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Conserved domains on  [gi|755537521|ref|XP_011247077|]
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kinase suppressor of Ras 1 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
441-719 0e+00

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: 621.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14152    1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKL 600
Cdd:cd14152   81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVQEGRRENELKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKE 680
Cdd:cd14152  161 PHDWLCYLAPEIVREMTPGKDEDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGEGMKQVLTTISLGKE 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 681 VGEILSACWAFDLQERPSFSLLMDMLERLPKLNRRLSHP 719
Cdd:cd14152  241 VTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRRLSHP 279
C1_KSR1 cd20872
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and ...
197-243 1.97e-31

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and similar proteins; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410422  Cd Length: 47  Bit Score: 116.30  E-value: 1.97e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 197 VTHRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPACR 243
Cdd:cd20872    1 VTHRFSTKSWLSQTCQVCQKSMMFGVKCKHCRLKCHNKCTKEAPACR 47
 
Name Accession Description Interval E-value
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
441-719 0e+00

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: 621.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14152    1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKL 600
Cdd:cd14152   81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVQEGRRENELKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKE 680
Cdd:cd14152  161 PHDWLCYLAPEIVREMTPGKDEDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGEGMKQVLTTISLGKE 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 681 VGEILSACWAFDLQERPSFSLLMDMLERLPKLNRRLSHP 719
Cdd:cd14152  241 VTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRRLSHP 279
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
442-706 1.42e-49

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 174.99  E-value: 1.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGegentkiKVAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREER 593
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVkISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  594 RENQLKLShdwLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGEgvrRVL 672
Cdd:pfam07714 160 KRGGGKLP---IKWMAPESLKDGK---------FTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLEDGY---RLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 755537521  673 ASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
442-706 1.07e-43

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 158.46  E-value: 1.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLeMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgvVREER 593
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVkISDFGL------SRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   594 RENQLKLSHDWLCY--LAPEIVREMIpgrdedqlpFSKAADVYAFG-TVW--YELQARDWPfkHQPAEALIWQIGSGEgv 668
Cdd:smart00219 154 DDDYYRKRGGKLPIrwMAPESLKEGK---------FTSKSDVWSFGvLLWeiFTLGEQPYP--GMSNEEVLEYLKNGY-- 220
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 755537521   669 rRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:smart00219 221 -RLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
C1_KSR1 cd20872
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and ...
197-243 1.97e-31

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and similar proteins; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410422  Cd Length: 47  Bit Score: 116.30  E-value: 1.97e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 197 VTHRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPACR 243
Cdd:cd20872    1 VTHRFSTKSWLSQTCQVCQKSMMFGVKCKHCRLKCHNKCTKEAPACR 47
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
443-732 3.02e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 105.59  E-value: 3.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQ-DHLKLFKKEVMNYRQTRHE-NVVLFMGACMNPPHLAIITSFCKG 520
Cdd:COG0515    3 RILRKLGEGSFGEVYLARDRKLVALKVLAKKLESKsKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEYVDG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDP--KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFGLFGISGVVREERREN 596
Cdd:COG0515   83 GSLEDLLKKIgrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrdGRVVKLIDFGLAKLLPDPGSTSSIP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDW-LCYLAPEIVREMIPGRDedqlpfSKAADVYAFGTVWYELQARDWPF---KHQPAEALIWQIGSGEGVRRVL 672
Cdd:COG0515  163 ALPSTSVGtPGYMAPEVLLGLSLAYA------SSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTPSLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 673 ASVS------LGKEVGEILSACWAFDLQERPS--FSLLMDMLERLPKLNRRLSHPGHFWKSADRWRSR 732
Cdd:COG0515  237 SPLSpsnpelISKAASDLLKKLLAKDPKNRLSssSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSL 304
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
443-650 3.14e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 68.31  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVhrgrwhgevaiRLLEMDGHNQDH-LKLFKK-EVMNYRQTRHEN-------------VVLFMGACMN 507
Cdd:PTZ00263  21 EMGETLGTGSFGRV-----------RIAKHKGTGEYYaIKCLKKrEILKMKQVQHVAqeksilmelshpfIVNMMCSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 508 PPHLAIITSFCKGRTLHSFVRDP-KTSLDINKTrqIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgi 585
Cdd:PTZ00263  90 ENRVYFLLEFVVGGELFTHLRKAgRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPENLLLDNkGHVKVTDFGF--- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 586 SGVVREERREnqlklshdwLC----YLAPEIVREmiPGRDedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:PTZ00263 165 AKKVPDRTFT---------LCgtpeYLAPEVIQS--KGHG-------KAVDWWTMGVLLYEFIAGYPPF 215
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
443-643 3.16e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 60.19  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRG---RWHGEVAIRLLEMD-GHNQDHLKLFKKEVMNYRQTRHENVV-------------LFMgac 505
Cdd:NF033483  10 EIGERIGRGGMAEVYLAkdtRLDRDVAVKVLRPDlARDPEFVARFRREAQSAASLSHPNIVsvydvgedggipyIVM--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 mnpphlaiitSFCKGRTLHSFVRD-----PKTSLDInkTRQIAQeiikGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITD 579
Cdd:NF033483  87 ----------EYVDGRTLKDYIREhgplsPEEAVEI--MIQILS----ALEHAHRNGIVHRDIKPQNILITkDGRVKVTD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 580 FGLF------------GISGVVreerrenqlklsHdwlcYLAPEIVR-EMIPGRdedqlpfskaADVYAFGTVWYEL 643
Cdd:NF033483 151 FGIAralssttmtqtnSVLGTV------------H----YLSPEQARgGTVDAR----------SDIYSLGIVLYEM 201
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
199-241 1.05e-07

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 49.00  E-value: 1.05e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755537521   199 HRFSTKSW-LSQVCNVCQKSMIF----GVKCKHCRLKCHNKCTKEAPA 241
Cdd:smart00109   1 HKHVFRTFtKPTFCCVCRKSIWGsfkqGLRCSECKVKCHKKCADKVPK 48
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
448-582 1.54e-05

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 46.43  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  448 IGQGRWGRVHRGRWHGEVAI---------RLLEMDghnqdhlklfkkEVMNYRQTRHE------------NV-VLFMgac 505
Cdd:TIGR03724   2 IAKGAEAIIYLGDFLGRKAVikervpksyRHPELD------------ERLRKERTRREarllsrarkagvNTpVIYD--- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  506 MNPPHLAIITSFCKGRTLHSFVRDPKTsldinktrqiaqEIIKGMGY----LHAKGIVHKDLKSKNVFYDNGKVVITDFG 581
Cdd:TIGR03724  67 VDPDNKTIVMEYIEGKPLKDVIEENGD------------ELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFG 134

                  .
gi 755537521  582 L 582
Cdd:TIGR03724 135 L 135
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
199-242 6.48e-04

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 38.19  E-value: 6.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755537521  199 HRFSTKSWLSQV-CNVCQKSMIF----GVKCKHCRLKCHNKCTKEAPAC 242
Cdd:pfam00130   1 HHFVHRNFKQPTfCDHCGEFLWGlgkqGLKCSWCKLNVHKRCHEKVPPE 49
 
Name Accession Description Interval E-value
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
441-719 0e+00

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: 621.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14152    1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKL 600
Cdd:cd14152   81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVQEGRRENELKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKE 680
Cdd:cd14152  161 PHDWLCYLAPEIVREMTPGKDEDCLPFSKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGEGMKQVLTTISLGKE 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 681 VGEILSACWAFDLQERPSFSLLMDMLERLPKLNRRLSHP 719
Cdd:cd14152  241 VTEILSACWAFDLEERPSFTLLMDMLEKLPKLNRRLSHP 279
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
441-711 9.82e-173

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: 497.26  E-value: 9.82e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14063    1 ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKL 600
Cdd:cd14063   81 RTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVITDFGLFSLSGLLQPGRREDTLVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRD-EDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvRRVLASVSLGK 679
Cdd:cd14063  161 PNGWLCYLAPEIIRALSPDLDfEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK--KQSLSQLDIGR 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 680 EVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd14063  239 EVKDILMQCWAYDPEKRPTFSDLLRMLERLPK 270
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
441-711 3.81e-153

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: 447.15  E-value: 3.81e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14153    1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKL 600
Cdd:cd14153   81 RTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFTISGVLQAGRREDKLRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgeGVRRVLASVSLGKE 680
Cdd:cd14153  161 QSGWLCHLAPEIIRQLSPETEEDKLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGS--GMKPNLSQIGMGKE 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 755537521 681 VGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd14153  239 ISDILLFCWAYEQEERPTFSKLMEMLEKLPK 269
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
448-706 6.05e-74

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: 240.52  E-value: 6.05e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSF 526
Cdd:cd13999    1 IGSGSFGEVYKGKWRGtDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFgisgvvREERRENQLKLSH-DW 604
Cdd:cd13999   81 LHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDeNFTVKIADFGLS------RIKNSTTEKMTGVvGT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 605 LCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGsGEGVRRVLaSVSLGKEVGEI 684
Cdd:cd13999  155 PRWMAPEVLRGE---------PYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVV-QKGLRPPI-PPDCPPELSKL 223
                        250       260
                 ....*....|....*....|..
gi 755537521 685 LSACWAFDLQERPSFSLLMDML 706
Cdd:cd13999  224 IKRCWNEDPEKRPSFSEIVKRL 245
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
448-707 2.30e-55

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: 190.68  E-value: 2.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGaCMNPPHLAIITSFCKGRTLHSFV 527
Cdd:cd14062    1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMG-YMTKPQLAIVTQWCEGSSLYKHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 528 RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLFGISGVVREERRENQLKLSHDWlc 606
Cdd:cd14062   80 HVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFlHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILW-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 607 yLAPEIVReMipgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKH-QPAEALIWQIGSGEgVRRVLASVS--LGKEVGE 683
Cdd:cd14062  158 -MAPEVIR-M-----QDENPYSFQSDVYAFGIVLYELLTGQLPYSHiNNRDQILFMVGRGY-LRPDLSKVRsdTPKALRR 229
                        250       260
                 ....*....|....*....|....
gi 755537521 684 ILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14062  230 LMEDCIKFQRDERPLFPQILASLE 253
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
442-706 1.42e-49

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 174.99  E-value: 1.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGegentkiKVAVKTLK-EGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREER 593
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVkISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  594 RENQLKLShdwLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGEgvrRVL 672
Cdd:pfam07714 160 KRGGGKLP---IKWMAPESLKDGK---------FTSKSDVWSFGVLLWEIFTLgEQPYPGMSNEEVLEYLEDGY---RLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 755537521  673 ASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:pfam07714 225 QPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
441-712 1.78e-49

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: 174.82  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAcMNPPHLAIITSFCKG 520
Cdd:cd14150    1 EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGF-MTRPNFAIITQWCEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVREERRENQLKL 600
Cdd:cd14150   80 SSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTV--KIGDFGLATVKTRWSGSQQVEQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKH-QPAEALIWQIGSGEgVRRVLASVSLG- 678
Cdd:cd14150  158 PSGSILWMAPEVIRM------QDTNPYSFQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRGY-LSPDLSKLSSNc 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 679 -KEVGEILSACWAFDLQERPSFSLLMDMLERLPKL 712
Cdd:cd14150  231 pKAMKRLLIDCLKFKREERPLFPQILVSIELLQRL 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
434-711 1.74e-48

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: 172.55  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNpPHLAI 513
Cdd:cd14151    2 DWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTK-PQLAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLFGISGVVREE 592
Cdd:cd14151   81 VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFlHEDLTVKIGDFGLATVKSRWSGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 RRENQLKLSHDWlcyLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKH-QPAEALIWQIGSGE---GV 668
Cdd:cd14151  161 HQFEQLSGSILW---MAPEVIRM------QDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYlspDL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 755537521 669 RRVLASVSlgKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd14151  232 SKVRSNCP--KAMKRLMAECLKKKRDERPLFPQILASIELLAR 272
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
435-714 5.03e-45

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: 163.28  E-value: 5.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAcMNPPHLAII 514
Cdd:cd14149    7 WEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREER 593
Cdd:cd14149   86 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVkIGDFGLATVKSRWSGSQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 RENQLKLSHDWlcyLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKH-QPAEALIWQIGSGeGVRRVL 672
Cdd:cd14149  166 QVEQPTGSILW---MAPEVIRM------QDNNPFSFQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRG-YASPDL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 673 ASV--SLGKEVGEILSACWAFDLQERPSFSLLMDMLE----RLPKLNR 714
Cdd:cd14149  236 SKLykNCPKAMKRLVADCIKKVKEERPLFPQILSSIEllqhSLPKINR 283
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
442-706 1.07e-43

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 158.46  E-value: 1.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLeMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgvVREER 593
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVkISDFGL------SRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   594 RENQLKLSHDWLCY--LAPEIVREMIpgrdedqlpFSKAADVYAFG-TVW--YELQARDWPfkHQPAEALIWQIGSGEgv 668
Cdd:smart00219 154 DDDYYRKRGGKLPIrwMAPESLKEGK---------FTSKSDVWSFGvLLWeiFTLGEQPYP--GMSNEEVLEYLKNGY-- 220
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 755537521   669 rRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:smart00219 221 -RLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
442-706 1.03e-41

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: 153.09  E-value: 1.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLeMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkevEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   515 TSFCKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgvVREE 592
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRpKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVkISDFGL------SRDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   593 RRENQLKLSHDWLCY--LAPEIVREMIpgrdedqlpFSKAADVYAFG-TVW--YELQARDWPfkHQPAEALIWQIGSGEg 667
Cdd:smart00221 154 YDDDYYKVKGGKLPIrwMAPESLKEGK---------FTSKSDVWSFGvLLWeiFTLGEEPYP--GMSNAEVLEYLKKGY- 221
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 755537521   668 vrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:smart00221 222 --RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
443-703 4.23e-39

