 1.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 431 PETSKEVSALECEIQLLKNLQHERIVQYYGclrdrAEKTLT-------IFMEYMPGGSVKDQLKAYgALTESVTRKYTRQ 503
Cdd:cd14053  27 PLQEKQSWLTEREIYSLPGMKHENILQFIG-----AEKHGEsleaeywLITEFHERGSLCDYLKGN-VISWNELCKIAES 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 504 ILEGMSYLHSNM----------IVHRDIKGANILRDSAGNVKLGDFGASKRLQT-ICMSGTGMRsvTGTPYWMSPEVISG 572
Cdd:cd14053 101 MARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPgKSCGDTHGQ--VGTRRYMAPEVLEG 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 573 E-GYGRKA----DVWSLGCTVVEMLTEkppwaeyeamaaiFKIATQP-TNPQLP------SHISehgRDFLRRIFVEARQ 640
Cdd:cd14053 179 AiNFTRDAflriDMYAMGLVLWELLSR-------------CSVHDGPvDEYQLPfeeevgQHPT---LEDMQECVVHKKL 242
                       250
                ....*....|.
gi 42794767 641 RPSAEELLTHH 651
Cdd:cd14053 243 RPQIRDEWRKH 253
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
396-585 1.18e-12

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: 68.42  E-value: 1.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydvdTGRELASKQvqfdPDSPETSKEVSALEC------EIQLLKNLQHERIVQYYGCLRDRaeKT 469
Cdd:cd05084   1 GERIGRGNFGEVF------SGRLRADNT----PVAVKSCRETLPPDLkakflqEARILKQYSHPNIVRLIGVCTQK--QP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIFMEYMPGGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTI 548
Cdd:cd05084  69 IYIVMELVQGGDFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDG 148
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42794767 549 CMSGT-GMRSVtgtPY-WMSPEVISGEGYGRKADVWSLG 585
Cdd:cd05084 149 VYAATgGMKQI---PVkWTAPEALNYGRYSSESDVWSFG 184
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
397-598 1.20e-12

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: 68.35  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVylCY---DVDTGREL--ASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLT 471
Cdd:cd05066  10 KVIGAGEFGEV--CSgrlKLPGKREIpvAIKTLK----AGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVT--RSKPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICM 550
Cdd:cd05066  82 IVTEYMENGSLDAFLRKHdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPE 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPW 598
Cdd:cd05066 162 AAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSygERPYW 211
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
398-632 1.64e-12

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: 68.90  E-value: 1.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 398 LLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSkevsalECEIQLLKNLQHER-----IVQYYGCLRDRAEKTLTI 472
Cdd:cd14229   7 FLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQG------QIEVGILARLSNENadefnFVRAYECFQHRNHTCLVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMEYMpggSVKDQLK--AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI-LRDSAGN---VKLGDFG-ASKRL 545
Cdd:cd14229  81 EMLEQ---NLYDFLKqnKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENImLVDPVRQpyrVKVIDFGsASHVS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 546 QTICMSGTGMRsvtgtpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKP--PWA-EYEAMAAIFKIATQPTNpQLPSH 622
Cdd:cd14229 158 KTVCSTYLQSR------YYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPlyPGAlEYDQIRYISQTQGLPGE-QLLNV 230
                       250
                ....*....|
gi 42794767 623 ISEHGRDFLR 632
Cdd:cd14229 231 GTKTSRFFCR 240
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
447-652 2.16e-12