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 145.37  E-value: 4.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKtgkLVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   520 GRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREERRENQL 598
Cdd:smart00220  81 GGDLFDLLKK-RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDeDGHVKLADFGL---ARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521   599 KLShdwLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLG 678
Cdd:smart00220 157 VGT---PEYMAPEVLLGK---------GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDIS 224
                          250       260
                   ....*....|....*....|....*
gi 755537521   679 KEVGEILSACWAFDLQERPSFSLLM 703
Cdd:smart00220 225 PEAKDLIRKLLVKDPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
443-699 3.19e-36

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 137.35  E-value: 3.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  443 ELGEPIGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:pfam00069   2 EVLEKLGSGSFGTVYKAKhrdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  520 GRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQL 598
Cdd:pfam00069  82 GGSLFDLLSE-KGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDeDGNLKITDFGL------ARQLNSGSSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  599 KLshdwLC----YLAPEIVREmipgrdedqLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGsGEGVRRVLAS 674
Cdd:pfam00069 155 TT----FVgtpwYMAPEVLGG---------NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-DQPYAFPELP 220
                         250       260
                  ....*....|....*....|....*
gi 755537521  675 VSLGKEVGEILSACWAFDLQERPSF 699
Cdd:pfam00069 221 SNLSEEAKDLLKKLLKKDPSKRLTA 245
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
446-707 5.00e-36

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: 136.90  E-value: 5.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHG------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGgdgktvDVAVKTLK-EDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVR--------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGL--FGISGV 588
Cdd:cd00192   80 GGDLLDFLRksrpvfpsPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVkISDFGLsrDIYDDD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKLShdWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGEg 667
Cdd:cd00192  160 YYRKKTGGKLPIR--W---MAPESLKDGI---------FTSKSDVWSFGVLLWEIFTLgATPYPGLSNEEVLEYLRKGY- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755537521 668 vrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd00192  225 --RLPKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
448-706 1.60e-34

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: 130.85  E-value: 1.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd00180    1 LGKGSFGKVYKARDKEtgkKVAVKVIPKEKLKKL-LEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREERRENQLKLSHD 603
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDsDGTVKLADFGL---AKDLDSDDSLLKTTGGTT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 604 WLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQardwpfkhqpaealiwqigsgegvrrvlasvslgkEVGE 683
Cdd:cd00180  157 PPYYAPPELLG---------GRYYGPKVDIWSLGVILYELE-----------------------------------ELKD 192
                        250       260
                 ....*....|....*....|...
gi 755537521 684 ILSACWAFDLQERPSFSLLMDML 706
Cdd:cd00180  193 LIRRMLQYDPKKRPSAKELLEHL 215
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
438-709 4.04e-33

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: 129.04  E-value: 4.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGRW------HGE-VAIRLLEMDGHNQdHLKLFKKEVMNYRQTRHENVVLFMGAC--MNP 508
Cdd:cd05038    2 EERHLKFIKQLGEGHFGSVELCRYdplgdnTGEqVAVKSLQPSGEEQ-HMSDFKREIEILRTLDHEYIVKYKGVCesPGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 509 PHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISG 587
Cdd:cd05038   81 RSLRLIMEYLPSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVkISDFGLAKVLP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 588 VVREERRENQLKLSHdwLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIwQIGSGEG 667
Cdd:cd05038  161 EDKEYYYVKEPGESP--IFWYAPECLRESR---------FSSASDVWSFGVTLYELFTYGDPSQSPPALFLR-MIGIAQG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 668 VRRVLASVSLGK-------------EVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05038  229 QMIVTRLLELLKsgerlprppscpdEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
448-709 6.48e-33

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: 127.89  E-value: 6.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDgHNQDH---LKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG--- 520
Cdd:cd14061    2 IGVGGFGKVYRGIWRGeEVAVKAARQD-PDEDIsvtLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGgal 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 -RTLHSFVRDPKTSLDinktrqIAQEIIKGMGYLHAKG---IVHKDLKSKNVF---------YDNGKVVITDFGLfgisg 587
Cdd:cd14061   81 nRVLAGRKIPPHVLVD------WAIQIARGMNYLHNEApvpIIHRDLKSSNILileaienedLENKTLKITDFGL----- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 588 vVREERRENQLKLSHDWlCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWqigsgeG 667
Cdd:cd14061  150 -AREWHKTTRMSAAGTY-AWMAPEVIK---------SSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAY------G 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 668 VrrvlASVSLG--------KEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14061  213 V----AVNKLTlpipstcpEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
448-699 7.05e-32

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: 124.87  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL- 523
Cdd:cd13978    1 LGSGGFGTVSKARhvsWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 ---HSFVRDPKTSLDInktrQIAQEIIKGMGYLH--AKGIVHKDLKSKNVFYDNG-KVVITDFGLFGISGVVREERRENQ 597
Cdd:cd13978   81 sllEREIQDVPWSLRF----RIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHfHVKISDFGLSKLGMKSISANRRRG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDWLCYLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVSL 677
Cdd:cd13978  157 TENLGGTPIYMAPEAF-------DDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVS-KGDRPSLDDIGR 228
                        250       260
                 ....*....|....*....|....*...
gi 755537521 678 GK------EVGEILSACWAFDLQERPSF 699
Cdd:cd13978  229 LKqienvqELISLMIRCWDGNPDARPTF 256
C1_KSR1 cd20872
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and ...
197-243 1.97e-31

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and similar proteins; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410422  Cd Length: 47  Bit Score: 116.30  E-value: 1.97e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 197 VTHRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPACR 243
Cdd:cd20872    1 VTHRFSTKSWLSQTCQVCQKSMMFGVKCKHCRLKCHNKCTKEAPACR 47
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
443-708 3.10e-30

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: 120.00  E-value: 3.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMD-GHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14014    3 RLVRLLGRGGMGEVYRARDTLlgrPVAIKVLRPElAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfglFGISGVVREER--RE 595
Cdd:cd14014   83 EGGSLADLLRERGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTeDGRVKLTD---FGIARALGDSGltQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDwlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASV 675
Cdd:cd14014  159 GSVLGTPA---YMAPEQARGG---------PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 676 SLGKEVGEILSACWAFDLQERP-SFSLLMDMLER 708
Cdd:cd14014  227 DVPPALDAIILRALAKDPEERPqSAAELLAALRA 260
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
443-666 3.57e-30

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: 119.54  E-value: 3.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwH---GE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14003    3 ELGKTLGEGSFGKVKLAR-HkltGEkVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQ 597
Cdd:cd14003   82 SGGELFDYIVN-NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDkNGNLKIIDFGL------SNEFRGGSL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 598 LKLSHDWLCYLAPeivrEMIPGRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14003  155 LKTFCGTPAYAAP----EVLLGRKYD----GPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGK 215
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
438-709 4.83e-30

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: 119.80  E-value: 4.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVmNYRQTRHENVVLFMGA--CMNPPHLA-I 513
Cdd:cd13979    1 DWEPLRLQEPLGSGGFGSVYKATYKGEtVAVKIVRRRRKNRASRQSFWAEL-NAARLRHENIVRVLAAetGTDFASLGlI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGlfgiSGVVREE 592
Cdd:cd13979   80 IMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIsEQGVCKLCDFG----CSVKLGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 RRENQLKLSHDW--LCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFkHQPAEALIWQIgSGEGVRR 670
Cdd:cd13979  156 GNEVGTPRSHIGgtYTYRAPELLK---------GERVTPKADIYSFGITLWQMLTRELPY-AGLRQHVLYAV-VAKDLRP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 671 VLASVS---LGKEVGEILSACWAFDLQERPSFSLlmDMLERL 709
Cdd:cd13979  225 DLSGLEdseFGQRLRSLISRCWSAQPAERPNADE--SLLKSL 264
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
448-707 4.64e-29

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: 116.05  E-value: 4.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAIRLLEmdghnqdhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSF 526
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEeVAVKKVR---------DEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKT---SLDINKTRQIAQeiikGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFgisgvvrEERRENQLKLSH 602
Cdd:cd14059   72 LRAGREitpSLLVDWSKQIAS----GMNYLHLHKIIHRDLKSPNVLVTYNDVLkISDFGTS-------KELSEKSTKMSF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 603 -DWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvRRVLASVSLGKEV 681
Cdd:cd14059  141 aGTVAWMAPEVIRNE---------PCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNS--LQLPVPSTCPDGF 209
                        250       260
                 ....*....|....*....|....*.
gi 755537521 682 GEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14059  210 KLLMKQCWNSKPRNRPSFRQILMHLD 235
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
445-698 5.52e-29

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: 116.47  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWH---GEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd06606    5 GELLGKGSFGSVYLALNLdtgELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERRENQLKL 600
Cdd:cd06606   85 SLASLLKK-FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVkLADFGC---AKRLAEIATGEGTKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWLCYLAPEIVREMIPGRdedqlpfskAADVYAFGTVWYEL--QARDWPFKHQPAeALIWQIGSGEGVRRVLASVSlg 678
Cdd:cd06606  161 LRGTPYWMAPEVIRGEGYGR---------AADIWSLGCTVIEMatGKPPWSELGNPV-AALFKIGSSGEPPPIPEHLS-- 228
                        250       260
                 ....*....|....*....|
gi 755537521 679 KEVGEILSACWAFDLQERPS 698
Cdd:cd06606  229 EEAKDFLRKCLQRDPKKRPT 248
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
449-709 5.82e-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: 115.82  E-value: 5.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 449 GQGRWGRVHRGRW---HGEVAIR-LLEMDghnqdhlklfkKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd14060    2 GGGSFGSVYRAIWvsqDKEVAVKkLLKIE-----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKG---IVHKDLKSKNVfydngkVVITDFGL----FGISGVVREERREN 596
Cdd:cd14060   71 DYLNSNESEeMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNV------VIAADGVLkicdFGASRFHSHTTHMS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 qLKLSHDWLcylAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIgsGEGVRRVLASVS 676
Cdd:cd14060  145 -LVGTFPWM---APEVIQ---------SLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLV--VEKNERPTIPSS 209
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 677 LGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14060  210 CPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
448-707 7.69e-29

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: 116.24  E-value: 7.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAIRLLEMDGHNQDHLKL--FKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd14148    2 IGVGGFGKVYKGLWRGEeVAVKAARQDPDEDIAVTAenVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFV---RDPKTSLdINKTRQIAqeiiKGMGYLHAKGIV---HKDLKSKNVF---------YDNGKVVITDFGLfgisgvV 589
Cdd:cd14148   82 RALagkKVPPHVL-VNWAVQIA----RGMNYLHNEAIVpiiHRDLKSSNILilepienddLSGKTLKITDFGL------A 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQLKLSHDWlCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVR 669
Cdd:cd14148  151 REWHKTTKMSAAGTY-AWMAPEVIRLSL---------FSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTL 220
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RVLASVSlgKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14148  221 PIPSTCP--EPFARLLEECWDPDPHGRPDFGSILKRLE 256
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
435-709 1.67e-28

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: 115.14  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHNQDHLkLFKKEVMNyrQTRHENVVLFMGACMNPPHLAI 513
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQkVAVKCLKDDSTAAQAF-LAEASVMT--TLRHPNLVQLLGVVLEGNGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLdINKTRQI--AQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgisgvVR 590
Cdd:cd05039   78 VTEYMAKGSLVDYLRSRGRAV-ITRKDQLgfALDVCEGMEYLESKKFVHRDLAARNVLVsEDNVAKVSDFGL------AK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQL-KLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQA--RDwPFKHQPAEALIWQIGSGeg 667
Cdd:cd05039  151 EASSNQDGgKLPIKW---TAPEALREKK---------FSTKSDVWSFGILLWEIYSfgRV-PYPRIPLKDVVPHVEKG-- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 668 vRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05039  216 -YRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
448-707 5.16e-28

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: 113.39  E-value: 5.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAI-RLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMN-PPHLAIITSFCKGRTLH 524
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKiVAIkRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDdPSQFAIVTQYVSGGSLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTSLDINKTRQIAQEIIKGMGYLH--AKGIVHKDLKSKNVF-YDNGKVVITDFGLfgiSGVVREERRENQLKLS 601
Cdd:cd14064   81 SLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILlYEDGHAVVADFGE---SRFLQSLDEDNMTKQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDwLCYLAPEIVREMipGRdedqlpFSKAADVYAFGTVWYELQARDWPFKH-QPAEAliwqiGSGEGVRRVLASV--SLG 678
Cdd:cd14064  158 GN-LRWMAPEVFTQC--TR------YSIKADVFSYALCLWELLTGEIPFAHlKPAAA-----AADMAYHHIRPPIgySIP 223
                        250       260
                 ....*....|....*....|....*....
gi 755537521 679 KEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14064  224 KPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
448-706 6.50e-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: 113.59  E-value: 6.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDGhNQD---HLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14146    2 IGVGGFGKVYRATWKGqEVAVKAARQDP-DEDikaTAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTSLDINKTRQI--------AQEIIKGMGYLHAKGIV---HKDLKSKNVF------YD---NGKVVITDFGLf 583
Cdd:cd14146   81 NRALAAANAAPGPRRARRIpphilvnwAVQIARGMLYLHEEAVVpilHRDLKSSNILllekieHDdicNKTLKITDFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 584 gisgvVREERRENQLKLSHDWlCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWqig 663
Cdd:cd14146  160 -----AREWHRTTKMSAAGTY-AWMAPEVIKSSL---------FSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAY--- 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 664 sGEGVRRVLASV--SLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd14146  222 -GVAVNKLTLPIpsTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
436-706 1.83e-27

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: 112.44  E-value: 1.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHG-EVAIRLLEMDGHN--QDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd14145    2 EIDFSELVLEEIIGIGGFGKVYRAIWIGdEVAVKAARHDPDEdiSQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPKTSLDI--NKTRQIAqeiiKGMGYLHAKGIV---HKDLKSKNVF----YDNGKVV-----IT 578
Cdd:cd14145   82 LVMEFARGGPLNRVLSGKRIPPDIlvNWAVQIA----RGMNYLHCEAIVpviHRDLKSSNILilekVENGDLSnkilkIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 579 DFGLfgisgvVREERRENQLKLSHDWlCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd14145  158 DFGL------AREWHRTTKMSAAGTY-AWMAPEVIRSSM---------FSKGSDVWSYGVLLWELLTGEVPFRGIDGLAV 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 659 IWQIGSGEGVRRVLASVSlgKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd14145  222 AYGVAMNKLSLPIPSTCP--EPFARLMEDCWNPDPHSRPPFTNILDQL 267
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
435-706 2.29e-27

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: 111.76  E-value: 2.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRW--HGEVAIRLLEMDghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEVWEGLWknRVRVAIKILKSD--DLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVR 590
Cdd:cd05148   79 IITELMEKGSLLAFLRSPEgQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCkVADFGL---ARLIK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EErrenqLKLSHD------WLcylAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIG 663
Cdd:cd05148  156 ED-----VYLSSDkkipykWT---APEAA---SHGT------FSTKSDVWSFGILLYEMFTYgQVPYPGMNNHEVYDQIT 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 755537521 664 SGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05148  219 AG---YRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREEL 258
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
465-711 3.03e-27

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: 111.92  E-value: 3.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 465 VAIRLLemdghNQDHLKL---FKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCkgrtlhsfvrdPKTSL-DINKTR 540
Cdd:cd14042   33 VAIKKV-----NKKRIDLtreVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYC-----------PKGSLqDILENE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 541 QI----------AQEIIKGMGYLHAKGIV-HKDLKSKNVFYDNGKVV-ITDFGLFgisgvvreERRENQLKLSHDWLCYL 608
Cdd:cd14042   97 DIkldwmfryslIHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLkITDFGLH--------SFRSGQEPPDDSHAYYA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 609 -----APEIVREMIPgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQ-----PAEALIWQIGSGEG--VRRVLASVS 676
Cdd:cd14042  169 kllwtAPELLRDPNP-----PPPGTQKGDVYSFGIILQEIATRQGPFYEEgpdlsPKEIIKKKVRNGEKppFRPSLDELE 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 677 LGKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd14042  244 CPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLNK 278
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
484-701 7.23e-27

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: 110.56  E-value: 7.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLH-AKGIVHKD 562
Cdd:cd13992   44 LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHsSSIGYHGR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 563 LKSKNVFYDNGKVV-ITDFGLFGISGvvREERRENQLKLSHDWLCYLAPEIVRemipGRDEDQLPfSKAADVYAFGTVWY 641
Cdd:cd13992  124 LKSSNCLVDSRWVVkLTDFGLRNLLE--EQTNHQLDEDAQHKKLLWTAPELLR----GSLLEVRG-TQKGDVYSFAIILY 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 642 ELQARDWPF-KHQPAEALIWQIGSGEGVRRVLASVSLGK---EVGEILSACWAFDLQERPSFSL 701
Cdd:cd13992  197 EILFRSDPFaLEREVAIVEKVISGGNKPFRPELAVLLDEfppRLVLLVKQCWAENPEKRPSFKQ 260
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
448-709 2.08e-26

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: 109.28  E-value: 2.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE--VAIRLLEMDGHNQDHlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL-- 523
Cdd:cd14066    1 IGSGGFGTVYKGVLENGtvVAVKRLNEMNCAASK-KEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLed 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTSLDInKTRQ-IAQEIIKGMGYLHAKG---IVHKDLKSKNVFYDNGKV-VITDFGLFGISGVVREERRENQL 598
Cdd:cd14066   80 RLHCHKGSPPLPW-PQRLkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEpKLTDFGLARLIPPSESVSKTSAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLShdwLCYLAPEIVREMIPgrdedqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGS------GEGVRRVL 672
Cdd:cd14066  159 KGT---IGYLAPEYIRTGRV---------STKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEwveskgKEELEDIL 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 673 ---------ASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14066  227 dkrlvdddgVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
439-709 4.57e-26

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: 108.19  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHNQDHL--KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14147    2 FQELRLEEVIGIGGFGKVYRGSWRGElVAVKAARQDPDEDISVtaESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFV---RDPKTSLdINKTRQIAqeiiKGMGYLHAKGIV---HKDLKSKNVF---------YDNGKVVITDF 580
Cdd:cd14147   82 EYAAGGPLSRALagrRVPPHVL-VNWAVQIA----RGMHYLHCEALVpviHRDLKSNNILllqpienddMEHKTLKITDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 581 GLfgisgvVREERRENQLKLSHDWlCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIW 660
Cdd:cd14147  157 GL------AREWHKTTQMSAAGTY-AWMAPEVIKAST---------FSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAY 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 661 qigsGEGVRRVLASV--SLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14147  221 ----GVAVNKLTLPIpsTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
446-706 1.87e-25

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: 106.27  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE------VAIRLLEMDGHNQ-DHLKLFKKEVMNYRQTRHENVVLFMGACMNPPhLAIITSFC 518
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPsgkviqVAVKCLKSDVLSQpNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLFGISGVVREERREN- 596
Cdd:cd05040   80 PLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILlASKDKVKIGDFGLMRALPQNEDHYVMQe 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWlCylAPEIVRemipgrdedQLPFSKAADVYAFG-TVWyELqardWPFKHQPAEAL----IWQIGSGEGvRRV 671
Cdd:cd05040  160 HRKVPFAW-C--APESLK---------TRKFSHASDVWMFGvTLW-EM----FTYGEEPWLGLngsqILEKIDKEG-ERL 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 672 LASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05040  222 ERPDDCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
446-646 7.61e-25

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 105.05  E-value: 7.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE-VAIRL---LEMDGhnqdhlklFKKEVMNYrQT---RHENVVLFMGACMNPPH----LAII 514
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRGEkVAVKIfssRDEDS--------WFRETEIY-QTvmlRHENILGFIAADIKSTGswtqLWLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfgi 585
Cdd:cd14056   72 TEYHEHGSLYDYLQ--RNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVkRDGTCCIADLGL--- 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 586 sgVVREERRENQLKLSHDWLC----YLAPEIVREMIPGRDEDQLpfsKAADVYAFGTVWYELQAR 646
Cdd:cd14056  147 --AVRYDSDTNTIDIPPNPRVgtkrYMAPEVLDDSINPKSFESF---KMADIYSFGLVLWEIARR 206
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
448-709 7.62e-25

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: 104.44  E-value: 7.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDGHNQDhlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSF 526
Cdd:cd14058    1 VGRGSFGVVCKARWRNqIVAVKIIESESEKKA----FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKTSLDINKTRQI--AQEIIKGMGYLHA---KGIVHKDLKSKNVF-YDNGKVV-ITDFGLfgisgVVREERRENQLK 599
Cdd:cd14058   77 LHGKEPKPIYTAAHAMswALQCAKGVAYLHSmkpKALIHRDLKPPNLLlTNGGTVLkICDFGT-----ACDISTHMTNNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDWlcyLAPEIvremIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKH--QPAEALIWQIGSGEgvRRVLASVsL 677
Cdd:cd14058  152 GSAAW---MAPEV----FEGSK-----YSEKCDVFSWGIILWEVITRRKPFDHigGPAFRIMWAVHNGE--RPPLIKN-C 216
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14058  217 PKPIESLMTRCWSKDPEKRPSMKEIVKIMSHL 248
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
448-709 1.60e-24

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: 104.33  E-value: 1.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH------GEV-AIRLLEMDghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP--PHLAIITSFC 518
Cdd:cd14205   12 LGKGNFGSVEMCRYDplqdntGEVvAVKKLQHS--TEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgiSGVVREERRENQ 597
Cdd:cd14205   90 PYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENeNRVKIGDFGL---TKVLPQDKEYYK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDW-LCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEaLIWQIGSG-EGVRRVLASV 675
Cdd:cd14205  167 VKEPGESpIFWYAPESLTES---------KFSVASDVWSFGVVLYELFTYIEKSKSPPAE-FMRMIGNDkQGQMIVFHLI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 676 SLGK-------------EVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14205  237 ELLKnngrlprpdgcpdEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
441-711 2.25e-24

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: 103.65  E-value: 2.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRW--HGE-----VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHlAI 513
Cdd:cd05057    8 ELEKGKVLGSGAFGTVYKGVWipEGEkvkipVAIKVLR-EETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQV-QL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLD----INKTRQIAqeiiKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGV 588
Cdd:cd05057   86 ITQLMPLGCLLDYVRNHRDNIGsqllLNWCVQIA----KGMSYLEEKRLVHRDLAARNVLVKTPNHVkITDFGLAKLLDV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEg 667
Cdd:cd05057  162 DEKEYHAEGGKVPIKW---MALESIQYRI---------YTHKSDVWSYGvTVWELMTFGAKPYEGIPAVEIPDLLEKGE- 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 755537521 668 vrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd05057  229 --RLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMAR 270
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
443-732 3.02e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 105.59  E-value: 3.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQ-DHLKLFKKEVMNYRQTRHE-NVVLFMGACMNPPHLAIITSFCKG 520
Cdd:COG0515    3 RILRKLGEGSFGEVYLARDRKLVALKVLAKKLESKsKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEYVDG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDP--KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFGLFGISGVVREERREN 596
Cdd:COG0515   83 GSLEDLLKKIgrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrdGRVVKLIDFGLAKLLPDPGSTSSIP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDW-LCYLAPEIVREMIPGRDedqlpfSKAADVYAFGTVWYELQARDWPF---KHQPAEALIWQIGSGEGVRRVL 672
Cdd:COG0515  163 ALPSTSVGtPGYMAPEVLLGLSLAYA------SSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTPSLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 673 ASVS------LGKEVGEILSACWAFDLQERPS--FSLLMDMLERLPKLNRRLSHPGHFWKSADRWRSR 732
Cdd:COG0515  237 SPLSpsnpelISKAASDLLKKLLAKDPKNRLSssSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSL 304
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
434-707 6.55e-24

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: 102.10  E-value: 6.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDHlklFKKEVMNYRQTRHENVVLFMGACMNPPHL 511
Cdd:cd05068    2 QWEIDRKSLKLLRKLGSGQFGEVWEGLWNNttPVAVKTLKPGTMDPED---FLREAQIMKKLRHPKLIQLYAVCTLEEPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVR 590
Cdd:cd05068   79 YIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVgENNICKVADFGLARVIKVED 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQLKLSHDWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGegvR 669
Cdd:cd05068  159 EYEAREGAKFPIKW---TAPEAAN---------YNRFSIKSDVWSFGILLTEIVTYgRIPYPGMTNAEVLQQVERG---Y 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05068  224 RMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLE 261
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
434-709 8.10e-24

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: 102.50  E-value: 8.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG---------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd05053    6 EWELPRDRLTLGKPLGEGAFGQVVKAEAVGldnkpnevvTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFVR-------DPKTSLDINKTRQIAQ--------EIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd05053   86 CTQDGPLYVVVEYASKGNLREFLRarrppgeEASPDDPRVPEEQLTQkdlvsfayQVARGMEYLASKKCIHRDLAARNVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 570 YDNGKVV-ITDFGLfgiSGVVREE---RRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQA 645
Cdd:cd05053  166 VTEDNVMkIADFGL---ARDIHHIdyyRKTTNGRLPVKW---MAPEALFDRV---------YTHQSDVWSFGVLLWEIFT 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 646 -RDWPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05053  231 lGGSPYPGIPVEELFKLLKEGH---RMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
431-709 1.49e-23

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: 101.79  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM 502
Cdd:cd05055   26 YDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGlsksdavmKVAVKMLKPTAHSSEREALMSELKIMSHLGNHENIVNLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHLAIITSFCKGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDF 580
Cdd:cd05055  106 GACTIGGPILVITEYCCYGDLLNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVkICDF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 581 GLfgisgvVREERRENQL------KLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDW-PFKHQ 653
Cdd:cd05055  186 GL------ARDIMNDSNYvvkgnaRLPVKW---MAPESIFNCV---------YTFESDVWSYGILLWEIFSLGSnPYPGM 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 654 PAEALIWQ-IGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05055  248 PVDSKFYKlIKEG---YRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQ 301
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
444-706 6.15e-23

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: 98.67  E-value: 6.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDHlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd05059    8 FLKELGSGQFGVVHLGKWRGkiDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREERRENQ-LK 599
Cdd:cd05059   85 CLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVgEQNVVKVSDFGL--ARYVLDDEYTSSVgTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDWLcylAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELqardWPFKHQPAEALiwqiGSGEGVRRVLASVSLGK 679
Cdd:cd05059  163 FPVKWS---PPEVF---------MYSKFSSKSDVWSFGVLMWEV----FSEGKMPYERF----SNSEVVEHISQGYRLYR 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 680 ------EVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05059  223 phlaptEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
446-706 1.03e-22

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: 97.90  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHG---EVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPdntEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgisgvVREERR---ENQL 598
Cdd:cd05041   80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVgENNVLKISDFGM------SREEEDgeyTVSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDWLCYLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYEL--------------QARDwpfkhqpaealiwQIGS 664
Cdd:cd05041  154 GLKQIPIKWTAPEALNY---GR------YTSESDVWSFGILLWEIfslgatpypgmsnqQTRE-------------QIES 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 665 GegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05041  212 G---YRMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
440-646 1.14e-22

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 99.05  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLEmdghNQDHLKLFKK-EVMNYRQTRHENVVLFMGACMNPPH----LAI 513
Cdd:cd14142    5 RQITLVECIGKGRYGEVWRGQWQGEsVAVKIFS----SRDEKSWFREtEIYNTVLLRHENILGFIASDMTSRNsctqLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfg 584
Cdd:cd14142   81 ITHYHENGSLYDYLQ--RTTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVkSNGQCCIADLGL-- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 585 isgVVREERRENQLKLSHDWLC----YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQAR 646
Cdd:cd14142  157 ---AVTHSQETNQLDVGNNPRVgtkrYMAPEVLDETI---NTDCFESYKRVDIYAFGLVLWEVARR 216
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
448-706 2.37e-22