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: 68.12  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 447 LKNLQHERIVQYYGCLRDRAEKT-----------LTIFMEYMPGGSVKDQLKAYGaLTESVTRKYTRQILEGMSYLHSNM 515
Cdd:cd14011  56 LTRLRHPRILTVQHPLEESRESLafatepvfaslANVLGERDNMPSPPPELQDYK-LYDVEIKYGLLQISEALSFLHNDV 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 516 -IVHRDIKGANILRDSAGNVKLGDFG-------ASKRLQTICMSGTGMRSV-TGTPYWMSPEVISGEGYGRKADVWSLGC 586
Cdd:cd14011 135 kLVHGNICPESVVINSNGEWKLAGFDfcisseqATDQFPYFREYDPNLPPLaQPNLNYLAPEYILSKTCDPASDMFSLGV 214
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 587 TVVEMLTE-KPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHGRDFLRR-IFVEARQRPSAEELLTHHF 652
Cdd:cd14011 215 LIYAIYNKgKPLFDCVNNLLSYKKNSNQLRQLSLSllEKVPEELRDHVKTlLNVTPEVRPDAEQLSKIPF 284
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
76-151 2.41e-12

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 62.68  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  76 VRIKFEHNGE-RRIIAFSRPVKYEDVEHKVTTVFGQP---LDLHYMNNELS-ILLKNQDDLDKAIDILDRSSSmKSLRIL 150
Cdd:cd05992   1 VRVKVKYGGEiRRFVVVSRSISFEDLRSKIAEKFGLDavsFKLKYPDEDGDlVTISSDEDLEEAIEEARRSGS-KKLRLF 79

                .
gi 42794767 151 L 151
Cdd:cd05992  80 V 80
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
399-596 3.25e-12

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: 67.37  E-value: 3.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYlcydvdtgRELASKQVQFDPDSP---ETSKEVSALECEIQLL------KNLQHERIVQYYGCLrDRAEKT 469
Cdd:cd05062  14 LGQGSFGMVY--------EGIAKGVVKDEPETRvaiKTVNEAASMRERIEFLneasvmKEFNCHHVVRLLGVV-SQGQPT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 470 LTIfMEYMPGGSVKDQLKAYGALTESVTR----------KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDF 539
Cdd:cd05062  85 LVI-MELMTRGDLKSYLRSLRPEMENNPVqappslkkmiQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDF 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 540 GASKRLQTICMSGTGMRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEM--LTEKP 596
Cdd:cd05062 164 GMTRDIYETDYYRKGGKGLLPV-RWMSPESLKDGVFTTYSDVWSFGVVLWEIatLAEQP 221
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
399-652 4.00e-12

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: 67.65  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCyDVDTGRELASKQVQFD---------------PDSPETSKevSALECEIQLLKNLQHERIVQYYG-CL 462
Cdd:cd05096  13 LGEGQFGEVHLC-EVVNPQDLPTLQFPFNvrkgrpllvavkilrPDANKNAR--NDFLKEVKILSRLKDPNIIRLLGvCV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 463 RDraeKTLTIFMEYMPGGSVKDQLKAYG-------------------ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKG 523
Cdd:cd05096  90 DE---DPLCMITEYMENGDLNQFLSSHHlddkeengndavppahclpAISYSSLLHVALQIASGMKYLSSLNFVHRDLAT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 524 ANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPWAEY 601
Cdd:cd05096 167 RNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPI-RWMAWECILMGKFTTASDVWAFGVTLWEILMlcKEQPYGEL 245
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794767 602 eamaaifkiatqpTNPQLPSHISEHGRDFLRRIFV--------------------EARQRPSAEELltHHF 652
Cdd:cd05096 246 -------------TDEQVIENAGEFFRDQGRQVYLfrpppcpqglyelmlqcwsrDCRERPSFSDI--HAF 301
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
397-593 5.32e-12

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: 66.67  E-value: 5.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYlcydvdtgrELASKQVqFDPDSPETSKEVSALE------------CEIQLLKNLQHERIVQYYG-CLR 463
Cdd:cd05044   1 KFLGSGAFGEVF---------EGTAKDI-LGDGSGETKVAVKTLRkgatdqekaeflKEAHLMSNFKHPNILKLLGvCLD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 464 DRAEktlTIFMEYMPGGSVKDQLKAygALTESVTRKYTR---------QILEGMSYLHSNMIVHRDIKGANILRDSAGN- 533
Cdd:cd05044  71 NDPQ---YIILELMEGGDLLSYLRA--ARPTAFTPPLLTlkdllsicvDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYr 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794767 534 ---VKLGDFGASKRLQT---ICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05044 146 ervVKIGDFGLARDIYKndyYRKEGEGLLPVR----WMAPESLVDGVFTTQSDVWAFGVLMWEILT 207
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
399-593 5.87e-12

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: 66.57  E-value: 5.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCY----DVDTGRELASKQVQfDPDSPETSKEvsaLECEIQLLKNLQHERIVQYYGCLRDraEKTLTIFM 474
Cdd:cd05090  13 LGECAFGKIYKGHlylpGMDHAQLVAIKTLK-DYNNPQQWNE---FQQEASLMTELHHPNIVCLLGVVTQ--EQPVCMLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAYGALT-------ESVTRKYTR----------QILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLG 537
Cdd:cd05090  87 EFMNQGDLHEFLIMRSPHSdvgcssdEDGTVKSSLdhgdflhiaiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKIS 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 538 DFGASKRLQT---ICMSGTGMRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd05090 167 DLGLSREIYSsdyYRVQNKSLLPIR----WMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 221
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
399-647 7.81e-12

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: 66.07  E-value: 7.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCyDVDTGRELAS---KQVQFDPDSPETSKEVSalecEIQLLKNLQHERIVQyygCLRDRAEKT-LTIFM 474
Cdd:cd05042   3 IGNGWFGKVLLG-EIYSGTSVAQvvvKELKASANPKEQDTFLK----EGQPYRILQHPNILQ---CLGQCVEAIpYLLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 475 EYMPGGSVKDQLKAY--GALTESVTRKYTRQILE---GMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTIC 549
Cdd:cd05042  75 EFCDLGDLKAYLRSEreHERGDSDTRTLQRMACEvaaGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKED 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 550 MSGTGMRSVtgTPY-WMSPEVIsGEGYG--------RKADVWSLGCTVVEML----TEKPPWAEYEAMAaiFKIATQPTN 616
Cdd:cd05042 155 YIETDDKLW--FPLrWTAPELV-TEFHDrllvvdqtKYSNIWSLGVTLWELFengaQPYSNLSDLDVLA--QVVREQDTK 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 42794767 617 ---PQLPSHISEHGRDFLRRIFVEARQRPSAEEL 647
Cdd:cd05042 230 lpkPQLELPYSDRWYEVLQFCWLSPEQRPAAEDV 263
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
406-598 8.12e-12

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 66.82  E-value: 8.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 406 RVYLCYDVDTGRELASKQVQFDPDSPEtskEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMPGGSVKDQ 485
Cdd:cd08226  15 SVYLARHTPTGTLVTVKITNLDNCSEE---HLKALQNEVVLSHFFRHPNIMTHWTVFTEGSW--LWVISPFMAYGSARGL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 486 LKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFgasKRLQTICMSGTGMRSVTGTPY 563
Cdd:cd08226  90 LKTYfpEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGL---SHLYSMVTNGQRSKVVYDFPQ 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42794767 564 -------WMSPEVISGE--GYGRKADVWSLGCTVVEMLTEKPPW 598
Cdd:cd08226 167 fstsvlpWLSPELLRQDlhGYNVKSDIYSVGITACELARGQVPF 210
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
399-592 8.42e-12

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: 66.81  E-value: 8.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQFD-PDSPETS-KEVSALEcEIQLlknlQHERIVQYYGCLRDR----------- 465
Cdd:cd13977   8 VGRGSYGVVYEAVVRRTGARVAVKKIRCNaPENVELAlREFWALS-SIQR----QHPNVIQLEECVLQRdglaqrmshgs 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 466 ---------------AEKT--------LTIFMEYMPGGSVKDQLkaygaLTESVTRK----YTRQILEGMSYLHSNMIVH 518
Cdd:cd13977  83 sksdlylllvetslkGERCfdprsacyLWFVMEFCDGGDMNEYL-----LSRRPDRQtntsFMLQLSSALAFLHRNQIVH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 519 RDIKGANIL---RDSAGNVKLGDFGASKrlqtICmSGTGMR-------------SVTGTPYWMSPEVISGEgYGRKADVW 582
Cdd:cd13977 158 RDLKPDNILishKRGEPILKVADFGLSK----VC-SGSGLNpeepanvnkhflsSACGSDFYMAPEVWEGH-YTAKADIF 231
                       250
                ....*....|
gi 42794767 583 SLGCTVVEML 592
Cdd:cd13977 232 ALGIIIWAMV 241
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
396-624 1.23e-11