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: 97.18  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRwHGEVA-IRLLEMDGHNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSF 526
Cdd:cd14065    1 LGKGFFGEVYKVT-HRETGkVMVMKELKRFDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGK-VVITDFGLFGISGVVREERRENQLKLSH 602
Cdd:cd14065   79 LKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLvreANRGRnAVVADFGLAREMPDEKTKKPDRKKRLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 603 DWLCY-LAPEIVRemipGRdedqlPFSKAADVYAFGTVWYELQARdwpfkhQPA--EALIWQIGSGEGVR--RVLASVSL 677
Cdd:cd14065  159 VGSPYwMAPEMLR----GE-----SYDEKVDVFSFGIVLCEIIGR------VPAdpDYLPRTMDFGLDVRafRTLYVPDC 223
                        250       260
                 ....*....|....*....|....*....
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd14065  224 PPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
440-650 3.18e-22

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: 96.55  E-value: 3.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHGE---VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTgqvVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRtLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREerre 595
Cdd:cd14002   81 YAQGE-LFQILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGkGGVVKLCDFGF------ARA---- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 596 nqlkLSHDWLC---------YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14002  149 ----MSCNTLVltsikgtplYMAPELVQEQ---------PYDHTADLWSLGCILYELFVGQPPF 199
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
443-666 4.21e-22

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: 96.39  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKtgeEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgisgvvreERRE 595
Cdd:cd05117   83 GGELFDRIVK-KGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskdPDSPIKIIDFGL---------AKIF 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 596 NQLKLSHDwLC----YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd05117  153 EEGEKLKT-VCgtpyYVAPEVLK---------GKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGK 217
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
442-703 1.64e-21

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: 94.58  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRGRwH----GEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd05122    2 FEILEKIGKGGFGVVYKAR-HkktgQIVAIK--KINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITDFGLfgiSGVVREERREN 596
Cdd:cd05122   79 CSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANIlLTSDGEVKLIDFGL---SAQLSDGKTRN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLShdwLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVS 676
Cdd:cd05122  156 TFVGT---PYWMAPEVIQGK---------PYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIAT-NGPPGLRNPKK 222
                        250       260
                 ....*....|....*....|....*..
gi 755537521 677 LGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd05122  223 WSKEFKDFLKKCLQKDPEKRPTAEQLL 249
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
448-709 1.89e-21

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: 95.35  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH------GE-VAIRLLEMDGhnQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP--PHLAIITSFC 518
Cdd:cd05081   12 LGKGNFGSVELCRYDplgdntGAlVAVKQLQHSG--PDQQRDFQREIQILKALHSDFIVKYRGVSYGPgrRSLRLVMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGI------SGVVRE 591
Cdd:cd05081   90 PSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESeAHVKIADFGLAKLlpldkdYYVVRE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ERRENqlklshdwLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-----QARDWPFK-------HQPAEALI 659
Cdd:cd05081  170 PGQSP--------IFWYAPESLSDNI---------FSRQSDVWSFGVVLYELftycdKSCSPSAEflrmmgcERDVPALC 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 660 WQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05081  233 RLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
435-709 6.31e-21

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: 93.12  E-value: 6.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG-EVAIRLLEMDGHNQdhlkLFKKEVMNYRQTRHENVVLFMGACMNPP-HLA 512
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDVMLGDYRGnKVAVKCIKNDATAQ----AFLAEASVMTQLRHSNLVQLLGVIVEEKgGLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDP-KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgVVR 590
Cdd:cd05082   77 IVTEYMAKGSLVDYLRSRgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAkVSDFGL-----TKE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQA-RDWPFKHQPAEALIWQIGSGegvR 669
Cdd:cd05082  152 ASSTQDTGKLPVKW---TAPEALREKK---------FSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKG---Y 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05082  217 KMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
448-646 6.82e-21

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: 93.34  E-value: 6.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV----HRGRwhGEVAIrLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14154    1 LGKGFFGQAikvtHRET--GEVMV-MKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK-VVITDFGLfgiSGVVREERRENQLKLSH 602
Cdd:cd14154   78 KDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKtVVVADFGL---ARLIVEERLPSGNMSPS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 603 DWLCYLAPEIVR--------------EMIPGRDEDQlpfskAADVYAFGTVWYELQAR 646
Cdd:cd14154  155 ETLRHLKSPDRKkrytvvgnpywmapEMLNGRSYDE-----KVDIFSFGIVLCEIIGR 207
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
439-643 7.69e-21

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: 93.13  E-value: 7.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRV----HRGRwHGEVAIRLLEMDGHNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd13996    8 FEEIEL---LGSGGFGSVykvrNKVD-GVTYAIKKIRLTEKSSASEKVLR-EVKALAKLNHPNIVRYYTAWVEEPPLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDPKTSLDINKT--RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV--ITDFGL-------- 582
Cdd:cd13996   83 MELCEGGTLRDWIDRRNSSSKNDRKlaLELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQvkIGDFGLatsignqk 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 583 -FGISGVVREERRENQLKLSHDWLCYLAPEivremipgrDEDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd13996  163 rELNNLNNNNNGNTSNNSVGIGTPLYASPE---------QLDGENYNEKADIYSLGIILFEM 215
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
448-707 1.24e-20

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: 92.66  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH------GE-VAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP--PHLAIITSFC 518
Cdd:cd05080   12 LGEGHFGKVSLYCYDptndgtGEmVAVKALKAD-CGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQLIMEYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVrdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGI--SGVVREERRE 595
Cdd:cd05080   91 PLGSLRDYL--PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVkIGDFGLAKAvpEGHEYYRVRE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NqlklSHDWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPfKHQPAEALIWQIGSGEGVRRVLASV 675
Cdd:cd05080  169 D----GDSPVFWYAPECLKEY---------KFYYASDVWSFGVTLYELLTHCDS-SQSPPTKFLEMIGIAQGQMTVVRLI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 676 SL-------------GKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05080  235 ELlergerlpcpdkcPQEVYHLMKNCWETEASFRPTFENLIPILK 279
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
434-709 1.60e-20

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: 93.11  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG----------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMG 503
Cdd:cd05099    6 KWEFPRDRLVLGKPLGEGCFGQVVRAEAYGidksrpdqtvTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNIINLLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 ACMNPPHLAIITSFCKGRTLHSFVR-----DPKTSLDINKTRQ----------IAQEIIKGMGYLHAKGIVHKDLKSKNV 568
Cdd:cd05099   86 VCTQEGPLYVIVEYAAKGNLREFLRarrppGPDYTFDITKVPEeqlsfkdlvsCAYQVARGMEYLESRRCIHRDLAARNV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 569 FYDNGKVV-ITDFGLF-GISGVVREERRENQlKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QA 645
Cdd:cd05099  166 LVTEDNVMkIADFGLArGVHDIDYYKKTSNG-RLPVKW---MAPEALFDRV---------YTHQSDVWSFGILMWEIfTL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 646 RDWPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05099  233 GGSPYPGIPVEELFKLLREGH---RMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKV 293
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
448-705 1.98e-20

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: 91.37  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd08215    8 IGKGSFGSAYlvRRKSDGKlYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTSLDINKTRQI----AQeIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDfglFGISGVVreerrENQLK 599
Cdd:cd08215   88 QKIKKQKKKGQPFPEEQIldwfVQ-ICLALKYLHSRKILHRDLKTQNIFLTKDGVVkLGD---FGISKVL-----ESTTD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgVRRVLASVS 676
Cdd:cd08215  159 LAKTVVgtpYYLSPELCENK---------PYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQ-YPPIPSQYS 228
                        250       260
                 ....*....|....*....|....*....
gi 755537521 677 lgKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd08215  229 --SELRDLVNSMLQKDPEKRPSANEILSS 255
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
435-708 2.73e-20

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: 91.64  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKlFKKE--VMNYRQTRHenVVLFMGA 504
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKGvvkgepetRVAIKTVNENASMRERIE-FLNEasVMKEFNCHH--VVRLLGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFVR---------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGK 574
Cdd:cd05032   78 VSTGQPTLVVMELMAKGDLKSYLRsrrpeaennPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNcMVAEDLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 575 VVITDFGLfgiSGVVREE---RRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQA-RDWPF 650
Cdd:cd05032  158 VKIGDFGM---TRDIYETdyyRKGGKGLLPVRW---MAPESLKDGV---------FTTKSDVWSFGVVLWEMATlAEQPY 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 651 KHQPAEALIWQIGSGEGVRRvlaSVSLGKEVGEILSACWAFDLQERPSFSLLMDMLER 708
Cdd:cd05032  223 QGLSNEEVLKFVIDGGHLDL---PENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
199-243 3.70e-20

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 84.30  E-value: 3.70e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 199 HRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPA-CR 243
Cdd:cd20812    3 HRFSKKLFMRQTCDYCHKQMFFGLKCKDCKYKCHKKCAKKAPPsCG 48
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
445-704 5.64e-20

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: 90.15  E-value: 5.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGrWHGEVA-------IRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd06632    5 GQLLGSGSFGSVYEG-FNGDTGdffavkeVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREERREN 596
Cdd:cd06632   84 VPGGSIHKLLQR-YGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDtNGVVKLADFGM---AKHVEAFSFAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHdwlCYLAPEIVREMipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVS 676
Cdd:cd06632  160 SFKGSP---YWMAPEVIMQK-------NSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIPDHLS 229
                        250       260
                 ....*....|....*....|....*...
gi 755537521 677 LgkEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06632  230 P--DAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
440-612 6.58e-20

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: 90.08  E-value: 6.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVflaVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLhsFVR-DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREERR 594
Cdd:cd14069   81 YASGGEL--FDKiEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDeNDNLKISDFGL---ATVFRYKGK 155
                        170
                 ....*....|....*...
gi 755537521 595 ENQLKLSHDWLCYLAPEI 612
Cdd:cd14069  156 ERLLNKMCGTLPYVAPEL 173
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
435-713 7.63e-20

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: 90.84  E-value: 7.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG----------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd05098    8 WELPRDRLVLGKPLGEGCFGQVVLAEAIGldkdkpnrvtKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFVR---------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd05098   88 CTQDGPLYVIVEYASKGNLREYLQarrppgmeycynpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 570 YDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QARD 647
Cdd:cd05098  168 VTEDNVMkIADFGLARDIHHIDYYKKTTNGRLPVKW---MAPEALFDRI---------YTHQSDVWSFGVLLWEIfTLGG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 648 WPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPKLN 713
Cdd:cd05098  236 SPYPGVPVEELFKLLKEGH---RMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALT 298
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
437-643 1.06e-19

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: 90.13  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 437 IPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP 508
Cdd:cd05048    2 IPLSAVRFLEELGEGAFGKVYKGELLGpsseesaiSVAIKTLK-ENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 509 PHLAIITSFCKGRTLHSFV---------------RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDN 572
Cdd:cd05048   81 QPQCMLFEYMAHGDLHEFLvrhsphsdvgvssddDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLvGDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 573 GKVVITDFGLFgisgvvreerrenQLKLSHDWlcY------LAPeiVREMIP-----GRdedqlpFSKAADVYAFGTVWY 641
Cdd:cd05048  161 LTVKISDFGLS-------------RDIYSSDY--YrvqsksLLP--VRWMPPeailyGK------FTTESDVWSFGVVLW 217

                 ..
gi 755537521 642 EL 643
Cdd:cd05048  218 EI 219
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
446-646 1.58e-19

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: 89.81  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHnqdhlKLFKKEVMNYRQT--RHENVVLFMGACMNPPHLA----IITSFC 518
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNEpVAVKIFSSRDK-----QSWFREKEIYRTPmlKHENILQFIAADERDTALRtelwLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK---------GIVHKDLKSKNVFY-DNGKVVITDFGL-FGISG 587
Cdd:cd13998   76 PNGSL*DYLS--LHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVkNDGTCCIADFGLaVRLSP 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 588 VVREERRENQLKLSHDWlcYLAPEIVREMIPGRDEDQLpfsKAADVYAFGTVWYELQAR 646
Cdd:cd13998  154 STGEEDNANNGQVGTKR--YMAPEVLEGAINLRDFESF---KRVDIYAMGLVLWEMASR 207
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
444-655 1.74e-19

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: 89.08  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGrWHG---------EVAIRLLEMDG-HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAI 513
Cdd:cd14076    5 LGRTLGEGEFGKVKLG-WPLpkanhrsgvQVAIKLIRRDTqQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGISGvvreE 592
Cdd:cd14076   84 VLEFVSGGELFDYILA-RRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDkNRNLVITDFGFANTFD----H 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 593 RRENQLKLSHDWLCYLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPA 655
Cdd:cd14076  159 FNGDLMSTSCGSPCYAAPELV-------VSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDPH 214
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
448-710 1.75e-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: 88.95  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPhLAIITSFCKGR 521
Cdd:cd05060    3 LGHGNFGSVRKGVYLMksgkevEVAVKTLK-QEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgiSGVVREERRENQLKL 600
Cdd:cd05060   81 PLLKYLKKRREIPVSDLK-ELAHQVAMGMAYLESKHFVHRDLAARNVLLVNrHQAKISDFGM---SRALGAGSDYYRATT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDW-LCYLAPEIVREMIpgrdedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVSLG 678
Cdd:cd05060  157 AGRWpLKWYAPECINYGK---------FSSKSDVWSYGvTLWEAFSYGAKPYGEMKGPEVIAMLESGE---RLPRPEECP 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 679 KEVGEILSACWAFDLQERPSFSLLMDMLERLP 710
Cdd:cd05060  225 QEIYSIMLSCWKYRPEDRPTFSELESTFRRDP 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
445-704 2.17e-19

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: 88.98  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGR--WHGEV-AIRLLEM--------DGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAI 513
Cdd:cd06629    6 GELIGKGTYGRVYLAMnaTTGEMlAVKQVELpktssdraDSRQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGISGVVREE 592
Cdd:cd06629   86 FLEYVPGGSIGSCLRKYG-KFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDlEGICKISDFGISKKSDDIYGN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 RRENQLKLSHDWlcyLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQA--RDWPFKHQpaEALIWQIGSGEGVRR 670
Cdd:cd06629  165 NGATSMQGSVFW---MAPEVI-------HSQGQGYSAKVDIWSLGCVVLEMLAgrRPWSDDEA--IAAMFKLGNKRSAPP 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 671 VLASVSLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06629  233 VPEDVNLSPEALDFLNACFAIDPRDRPTAAELLS 266
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
442-709 2.92e-19

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: 88.36  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRGRWH------GEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACM------NPP 509
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQLKqddgsqLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFtasdlnKPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDPKTS-----LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLf 583
Cdd:cd05035   81 SPMVILPFMKHGDLHSYLLYSRLGglpekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNcMLDENMTVCVADFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 584 giSGVVREERRENQLKLSHDWLCYLAPEIVREMIpgrdedqlpFSKAADVYAFG-TVWYELQARDWPF----KHQPAEAL 658
Cdd:cd05035  160 --SRKIYSGDYYRQGRISKMPVKWIALESLADNV---------YTSKSDVWSFGvTMWEIATRGQTPYpgveNHEIYDYL 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 659 IwqigsgeGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05035  229 R-------NGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
448-707 4.05e-19

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: 87.34  E-value: 4.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG--EVAIRLLE---MDghnqdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd05034    3 LGAGQFGEVWMGVWNGttKVAVKTLKpgtMS------PEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVV--REERRENQL 598
Cdd:cd05034   77 LLDYLRTGEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCkVADFGL---ARLIedDEYTAREGA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDWLcylAPEivrEMIPGRdedqlpFSKAADVYAFGTVWYELQArdwpFKHQPAEaliwqigsGEGVRRVLASVSLG 678
Cdd:cd05034  154 KFPIKWT---APE---AALYGR------FTIKSDVWSFGILLYEIVT----YGRVPYP--------GMTNREVLEQVERG 209
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 679 ----------KEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05034  210 yrmpkppgcpDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
C1_KSR2 cd20873
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ...
194-247 4.31e-19

protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; 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. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410423  Cd Length: 57  Bit Score: 81.28  E-value: 4.31e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 194 GLSVTHRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRITFL 247
Cdd:cd20873    1 GNSIKHRFSTKYWMSQTCTVCGKGMLFGLKCKNCKLKCHNKCTKEAPPCHLLII 54
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
440-707 4.83e-19

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: 87.86  E-value: 4.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHG------EVAIRLLEMDGhNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPhLAI 513
Cdd:cd05056    6 EDITLGRCIGEGQFGDVYQGVYMSpenekiAVAVKTCKNCT-SPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgiSGVVREE 592
Cdd:cd05056   84 VMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSPDCVKLGDFGL---SRYMEDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 R--RENQLKLSHDWlcyLAPEIV--REmipgrdedqlpFSKAADVYAFGT-VWYELQARDWPFKHQPAEALIWQIGSGEg 667
Cdd:cd05056  161 SyyKASKGKLPIKW---MAPESInfRR-----------FTSASDVWMFGVcMWEILMLGVKPFQGVKNNDVIGRIENGE- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755537521 668 vrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05056  226 --RLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
438-705 6.25e-19

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: 87.53  E-value: 6.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELgepIGQGRWGRVHRGRwHGE----VAIRLLEMDGhNQDHLKLFKKEVMNYRQTRH---ENVVLFMGACMNPPH 510
Cdd:cd06917    2 LYRRLEL---VGRGSYGAVYRGY-HVKtgrvVALKVLNLDT-DDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKtsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDfglFGISGVV 589
Cdd:cd06917   77 LWIIMDYCEGGSIRTLMRAGP--IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNtGNVKLCD---FGVAASL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQLKLSHDWlcYLAPEIVREmipGRDEDQlpfskAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVR 669
Cdd:cd06917  152 NQNSSKRSTFVGTPY--WMAPEVITE---GKYYDT-----KADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPR 221
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755537521 670 rvLASVSLGKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd06917  222 --LEGNGYSPLLKEFVAACLDEEPKDRLSADELLKS 255
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
444-703 6.91e-19

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: 86.90  E-value: 6.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRG--RWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd06627    4 LGDLIGRGAFGSVYKGlnLNTGEfVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVrdpKTSLDINKT---RQIAQeIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREERREN 596
Cdd:cd06627   84 GSLASII---KKFGKFPESlvaVYIYQ-VLEGLAYLHEQGVIHRDIKGANILTtKDGLVKLADFGV--ATKLNEVEKDEN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWlcyLAPEIVrEMIpgrdedqlPFSKAADVYAFGTVWYELQARDWP-FKHQPAEALiWQIGSGEgvRRVLASv 675
Cdd:cd06627  158 SVVGTPYW---MAPEVI-EMS--------GVTTASDIWSVGCTVIELLTGNPPyYDLQPMAAL-FRIVQDD--HPPLPE- 221
                        250       260
                 ....*....|....*....|....*...
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06627  222 NISPELRDFLLQCFQKDPTLRPSAKELL 249
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
491-704 8.30e-19

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 87.08  E-value: 8.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 491 RQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY 570
Cdd:cd14043   51 RELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNCVV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 DnGKVV--ITDFGLFGISG---VVREERR-ENQLklshdwlcYLAPEIVREMIPGRDEDQlpfskAADVYAFGTVWYELQ 644
Cdd:cd14043  131 D-GRFVlkITDYGYNEILEaqnLPLPEPApEELL--------WTAPELLRDPRLERRGTF-----PGDVFSFAIIMQEVI 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 645 ARDWPFkhqpaeaLIWQIGSGEGVRRVLA-------SVSLGK---EVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14043  197 VRGAPY-------CMLGLSPEEIIEKVRSppplcrpSVSMDQaplECIQLMKQCWSEAPERRPTFDQIFD 259
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
445-704 1.04e-18

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: 86.72  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWH-GE-VAIRLLEMDGHNQD-----HLKLfKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd06631    6 GNVLGKGAYGTVYCGLTStGQlIAVKQVELDTSDKEkaekeYEKL-QEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITDFGLFG-ISGVVREERRE 595
Cdd:cd06631   85 VPGGSIASILAR-FGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNImLMPNGVIKLIDFGCAKrLCINLSSGSQS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDWLCYLAPEIVREMIPGRdedqlpfskAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLaSV 675
Cdd:cd06631  164 QLLKSMRGTPYWMAPEVINETGHGR---------KSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRL-PD 233
                        250       260
                 ....*....|....*....|....*....
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06631  234 KFSPEARDFVHACLTRDQDERPSAEQLLK 262
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
443-704 1.04e-18

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: 86.31  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR--WHGEV-AIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd08529    3 EILNKLGKGSFGVVYKVVrkVDGRVyALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLFGISGvvreerreNQ 597
Cdd:cd08529   83 NGDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGdNVKIGDLGVAKILS--------DT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIgsgegVRRVLAS 674
Cdd:cd08529  155 TNFAQTIVgtpYYLSPELCEDK---------PYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKI-----VRGKYPP 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 675 VSLG--KEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd08529  221 ISASysQDLSQLIDSCLTKDYRQRPDTTELLR 252
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
459-709 1.20e-18

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 86.45  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 459 GRWHGE-VAIRLLEMDGHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDIN 537
Cdd:cd14045   26 GIYDGRtVAIKKIAKKSFTLS--KRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIPLNWG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 538 KTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERREN----QLKLSHdwlCYLAPEI 612
Cdd:cd14045  104 FRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCkIADYGL---TTYRKEDGSENasgyQQRLMQ---VYLPPEN 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 613 vremipGRDEDQLPfSKAADVYAFGTVWYELQARDWPFkhqPAEaliwQIGSGEGVRRVLASVSLGK---------EVGE 683
Cdd:cd14045  178 ------HSNTDTEP-TQATDVYSYAIILLEIATRNDPV---PED----DYSLDEAWCPPLPELISGKtenscpcpaDYVE 243
                        250       260
                 ....*....|....*....|....*.
gi 755537521 684 ILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14045  244 LIRRCRKNNPAQRPTFEQIKKTLHKI 269
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
435-708 1.39e-18

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: 86.08  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHNQDhlklFKKEVMNYRQTRHENVVLFMGACMNPpHLAI 513
Cdd:cd05083    1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQkVAVKNIKCDVTAQA----FLEETAVMTKLQHKNLVRLLGVILHN-GLYI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSL-DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGIsgvvrE 591
Cdd:cd05083   76 VMELMSKGNLVNFLRSRGRALvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVsEDGVAKISDFGLAKV-----G 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ERRENQLKLSHDWlcyLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELqardWPFKHQPAEALiwqigsgeGVRRV 671
Cdd:cd05083  151 SMGVDNSRLPVKW---TAPEALKNK---------KFSSKSDVWSYGVLLWEV----FSYGRAPYPKM--------SVKEV 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 672 LASVSLG----------KEVGEILSACWAFDLQERPSFSLLMDMLER 708
Cdd:cd05083  207 KEAVEKGyrmeppegcpPDVYSIMTSCWEAEPGKRPSFKKLREKLEK 253
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-666 1.46e-18

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: 85.92  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14663    3 ELGRTLGEGTFAKVKFARntkTGESVAIKIIDKEQVAREGMvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISGVVREErrenq 597
Cdd:cd14663   83 TGGELFSKIAKNG-RLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEdGNLKISDFGLSALSEQFRQD----- 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 598 lKLSHDwLC----YLAPEIVREMipGRDedqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14663  157 -GLLHT-TCgtpnYVAPEVLARR--GYD------GAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGE 219
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
435-712 1.54e-18

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: 87.38  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG----------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd05101   19 WEFPRDKLTLGKPLGEGCFGQVVMAEAVGidkdkpkeavTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFVRDPKT-----SLDINKTRQ----------IAQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd05101   99 CTQDGPLYVIVEYASKGNLREYLRARRPpgmeySYDINRVPEeqmtfkdlvsCTYQLARGMEYLASQKCIHRDLAARNVL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 570 YDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QARD 647
Cdd:cd05101  179 VTENNVMkIADFGLARDINNIDYYKKTTNGRLPVKW---MAPEALFDRV---------YTHQSDVWSFGVLMWEIfTLGG 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 648 WPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPKL 712
Cdd:cd05101  247 SPYPGIPVEELFKLLKEGH---RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTL 308
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
448-709 1.58e-18

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: 86.16  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHR--GRWHGEVAI--RLLEMDGHNQdhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14221    1 LGKGCFGQAIKvtHRETGEVMVmkELIRFDEETQ---RTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL-----------FGISGVVRE 591
Cdd:cd14221   78 RGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVrENKSVVVADFGLarlmvdektqpEGLRSLKKP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ERRENQLKLSHDWlcYLAPeivrEMIPGRDEDQlpfskAADVYAFGTVWYELQARdwpfKHQPAEALIWQIGSGEGVRRV 671
Cdd:cd14221  158 DRKKRYTVVGNPY--WMAP----EMINGRSYDE-----KVDVFSFGIVLCEIIGR----VNADPDYLPRTMDFGLNVRGF 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755537521 672 L---ASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14221  223 LdryCPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETL 263
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
446-704 1.73e-18

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: 85.73  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHG---EVAIRLLEMdghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06614    6 EKIGEGASGEVYKATDRAtgkEVAIKKMRL---RKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRdpKTSLDINKTrQIA---QEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlFGISGVVREERRENQL 598
Cdd:cd06614   83 LTDIIT--QNPVRMNES-QIAyvcREVLQGLEYLHSQNVIHRDIKSDNILLSkDGSVKLADFG-FAAQLTKEKSKRNSVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHdWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWP-FKHQPAEALiWQIgSGEGVRRVLASVSL 677
Cdd:cd06614  159 GTPY-W---MAPEVIK---------RKDYGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRAL-FLI-TTKGIPPLKNPEKW 223
                        250       260
                 ....*....|....*....|....*...
gi 755537521 678 GKEVGEILSACWAFDLQERPSF-SLLMD 704
Cdd:cd06614  224 SPEFKDFLNKCLVKDPEKRPSAeELLQH 251
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
448-709 1.80e-18

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: 86.52  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-------VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAI--ITSFC 518
Cdd:cd05079   12 LGEGHFGKVELCRYDPEgdntgeqVAVKSLK-PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIklIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgiSGVVREERRENQ 597
Cdd:cd05079   91 PSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESeHQVKIGDFGL---TKAIETDKEYYT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDW-LCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARdWPFKHQPAEALIWQIGSGEG---VRRVLA 673
Cdd:cd05079  168 VKDDLDSpVFWYAPECLI---------QSKFYIASDVWSFGVTLYELLTY-CDSESSPMTLFLKMIGPTHGqmtVTRLVR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 674 SVSLGK----------EVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05079  238 VLEEGKrlprppncpeEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
445-661 2.58e-18

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: 85.73  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHG---EVAIRLLE----MDGHNQDHLKLfKKEVMNYrqTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd05581    6 GKPLGEGSYSTVVLAKEKEtgkEYAIKVLDkrhiIKEKKVKYVTI-EKEVLSR--LAHPGIVKLYYTFQDESKLYFVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFG---LFGISGvVREER 593
Cdd:cd05581   83 APNGDLLEYIRK-YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDeDMHIKITDFGtakVLGPDS-SPEST 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 594 RENQLKLSHDWLC----------YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFkHQPAEALIWQ 661
Cdd:cd05581  161 KGDADSQIAYNQAraasfvgtaeYVSPELLNEK---------PAGKSSDLWALGCIIYQMLTGKPPF-RGSNEYLTFQ 228
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
445-703 2.84e-18

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: 85.28  E-value: 2.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRG--RWHGEV-AIRLLEM---DGHNQDH----LKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd06628    5 GALIGSGSFGSVYLGmnASSGELmAVKQVELpsvSAENKDRkksmLDALQREIALLRELQHENIVQYLGSSSDANHLNIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVrDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFG------ISG 587
Cdd:cd06628   85 LEYVPGGSVATLL-NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNkGGIKISDFGISKkleansLST 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 588 VVREERreNQLKLSHDWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIgsGEG 667
Cdd:cd06628  164 KNNGAR--PSLQGSVFW---MAPEVVK---------QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKI--GEN 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755537521 668 VRRVLASvSLGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06628  228 ASPTIPS-NISSEARDFLEKTFEIDHNKRPTADELL 262
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
448-707 2.84e-18