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: 65.76  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVYlcydvdTGR---ELASKQVQFDPDSPETSKevsALECEIQLLKNLQHERIVQYYG-CLRdraEKTLT 471
Cdd:cd14152   5 GELIGQGRWGKVH------RGRwhgEVAIRLLEIDGNNQDHLK---LFKKEVMNYRQTRHENVVLFMGaCMH---PPHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 472 IFMEYMPGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGaskrlqTICM 550
Cdd:cd14152  73 IITSFCKGRTLYSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFG------LFGI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 551 SGT---GMRS-----VTGTPYWMSPEVISGEGYGRK---------ADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQ 613
Cdd:cd14152 146 SGVvqeGRREnelklPHDWLCYLAPEIVREMTPGKDedclpfskaADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSG 225
                       250
                ....*....|.
gi 42794767 614 PTNPQLPSHIS 624
Cdd:cd14152 226 EGMKQVLTTIS 236
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
396-647 1.35e-11

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: 65.41  E-value: 1.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRVY---LCYDvDTGRELASKQVQFdpdSPETSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRAEKTL- 470
Cdd:cd05075   5 GKTLGEGEFGSVMegqLNQD-DSVLKVAVKTMKI---AICTRSEMEDFLSEAVCMKEFDHPNVMRLIGvCLQNTESEGYp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 --TIFMEYMPGGSVKDQLkAYGALTES-------VTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 541
Cdd:cd05075  81 spVVILPFMKHGDLHSFL-LYSRLGDCpvylptqMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 542 SKRLqticMSGTGMRS--VTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPWAEYEAmAAIFKIATQPTNP 617
Cdd:cd05075 160 SKKI----YNGDYYRQgrISKMPVkWIAIESLADRVYTTKSDVWSFGVTMWEIATRgQTPYPGVEN-SEIYDYLRQGNRL 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 42794767 618 QLPSHISEHGRDFLRRIF-VEARQRPSAEEL 647
Cdd:cd05075 235 KQPPDCLDGLYELMSSCWlLNPKDRPSFETL 265
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
396-593 1.62e-11

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: 65.34  E-value: 1.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 396 GKLLGQGAFGRV---YLCYDVDTGRELASKQVQFDPDSpetSKEVSALECEIQLLKNLQHERIVQYYG-CLR---DRAEK 468
Cdd:cd14204  12 GKVLGEGEFGSVmegELQQPDGTNHKVAVKTMKLDNFS---QREIEEFLSEAACMKDFNHPNVIRLLGvCLEvgsQRIPK 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 469 TLTI--FMEYmpgGSVKDQL--KAYGALTESVTR----KYTRQILEGMSYLHSNMIVHRDIKGAN-ILRDSAgNVKLGDF 539
Cdd:cd14204  89 PMVIlpFMKY---GDLHSFLlrSRLGSGPQHVPLqtllKFMIDIALGMEYLSSRNFLHRDLAARNcMLRDDM-TVCVADF 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 540 GASKRLqticMSGTGMRS--VTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd14204 165 GLSKKI----YSGDYYRQgrIAKMPVkWIAVESLADRVYTVKSDVWAFGVTMWEIAT 217
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
443-650 1.62e-11