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: 85.32  E-value: 2.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE--VAIRLLEMDGHNQDHLKLFKKEVMNYRqtrHENVVLFMGACMNPPHLAIITSFCKGRTLHS 525
Cdd:cd05113   12 LGTGQFGVVKYGKWRGQydVAIKMIKEGSMSEDEFIEEAKVMMNLS---HEKLVQLYGVCTKQRPIFIITEYMANGCLLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 526 FVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREERRENQL--KLSH 602
Cdd:cd05113   89 YLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNdQGVVKVSDFGL---SRYVLDDEYTSSVgsKFPV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 603 DWLcylAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGEGVRRV-LASvslgKE 680
Cdd:cd05113  166 RWS---PPEVLM---------YSKFSSKSDVWAFGVLMWEVYSLgKMPYERFTNSETVEHVSQGLRLYRPhLAS----EK 229
                        250       260
                 ....*....|....*....|....*..
gi 755537521 681 VGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05113  230 VYTIMYSCWHEKADERPTFKILLSNIL 256
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
440-654 4.22e-18

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: 85.10  E-value: 4.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRW---HGEVAIRLLEMDGHNQDhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYClpkKEKVAIKRIDLEKCQTS-MDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRD--PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfglFGISGVVrEER 593
Cdd:cd06610   80 LLSGGSLLDIMKSsyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGeDGSVKIAD---FGVSASL-ATG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 594 RENQLKLSHDWL---CYLAPEIVREmIPGRDEdqlpfskAADVYAFGTVWYELQARDWPFKHQP 654
Cdd:cd06610  156 GDRTRKVRKTFVgtpCWMAPEVMEQ-VRGYDF-------KADIWSFGITAIELATGAAPYSKYP 211
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
440-706 4.30e-18

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: 84.62  E-value: 4.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDHlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLGYWLNkdKVAIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERREN 596
Cdd:cd05112   81 MEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVkVSDFGM---TRFVLDDQYTS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 Q--LKLSHDWlcyLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGegvRRVLA 673
Cdd:cd05112  158 StgTKFPVKW---SSPEVFSF---SR------YSSKSDVWSFGVLMWEVFSEgKIPYENRSNSEVVEDINAG---FRLYK 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 674 SVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05112  223 PRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
435-707 5.45e-18

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: 84.73  E-value: 5.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDHlklFKKEVMNYRQTRHENVVLFMGACMNPPhLA 512
Cdd:cd05070    4 WEIPRESLQLIKRLGNGQFGEVWMGTWNGntKVAIKTLKPGTMSPES---FLEEAQIMKKLKHDKLVQLYAVVSEEP-IY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVR 590
Cdd:cd05070   80 IVTEYMSKGSLLDFLKDGEgRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICkIADFGLARLIEDNE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQlKLSHDWlcyLAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELQARDW-PFKHQPAEALIWQIGSGegvR 669
Cdd:cd05070  160 YTARQGA-KFPIKW---TAPEAA---LYGR------FTIKSDVWSFGILLTELVTKGRvPYPGMNNREVLEQVERG---Y 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05070  224 RMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
441-709 6.04e-18

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: 85.01  E-value: 6.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRG---RWHG-----EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKAtafRLKGragytTVAVKMLK-ENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPK---------------TSLDINKTRQI--------AQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd05045   80 LIVEYAKYGSLRSFLRESRkvgpsylgsdgnrnsSYLDNPDERALtmgdlisfAWQISRGMQYLAEMKLVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 570 YDNGKVV-ITDFGLfgiSGVVREErrENQLKLSHDWLC--YLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR 646
Cdd:cd05045  160 VAEGRKMkISDFGL---SRDVYEE--DSYVKRSKGRIPvkWMAIESLFDHI---------YTTQSDVWSFGVLLWEIVTL 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 647 DW-PFKHQPAEALIWQIGSGEGVRRvlaSVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05045  226 GGnPYPGIAPERLFNLLKTGYRMER---PENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
445-702 8.50e-18

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: 83.90  E-value: 8.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRG--RWHGEVAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd05085    1 GELLGKGNFGEVYKGtlKDKTPVAVKTCKEDLPQELKIK-FLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgisgvvreERRENQLKLS 601
Cdd:cd05085   80 FLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVgENNALKISDFGM---------SRQEDDGVYS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWL-----CYLAPEIVREmipGRdedqlpFSKAADVYAFGT-VWYELQARDWPFKHQPAEALIWQIGSGegvRRVLASV 675
Cdd:cd05085  151 SSGLkqipiKWTAPEALNY---GR------YSSESDVWSFGIlLWETFSLGVCPYPGMTNQQAREQVEKG---YRMSAPQ 218
                        250       260
                 ....*....|....*....|....*..
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSFSLL 702
Cdd:cd05085  219 RCPEDIYKIMQRCWDYNPENRPKFSEL 245
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
434-709 1.45e-17

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: 84.69  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG----------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMG 503
Cdd:cd05100    6 KWELSRTRLTLGKPLGEGCFGQVVMAEAIGidkdkpnkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 ACMNPPHLAIITSFCKGRTLHSFVRD---------------PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV 568
Cdd:cd05100   86 ACTQDGPLYVLVEYASKGNLREYLRArrppgmdysfdtcklPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 569 FYDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QAR 646
Cdd:cd05100  166 LVTEDNVMkIADFGLARDVHNIDYYKKTTNGRLPVKW---MAPEALFDRV---------YTHQSDVWSFGVLLWEIfTLG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 647 DWPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05100  234 GSPYPGIPVEELFKLLKEGH---RMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRV 293
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
434-707 1.52e-17

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: 83.40  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRW--HGEVAIRLLEMDGHNQDhlkLFKKEVMNYRQTRHENVVLFMGACMNPPhL 511
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEVWMGYYngHTKVAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQEP-I 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVV 589
Cdd:cd05067   77 YIITEYMENGSLVDFLKTPSGIkLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVsDTLSCKIADFGLARLIEDN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQlKLSHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARD---WPFKHQPAealiwQIGSGE 666
Cdd:cd05067  157 EYTAREGA-KFPIKW---TAPEAI---------NYGTFTIKSDVWSFGILLTEIVTHGripYPGMTNPE-----VIQNLE 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755537521 667 GVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05067  219 RGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLE 259
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
429-582 1.67e-17

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: 83.57  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 429 SVYLQEwdipFEQVELgepIGQGRWGRVHR------GRWHGEVAIRLLEMDGHNQDhlklFKKEVMNYRQTRHENVVLFM 502
Cdd:cd14046    2 SRYLTD----FEELQV---LGKGAFGQVVKvrnkldGRYYAIKKIKLRSESKNNSR----ILREVMLLSRLNHQHVVRYY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFG 581
Cdd:cd14046   71 QAWIERANLYIQMEYCEKSTLRDLIDS-GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDsNGNVKIGDFG 149

                 .
gi 755537521 582 L 582
Cdd:cd14046  150 L 150
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
448-707 1.68e-17

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: 83.28  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE--------VAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMNP-PHLaIITSFC 518
Cdd:cd05046   13 LGRGEFGEVFLAKAKGIeeeggetlVLVKALQKTKDENLQSE-FRRELDMFRKLSHKNVVRLLGLCREAePHY-MILEYT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLDINK-----TRQ---IAQEIIKGMGYLHAKGIVHKDLKSKN--VFYDNgkvvITDFGLFGISGV 588
Cdd:cd05046   91 DLGDLKQFLRATKSKDEKLKppplsTKQkvaLCTQIALGMDHLSNARFVHRDLAARNclVSSQR----EVKVSLLSLSKD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 V--REERRENQLKLSHDWLcylAPEIVREmipgrDEdqlpFSKAADVYAFGTVWYEL-QARDWPFKHQPAEALIWQIGSG 665
Cdd:cd05046  167 VynSEYYKLRNALIPLRWL---APEAVQE-----DD----FSTKSDVWSFGVLMWEVfTQGELPFYGLSDEEVLNRLQAG 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 666 EgVRRVLASvSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05046  235 K-LELPVPE-GCPSRLYKLMTRCWAVNPKDRPSFSELVSALG 274
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
436-643 2.23e-17

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 83.14  E-value: 2.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHGE--------VAIRLLEmdghNQDHLKL---FKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd05091    2 EINLSAVRFMEELGEDRFGKVYKGHLFGTapgeqtqaVAIKTLK----DKAEGPLreeFRHEAMLRSRLQHPNIVCLLGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFV--RDPKT---SLDINKTRQ----------IAQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd05091   78 VTKEQPMSMIFSYCSHGDLHEFLvmRSPHSdvgSTDDDKTVKstlepadflhIVTQIAAGMEYLSSHHVVHKDLATRNVL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 570 -YDNGKVVITDFGLFgisgvvREERRENQLKLSHDWLC---YLAPEIVremIPGRdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd05091  158 vFDKLNVKISDLGLF------REVYAADYYKLMGNSLLpirWMSPEAI---MYGK------FSIDSDIWSYGVVLWEV 220
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
446-661 2.35e-17

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: 82.92  E-value: 2.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRV----HR--GRWHgevAIRLLEMDGHNQdhlklfKKEVMNYRQTRHENVVLFMGA------CM-----NP 508
Cdd:cd14047   12 ELIGSGGFGQVfkakHRidGKTY---AIKRVKLNNEKA------EREVKALAKLDHPNIVRYNGCwdgfdyDPetsssNS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 509 P-----HLAIITSFCKGRTLHSFV-RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFG 581
Cdd:cd14047   83 SrsktkCLFIQMEFCEKGTLESWIeKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLvDTGKVKIGDFG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 582 LfgisgvVREERRENQLKLSHDWLCYLAPEivremipgrDEDQLPFSKAADVYAFGTVWYELQardWPFKHQPAEALIWQ 661
Cdd:cd14047  163 L------VTSLKNDGKRTKSKGTLSYMSPE---------QISSQDYGKEVDIYALGLILFELL---HVCDSAFEKSKFWT 224
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
438-643 3.06e-17

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: 82.31  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGRW--HGE-VAIRLLEMDGHNQDhlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHkeTGQvVAIKVVPVEEDLQE----IIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDPKTSLDinkTRQIA---QEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDfglFGISGVVR 590
Cdd:cd06612   77 MEYCGAGSVSDIMKITNKTLT---EEEIAailYQTLKGLEYLHSNKKIHRDIKAGNILLNEeGQAKLAD---FGVSGQLT 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 591 EERRENQLKLSHDwlCYLAPEIVREmipgrdedqLPFSKAADVYAFGTVWYEL 643
Cdd:cd06612  151 DTMAKRNTVIGTP--FWMAPEVIQE---------IGYNNKADIWSLGITAIEM 192
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-651 4.15e-17

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: 81.96  E-value: 4.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWG--RVHRGRWHGE-VAIRLLEMdGHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14665    3 ELVKDIGSGNFGvaRLMRDKQTKElVAVKYIER-GEKID--ENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDP-KTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG---KVVITDFGlFGISGVVreerrE 595
Cdd:cd14665   80 GGELFERICNAgRFSED--EARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpapRLKICDFG-YSKSSVL-----H 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 596 NQLKLSHDWLCYLAPEIVREmipgRDEDqlpfSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14665  152 SQPKSTVGTPAYIAPEVLLK----KEYD----GKIADVWSCGVTLYVMLVGAYPFE 199
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
445-704 4.72e-17

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: 81.97  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRG--RWHGEV----AIRLLEMDGHNqdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd06626    5 GNKIGEGTFGKVYTAvnLDTGELmamkEIRFQDNDPKT---IKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGIsgVVREERRENQ 597
Cdd:cd06626   82 QEGTLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDsNGLIKLGDFGSAVK--LKNNTTTMAP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHdWL---CYLAPEIVR-EMIPGRdedqlpfSKAADVYAFGTVWYELQA--RDWPFkHQPAEALIWQIGSGEgVRRV 671
Cdd:cd06626  159 GEVNS-LVgtpAYMAPEVITgNKGEGH-------GRAADIWSLGCVVLEMATgkRPWSE-LDNEWAIMYHVGMGH-KPPI 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 672 LASVSLGKEVGEILSACWAFDLQERPSFS-LLMD 704
Cdd:cd06626  229 PDSLQLSPEGKDFLSRCLESDPKKRPTASeLLDH 262
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
435-709 6.35e-17

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: 81.31  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRW---HGEVAIRLLEMDGHNqdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHL 511
Cdd:cd05052    1 WEIERTDITMKHKLGGGQYGEVYEGVWkkyNLTVAVKTLKEDTME---VEEFLKEAAVMKEIKHPNLVQLLGVCTREPPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRDP-KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgiSGVV 589
Cdd:cd05052   78 YIITEFMPYGNLLDYLRECnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVgENHLVKVADFGL---SRLM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REE--RRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQArdWPFKHQPAEALIWQIGSGEG 667
Cdd:cd05052  155 TGDtyTAHAGAKFPIKW---TAPESLAYNK---------FSIKSDVWAFGVLLWEIAT--YGMSPYPGIDLSQVYELLEK 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 668 VRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05052  221 GYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
448-643 7.67e-17

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: 81.53  E-value: 7.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGR----VHRGRWHGEVAIRLLEMDGHNQdhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14222    1 LGKGFFGQaikvTHKATGKVMVMKELIRCDEETQ---KTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREER--------- 593
Cdd:cd14222   78 KDFLRA-DDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKlDKTVVVADFGL---SRLIVEEKkkpppdkpt 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 594 ------RENQLKLSHDWL---CYLAPeivrEMIPGRDEDQlpfskAADVYAFGTVWYEL 643
Cdd:cd14222  154 tkkrtlRKNDRKKRYTVVgnpYWMAP----EMLNGKSYDE-----KVDIFSFGIVLCEI 203
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
445-702 9.76e-17

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: 80.75  E-value: 9.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHGE---VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADntpVAVKSCR-ETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgvVREER------- 593
Cdd:cd05084   80 DFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLkISDFGM------SREEEdgvyaat 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 ---RENQLKlshdwlcYLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYELQARDW-----PFKHQPAEALiwqigsg 665
Cdd:cd05084  154 ggmKQIPVK-------WTAPEALNY---GR------YSSESDVWSFGILLWETFSLGAvpyanLSNQQTREAV------- 210
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 755537521 666 EGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLL 702
Cdd:cd05084  211 EQGVRLPCPENCPDEVYRLMEQCWEYDPRKRPSFSTV 247
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
444-709 1.33e-16

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: 80.75  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGRWHGE------VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP-----PHLA 512
Cdd:cd14204   11 LGKVLGEGEFGSVMEGELQQPdgtnhkVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVgsqriPKPM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFV------RDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLfgi 585
Cdd:cd14204   91 VILPFMKYGDLHSFLlrsrlgSGPQ-HVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNcMLRDDMTVCVADFGL--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 586 SGVVREERRENQLKLSHDWLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDW-PF----KHQPAEALIw 660
Cdd:cd14204  167 SKKIYSGDYYRQGRIAKMPVKWIAVESLADRV---------YTVKSDVWAFGVTMWEIATRGMtPYpgvqNHEIYDYLL- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 661 qigsgEGVRRVLASVSLgKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14204  237 -----HGHRLKQPEDCL-DELYDIMYSCWRSDPTDRPTFTQLRENLEKL 279
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
446-646 1.43e-16

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 80.95  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE-VAIRLLEmdghNQDHLKLFkKEVMNYrQT---RHENVVLFMGACMNP----PHLAIITSF 517
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEdVAVKIFS----SREERSWF-REAEIY-QTvmlRHENILGFIAADNKDngtwTQLWLVSDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfgisgV 588
Cdd:cd14143   75 HEHGSLFDYLN--RYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVkKNGTCCIADLGL-----A 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 589 VREERRENQLKLSHDWLC----YLAPEIVREMIPGRDEDQLpfsKAADVYAFGTVWYELQAR 646
Cdd:cd14143  148 VRHDSATDTIDIAPNHRVgtkrYMAPEVLDDTINMKHFESF---KRADIYALGLVFWEIARR 206
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
435-707 1.51e-16

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: 80.50  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDhlkLFKKEVMNYRQTRHENVVLFMGACMNPPhLA 512
Cdd:cd05071    4 WEIPRESLRLEVKLGQGCFGEVWMGTWNGttRVAIKTLKPGTMSPE---AFLQEAQVMKKLRHEKLVQLYAVVSEEP-IY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVR-DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVR 590
Cdd:cd05071   80 IVTEYMSKGSLLDFLKgEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVgENLVCKVADFGLARLIEDNE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQlKLSHDWlcyLAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELQARDW-PFKHQPAEALIWQIGSGegvR 669
Cdd:cd05071  160 YTARQGA-KFPIKW---TAPEAA---LYGR------FTIKSDVWSFGILLTELTTKGRvPYPGMVNREVLDQVERG---Y 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05071  224 RMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
448-646 1.55e-16

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 80.60  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAIRLLemdghnqdhlkLFKKEVMNYRQT--------RHENVVLFMGACMNP----PHLAII 514
Cdd:cd14144    3 VGKGRYGEVWKGKWRGEkVAVKIF-----------FTTEEASWFRETeiyqtvlmRHENILGFIAADIKGtgswTQLYLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfgi 585
Cdd:cd14144   72 TDYHENGSLYDFLR--GNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVkKNGTCCIADLGL--- 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 586 sgVVREERRENQLKLSHDWLC----YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQAR 646
Cdd:cd14144  147 --AVKFISETNEVDLPPNTRVgtkrYMAPEVLDESL---NRNHFDAYKMADMYSFGLVLWEIARR 206
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
448-709 1.66e-16

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: 79.87  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFV 527
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVR-EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 528 RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY---DNGK-VVITDFGLFGISGVVREERRENQLKL--S 601
Cdd:cd14156   80 AREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGReAVVTDFGLAREVGEMPANDPERKLSLvgS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVRemipGRdedqlPFSKAADVYAFGTVWYELQARdwpfkhQPAEALIWQIGSGEGVrrvlaSVSLGKE- 680
Cdd:cd14156  160 AFW---MAPEMLR----GE-----PYDRKVDVFSFGIVLCEILAR------IPADPEVLPRTGDFGL-----DVQAFKEm 216
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755537521 681 -------VGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14156  217 vpgcpepFLDLAASCCRMDAFKRPSFAELLDELEDI 252
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
441-711 2.07e-16

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: 80.05  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRGRWHGE-----VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP------P 509
Cdd:cd05075    1 KLALGKTLGEGEFGSVMEGQLNQDdsvlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNtesegyP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVR-----DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLf 583
Cdd:cd05075   81 SPVVILPFMKHGDLHSFLLysrlgDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNcMLNENMNVCVADFGL- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 584 giSGVVREERRENQLKLSHDWLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQI 662
Cdd:cd05075  160 --SKKIYNGDYYRQGRISKMPVKWIAIESLADRV---------YTTKSDVWSFGVTMWEIATRgQTPYPGVENSEIYDYL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 663 GSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd05075  229 RQGN---RLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILK 274
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
438-658 2.52e-16

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: 79.69  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGR--WHGEVA-IRLLEMDghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKARnlHTGELAaVKIIKLE--PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWIC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSF--VRDPKTSLDInktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFG-ISGVVr 590
Cdd:cd06646   85 MEYCGGGSLQDIyhVTGPLSELQI---AYVCRETLQGLAYLHSKGKMHRDIKGANILLtDNGDVKLADFGVAAkITATI- 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 591 eERRENQLKLSHdwlcYLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYELQARDWP-FKHQPAEAL 658
Cdd:cd06646  161 -AKRKSFIGTPY----WMAPEVAAV------EKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRAL 218
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
476-704 3.34e-16

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: 79.44  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 476 NQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHA 555
Cdd:cd14098   41 NDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDFIMA-WGAIPEQHARELTKQILEAMAYTHS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 556 KGIVHKDLKSKN--VFYDNGKVV-ITDFGLFGISGvvreerRENQLKLSHDWLCYLAPEIVRemipGRDEDQLP-FSKAA 631
Cdd:cd14098  120 MGITHRDLKPENilITQDDPVIVkISDFGLAKVIH------TGTFLVTFCGTMAYLAPEILM----SKEQNLQGgYSNLV 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 632 DVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14098  190 DMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALD 262
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
446-662 3.58e-16

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: 79.26  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE---VAIRLLEmdghnqdhlKLFKKEVMNY-RQTR---HENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14010    6 DEIGRGKHSVVYKGRRKGTiefVAIKCVD---------KSKRPEVLNEvRLTHelkHPNVLKFYEWYETSNHLWLVVEYC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL-----------FGIS 586
Cdd:cd14010   77 TGGDLETLLRQ-DGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDgNGTLKLSDFGLarregeilkelFGQF 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 587 GVVREERRENQLKLSHDWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd14010  156 SDEGNVNKVSKKQAKRGTPYYMAPELFQGG---------VHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKI 222
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
448-709 4.03e-16

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: 79.25  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG------RWHGEVAIRLLEMdGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd05063   13 IGAGEFGEVFRGilkmpgRKEVAVAIKTLKP-GYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisGVVREERRENQL-- 598
Cdd:cd05063   92 ALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECkVSDFGL----SRVLEDDPEGTYtt 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 ---KLSHDWlcyLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQArdwpFKHQPaealIWQIGSGEGVR------ 669
Cdd:cd05063  168 sggKIPIRW---TAPEAIAYR---------KFTSASDVWSFGIVMWEVMS----FGERP----YWDMSNHEVMKaindgf 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05063  228 RLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
436-708 4.40e-16

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: 79.69  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVH---------------RGRW-HGE---VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHE 496
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGEVHlceanglsdltsddfIGNDnKDEpvlVAVKMLR-PDASKNAREDFLKEVKIMSQLKDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 497 NVVLFMGACMNPPHLAIITSFCKGRTLHSFVRD--PKTSLDINKTRQ---------IAQEIIKGMGYLHAKGIVHKDLKS 565
Cdd:cd05051   80 NIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKheAETQGASATNSKtlsygtllyMATQIASGMKYLESLNFVHRDLAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 566 KNVFYDNG-KVVITDFGL---------FGISGvvreerrenqlklshdwlcylapeivREMIPGR---DEDQL--PFSKA 630
Cdd:cd05051  160 RNCLVGPNyTIKIADFGMsrnlysgdyYRIEG--------------------------RAVLPIRwmaWESILlgKFTTK 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 631 ADVYAFG-TVW--YELqARDWPFKHQPAEALIWQIGSG---EGVRRVLASVSL-GKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd05051  214 SDVWAFGvTLWeiLTL-CKEQPYEHLTDEQVIENAGEFfrdDGMEVYLSRPPNcPKEIYELMLECWRRDEEDRPTFREIH 292

                 ....*
gi 755537521 704 DMLER 708
Cdd:cd05051  293 LFLQR 297
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
448-719 4.57e-16

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: 78.46  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKlfkKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd14006    1 LGRGRFGVVKRCIEKAtgrEFAAKFIPKRDKKKEAVL---REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG---KVVITDFGLfgisgvVREERRENQLKLS 601
Cdd:cd14006   78 DRLAERG-SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRpspQIKIIDFGL------ARKLNPGEELKEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFkhqpaealiwqigSGEGVRRVLASVSLGKev 681
Cdd:cd14006  151 FGTPEFVAPEIVN---------GEPVSLATDMWSIGVLTYVLLSGLSPF-------------LGEDDQETLANISACR-- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 682 geilsacWAFDlqeRPSFSLL----MDMLERLPKLNRR--------LSHP 719
Cdd:cd14006  207 -------VDFS---EEYFSSVsqeaKDFIRKLLVKEPRkrptaqeaLQHP 246
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
440-699 5.74e-16

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 78.83  E-value: 5.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGepigQGRWGRVHRGRWHGE-----VAIRLLEmdghnQDHLKLFKKEVMNYRQTRHE----NVVLFMGACmNPPH 510
Cdd:cd05115    8 DEVELG----SGNFGCVKKGVYKMRkkqidVAIKVLK-----QGNEKAVRDEMMREAQIMHQldnpYIVRMIGVC-EAEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVV 589
Cdd:cd05115   78 LMLVMEMASGGPLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAkISDFGL---SKAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQLKLSHDW-LCYLAPEIVremipgrdeDQLPFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIgsgEG 667
Cdd:cd05115  155 GADDSYYKARSAGKWpLKWYAPECI---------NFRKFSSRSDVWSYGvTMWEAFSYGQKPYKKMKGPEVMSFI---EQ 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 668 VRRVLASVSLGKEVGEILSACWAFDLQERPSF 699
Cdd:cd05115  223 GKRMDCPAECPPEMYALMSDCWIYKWEDRPNF 254
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
432-709 6.41e-16

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: 78.81  E-value: 6.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 432 LQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGE------VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd05074    1 LKDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEdgsfqkVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNP------PHLAIITSFCKGRTLHSF-----VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NG 573
Cdd:cd05074   81 LRSrakgrlPIPMVILPFMKHGDLHTFllmsrIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNeNM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 574 KVVITDFGLFGISGVVREERRENQLKLSHDWLcylAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKH 652
Cdd:cd05074  161 TVCVADFGLSKKIYSGDYYRQGCASKLPVKWL---ALESLADNV---------YTTHSDVWAFGVTMWEIMTRgQTPYAG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 653 -QPAEALIWQIGsGEGVRRVLASVSlgkEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05074  229 vENSEIYNYLIK-GNRLKQPPDCLE---DVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
435-707 6.74e-16

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: 78.54  E-value: 6.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNqdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNstKVAVKTLKPGTMS---VQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVR-DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVR 590
Cdd:cd05072   79 IITEYMAKGSLLDFLKsDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCkIADFGL---ARVIE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EER---RENQlKLSHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGE 666
Cdd:cd05072  156 DNEytaREGA-KFPIKW---TAPEAI---------NFGSFTIKSDVWSFGILLYEIVTYgKIPYPGMSNSDVMSALQRGY 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755537521 667 GVRRVlasVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05072  223 RMPRM---ENCPDELYDIMKTCWKEKAEERPTFDYLQSVLD 260
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
435-707 7.08e-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: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDhlkLFKKEVMNYRQTRHENVVLFMGACMNPPhLA 512
Cdd:cd05069    7 WEIPRESLRLDVKLGQGCFGEVWMGTWNGttKVAIKTLKPGTMMPE---AFLQEAQIMKKLRHDKLVPLYAVVSEEP-IY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVR 590
Cdd:cd05069   83 IVTEFMGKGSLLDFLKEGDGKyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVgDNLVCKIADFGLARLIEDNE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQlKLSHDWlcyLAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELQARDW-PFKHQPAEALIWQIGSGegvR 669
Cdd:cd05069  163 YTARQGA-KFPIKW---TAPEAA---LYGR------FTIKSDVWSFGILLTELVTKGRvPYPGMVNREVLEQVERG---Y 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05069  227 RMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
460-700 7.52e-16

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: 78.31  E-value: 7.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 460 RWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC-KGRTLHSFvrdPKTSLDINK 538
Cdd:cd14027   15 RTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMeKGNLMHVL---KKVSVPLSV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 539 TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLFGI---SGVVREE-RRENQLKLSHD----WLCYLA 609
Cdd:cd14027   92 KGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDfHIKIADLGLASFkmwSKLTKEEhNEQREVDGTAKknagTLYYMA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 610 PEIVremipgRDEDQLPFSKaADVYAFGTVWYELQARDWPFKHQPAE-ALIWQIGSGEGVRRVLASVSLGKEVGEILSAC 688
Cdd:cd14027  172 PEHL------NDVNAKPTEK-SDVYSFAIVLWAIFANKEPYENAINEdQIIMCIKSGNRPDVDDITEYCPREIIDLMKLC 244
                        250
                 ....*....|..
gi 755537521 689 WAFDLQERPSFS 700
Cdd:cd14027  245 WEANPEARPTFP 256
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
434-706 7.98e-16