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: 65.31  E-value: 1.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 443 EIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMPGGSVKDQLKaygalTESVTR----KYT--RQILEGMSYLHSNMI 516
Cdd:cd14042  52 ELKHMRDLQHDNLTRFIGACVDPP--NICILTEYCPKGSLQDILE-----NEDIKLdwmfRYSliHDIVKGMHYLHDSEI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 517 V-HRDIKGANILRDSAGNVKLGDFGASKrLQTICMSGTGMRSVTGTPYWMSPEVISGEG---YG-RKADVWSLGCTVVEM 591
Cdd:cd14042 125 KsHGNLKSSNCVVDSRFVLKITDFGLHS-FRSGQEPPDDSHAYYAKLLWTAPELLRDPNpppPGtQKGDVYSFGIILQEI 203
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 592 LTEKPPWAEYEA----MAAIFKIATQPTNPQL-----PSHISEHGRDFLRRIFVE-ARQRPSAEELLTH 650
Cdd:cd14042 204 ATRQGPFYEEGPdlspKEIIKKKVRNGEKPPFrpsldELECPDEVLSLMQRCWAEdPEERPDFSTLRNK 272
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
501-590 1.70e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 66.84  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767  501 TRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKAD 580
Cdd:PHA03211 266 ARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARG-SWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVD 344
                         90
                 ....*....|
gi 42794767  581 VWSLGCTVVE 590
Cdd:PHA03211 345 IWSAGLVIFE 354
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
397-621 3.01e-11

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: 64.51  E-value: 3.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 397 KLLGQGAFGRVYLCYDVDTGRE---LASKQVQfdpdSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRdrAEKTLTIF 473
Cdd:cd05065  10 EVIGAGEFGEVCRGRLKLPGKReifVAIKTLK----SGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVT--KSRPVMII 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 474 MEYMPGGSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSG 552
Cdd:cd05065  84 TEFMENGALDSFLRQNdGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDP 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794767 553 TGMRSVTGT-PY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPW--AEYEAMAAIFKIATQPTNPQLPS 621
Cdd:cd05065 164 TYTSSLGGKiPIrWTAPEAIAYRKFTSASDVWSYGIVMWEVMSygERPYWdmSNQDVINAIEQDYRLPPPMDCPT 238
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
399-590 4.00e-11

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 64.87  E-value: 4.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVD-TGRELASKQVQfdpdspETSKEVSALECEIQLLKNLQHERIVQYYGCLR-----DRAEKTLTI 472
Cdd:cd14213  20 LGEGAFGKVVECIDHKmGGMHVAVKIVK------NVDRYREAARSEIQVLEHLNTTDPNSTFRCVQmlewfDHHGHVCIV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 473 FMeyMPGGSVKDQLKAYGALTESV--TRKYTRQILEGMSYLHSNMIVHRDIKGANIL---------------RDSA---- 531
Cdd:cd14213  94 FE--LLGLSTYDFIKENSFLPFPIdhIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyvvkynpkmkRDERtlkn 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42794767 532 GNVKLGDFGASKrlqticMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVE 590
Cdd:cd14213 172 PDIKVVDFGSAT------YDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIE 224
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
399-593 5.53e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 64.67  E-value: 5.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 399 LGQGAFGRVYLCYDVDTGRELASKQVQfdpdSPETSKEvSALEcEIQLLKNLQH--------ERIVQYYGCLRDRAEKTL 470
Cdd:cd14216  18 LGWGHFSTVWLSWDIQGKRFVAMKVVK----SAEHYTE-TALD-EIKLLKSVRNsdpndpnrEMVVQLLDDFKISGVNGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794767 471 TIFMEYMPGGS--VKDQLKA-YGALTESVTRKYTRQILEGMSYLHSN-MIVHRDIKGANIL--------RDSAG------ 532
Cdd:cd14216  92 HICMVFEVLGHhlLKWIIKSnYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILlsvneqyiRRLAAeatewq 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794767 533 ----------------NVKLGDFGASkrlqtiCMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLT 593
Cdd:cd14216 172 rnflvnplepknaeklKVKIADLGNA------CWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELAT 242
 
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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