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: 78.69  E-value: 7.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGidksatcrTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNPPH-LAIITSFCKGRTLHSFVR------------DPKTSLDINKTRQIAQE-------------IIKGMGYLHAKGIV 559
Cdd:cd05054   81 TKPGGpLMVIVEFCKFGNLSNYLRskreefvpyrdkGARDVEEEEDDDELYKEpltledlicysfqVARGMEFLASRKCI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 560 HKDLKSKNVFYDNGKVV-ITDFGL----FGISGVVREERRENQLKlshdwlcYLAPEIVREMIpgrdedqlpFSKAADVY 634
Cdd:cd05054  161 HRDLAARNILLSENNVVkICDFGLardiYKDPDYVRKGDARLPLK-------WMAPESIFDKV---------YTTQSDVW 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 635 AFGTVWYE---LQARDWPfKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05054  225 SFGVLLWEifsLGASPYP-GVQMDEEFCRRLKEGT---RMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
448-707 8.73e-16

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: 78.23  E-value: 8.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG---------RWHGEVAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACM-NPPHLaIITSF 517
Cdd:cd05044    3 LGSGAFGEVFEGtakdilgdgSGETKVAVKTLRKGATDQEKAE-FLKEAHLMSNFKHPNILKLLGVCLdNDPQY-IILEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTS------LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-----YDNGKVVITDFGLfgis 586
Cdd:cd05044   81 MEGGDLLSYLRAARPTaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLvsskdYRERVVKIGDFGL---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 gvVRE------ERRENQLKLSHDWLcylAPEivrEMIPGRdedqlpFSKAADVYAFGTVWYELQArdwpFKHQPAEALIW 660
Cdd:cd05044  157 --ARDiykndyYRKEGEGLLPVRWM---APE---SLVDGV------FTTQSDVWAFGVLMWEILT----LGQQPYPARNN 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 661 QigsgegvrRVLASVSLG----------KEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05044  219 L--------EVLHFVRAGgrldqpdncpDDLYELMLRCWSTDPEERPSFARILEQLQ 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
443-662 8.83e-16

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: 78.11  E-value: 8.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRW--HG-EVAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14162    3 IVGKTLGHGSYAVVKKAYStkHKcKVAIKIVSKKKAPEDYLqKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERR--E 595
Cdd:cd14162   83 ENGDLLDYIRK-NGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDkNNNLKITDFGF------ARGVMKtkD 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 596 NQLKLSHDWlC----YLAPEIVRemipGRDEDqlPFskAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd14162  156 GKPKLSETY-CgsyaYASPEILR----GIPYD--PF--LSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV 217
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
448-646 9.17e-16

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: 77.90  E-value: 9.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGEVAIrlLEMDGHNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHS 525
Cdd:cd14155    1 IGSGFFSEVYkvRHRTSGQVMA--LKMNTLSSNRANMLR-EVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 526 FVrDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY---DNG-KVVITDFGLFGISGVVREERRENQLKLS 601
Cdd:cd14155   78 LL-DSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGyTAVVGDFGLAEKIPDYSDGKEKLAVVGS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 602 HDWlcyLAPEIVremipgRDEdqlPFSKAADVYAFGTVWYELQAR 646
Cdd:cd14155  157 PYW---MAPEVL------RGE---PYNEKADVFSYGIILCEIIAR 189
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
436-709 1.04e-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: 78.20  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHGE--------VAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMN 507
Cdd:cd05036    2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMpgdpsplqVAVKTLPELCSEQDEMD-FLMEALIMSKFNHPNIVRCIGVCFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 508 P-PHLaIITSFCKGRTLHSFVRD--PKT----SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN---GKVV- 576
Cdd:cd05036   81 RlPRF-ILLELMAGGDLKSFLREnrPRPeqpsSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCkgpGRVAk 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 577 ITDFGLfgISGVVREE--RRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTvwyelqardwpfkhqp 654
Cdd:cd05036  160 IGDFGM--ARDIYRADyyRKGGKAMLPVKW---MPPEAFLDGI---------FTSKTDVWSFGV---------------- 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 655 aeaLIWQIGS-------GEGVRRVLASVSLGKE----------VGEILSACWAFDLQERPSFSLLmdmLERL 709
Cdd:cd05036  210 ---LLWEIFSlgympypGKSNQEVMEFVTSGGRmdppkncpgpVYRIMTQCWQHIPEDRPNFSTI---LERL 275
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
439-704 1.30e-15

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: 77.45  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPI--GQGRWGRVHRGR-WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd06624    5 YEYDESGERVvlGKGTFGVVYAARdLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDPKTSLDINKTRQI--AQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFG----LFGISG 587
Cdd:cd06624   85 EQVPGGSLSALLRSKWGPLKDNENTIGyyTKQILEGLKYLHDNKIVHRDIKGDNVLVNtySGVVKISDFGtskrLAGINP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 588 VVREERRENQlklshdwlcYLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQARDWPF-KHQPAEALIWQIGSGE 666
Cdd:cd06624  165 CTETFTGTLQ---------YMAPEVI-------DKGQRGYGPPADIWSLGCTIIEMATGKPPFiELGEPQAAMFKVGMFK 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 667 GVRRVLASVSlgKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06624  229 IHPEIPESLS--EEAKSFILRCFEPDPDKRATASDLLQ 264
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-653 1.36e-15

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: 77.50  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWG--RVHRGRWHGE-VAIRLLEMdGHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14662    3 ELVKDIGSGNFGvaRLMRNKETKElVAVKYIER-GLKID--ENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDP-KTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG---KVVITDFGlFGISGVVreerrE 595
Cdd:cd14662   80 GGELFERICNAgRFSED--EARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpapRLKICDFG-YSKSSVL-----H 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 596 NQLKLSHDWLCYLAPEIVREmipgRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14662  152 SQPKSTVGTPAYIAPEVLSR----KEYD----GKVADVWSCGVTLYVMLVGAYPFEDP 201
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
444-698 1.42e-15

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: 77.40  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVH------RGRwhgEVAIRLLEMDGHNQD---HLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd06625    4 QGKLLGQGAFGQVYlcydadTGR---ELAVKQVEIDPINTEaskEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfglFGISGVVREER 593
Cdd:cd06625   81 MEYMPGGSVKDEIKA-YGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDsNGNVKLGD---FGASKRLQTIC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 RENQLKLSHDWLCYLAPEIvremIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLA 673
Cdd:cd06625  157 SSTGMKSVTGTPYWMSPEV----INGEG-----YGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLPP 227
                        250       260
                 ....*....|....*....|....*
gi 755537521 674 SVSlgKEVGEILSACWAFDLQERPS 698
Cdd:cd06625  228 HVS--EDARDFLSLIFVRNKKQRPS 250
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
448-646 1.59e-15

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: 77.79  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLemdghNQDHLKLF--KKEVMNYRQTRHENVVLFMGACMNPP------HLAIITSFC 518
Cdd:cd14054    3 IGQGRYGTVWKGSLDErPVAVKVF-----PARHRQNFqnEKDIYELPLMEHSNILRFIGADERPTadgrmeYLLVLEYAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGrTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK---------GIVHKDLKSKNVFYDN-GKVVITDFG----LFG 584
Cdd:cd14054   78 KG-SLCSYLR--ENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKAdGSCVICDFGlamvLRG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 585 ISGVVREERRENQLKLSH-DWLCYLAPEIVREMIPGRD-EDQLpfsKAADVYAFGTVWYELQAR 646
Cdd:cd14054  155 SSLVRGRPGAAENASISEvGTLRYMAPEVLEGAVNLRDcESAL---KQVDVYALGLVLWEIAMR 215
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
445-704 1.68e-15

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: 77.20  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRG-------RWhgevAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14097    6 GRKLGQGSFGVVIEAthketqtKW----AIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVrDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY--------DNGKVVITDFGLfgisGVV 589
Cdd:cd14097   82 CEDGELKELL-LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnnDKLNIKVTDFGL----SVQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQLKLSHDWLCYLAPEIvremIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVR 669
Cdd:cd14097  157 KYGLGEDMLQETCGTPIYMAPEV----ISAHG-----YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTF 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 670 RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14097  228 TQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLD 262
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
436-706 1.74e-15

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: 77.71  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHG-----------------EVAIRLLEMDGhNQDHLKLFKKEVMNYRQTRHENV 498
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGlaeflgegapefdgqpvLVAVKMLRADV-TKTARNDFLKEIKIMSRLKNPNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 499 VLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQI-----------AQEIIKGMGYLHAKGIVHKDLKSKN 567
Cdd:cd05097   80 IRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIESTFTHANNIpsvsianllymAVQIASGMKYLASLNFVHRDLATRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 568 VFYDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDWLCYlapeivREMIPGRdedqlpFSKAADVYAFGTVWYEL--Q 644
Cdd:cd05097  160 CLVGNHYTIkIADFGMSRNLYSGDYYRIQGRAVLPIRWMAW------ESILLGK------FTTASDVWAFGVTLWEMftL 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 645 ARDWPFKHQPAEALIWQIGS---GEGVRRVLASVSL-GKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05097  228 CKEQPYSLLSDEQVIENTGEffrNQGRQIYLSQTPLcPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
440-653 1.88e-15

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: 76.86  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRG--RWHGE-VAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVrhKPTGKiYALKKIHVD-GDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTsldINKT--RQIAQEIIKGMGYLHAK-GIVHKDLKSKNVFYD-NGKVVITDfglFGISGVVree 592
Cdd:cd06623   80 YMDGGSLADLLKKVGK---IPEPvlAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINsKGEVKIAD---FGISKVL--- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 593 rrENQLKLSHDW---LCYLAPEivRemIPGRdedqlPFSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd06623  151 --ENTLDQCNTFvgtVTYMSPE--R--IQGE-----SYSYAADIWSLGLTLLECALGKFPFLPP 203
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
446-709 1.91e-15

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: 77.14  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVH--RGRWHGE-VAIRLL---EMDGHNQ-DHLKLFKKEVMNyrQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd05611    2 KPISKGAFGSVYlaKKRSTGDyFAIKVLkksDMIAKNQvTNVKAERAIMMI--QGESPYVAKLYYSFQSKDYLYLVMEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVrdpKT--SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgiSGVVREERRE 595
Cdd:cd05611   80 NGGDCASLI---KTlgGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQtGHLKLTDFGL---SRNGLEKRHN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDwlcYLAPEIvremIPGRDEDqlpfsKAADVYAFGTVWYELQARDWPFKHQPAEAlIWQigsgegvrRVLAS- 674
Cdd:cd05611  154 KKFVGTPD---YLAPET----ILGVGDD-----KMSDWWSLGCVIFEFLFGYPPFHAETPDA-VFD--------NILSRr 212
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 675 VSLGKEVGEILSAcWAFDLQERpsfSLLMDMLERL 709
Cdd:cd05611  213 INWPEEVKEFCSP-EAVDLINR---LLCMDPAKRL 243
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
443-643 2.10e-15

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: 76.96  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR--WHGE-VAIRLLEMDghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd06613    3 ELIQRIGSGTYGDVYKARniATGElAAVKVIKLE--PGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHsfvrdpktslDI-NKTR-----QIA---QEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDfglFGISGVV 589
Cdd:cd06613   81 GGSLQ----------DIyQVTGplselQIAyvcRETLKGLAYLHSTGKIHRDIKGANILLtEDGDVKLAD---FGVSAQL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 590 RE--ERRENQLKLSHdWlcyLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd06613  148 TAtiAKRKSFIGTPY-W---MAPEVAAV------ERKGGYDGKCDIWALGITAIEL 193
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
448-702 4.70e-15

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 75.77  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-----VAIRLLEMDGHN---QDHLkLFKKEVMnyRQTRHENVVLFMGACmNPPHLAIITSFCK 519
Cdd:cd05116    3 LGSGNFGTVKKGYYQMKkvvktVAVKILKNEANDpalKDEL-LREANVM--QQLDNPYIVRMIGIC-EAESWMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERRENQL 598
Cdd:cd05116   79 LGPLNKFLQKNRHVTEKNIT-ELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAkISDFGL---SKALRADENYYKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDW-LCYLAPEIVremipgrdeDQLPFSKAADVYAFGTV-WYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVS 676
Cdd:cd05116  155 QTHGKWpVKWYAPECM---------NYYKFSSKSDVWSFGVLmWEAFSYGQKPYKGMKGNEVTQMIEKGE---RMECPAG 222
                        250       260
                 ....*....|....*....|....*.
gi 755537521 677 LGKEVGEILSACWAFDLQERPSFSLL 702
Cdd:cd05116  223 CPPEMYDLMKLCWTYDVDERPGFAAV 248
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
443-699 5.03e-15

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 75.59  E-value: 5.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---------EVAIRLLEMDGHNQDhLKLFKKEVMnYRQTRHENVVLFMGACMNPPHLaI 513
Cdd:cd05037    2 TFHEHLGQGTFTNIYDGILREvgdgrvqevEVLLKVLDSDHRDIS-ESFFETASL-MSQISHKHLVKLYGVCVADENI-M 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLFGIS-GV 588
Cdd:cd05037   79 VQEYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregLDGYPPFIKLSDPGVPiTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKlshdwlcYLAPEIVRemipgrdEDQLPFSKAADVYAFGTVWYELQAR-DWPFK-HQPAEALIWQigsge 666
Cdd:cd05037  159 LSREERVDRIP-------WIAPECLR-------NLQANLTIAADKWSFGTTLWEICSGgEEPLSaLSSQEKLQFY----- 219
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 667 GVRRVLASVSLGkEVGEILSACWAFDLQERPSF 699
Cdd:cd05037  220 EDQHQLPAPDCA-ELAELIMQCWTYEPTKRPSF 251
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
435-707 6.18e-15

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: 76.16  E-value: 6.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVH--------RGRWHGEVAIRLLEMDGHNQDHLKLFKK-EVMNYRQTRHenVVLFMGAC 505
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYegnardiiKGEAETRVAVKTVNESASLRERIEFLNEaSVMKGFTCHH--VVRLLGVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MN-PPHLAIITSFCKGrTLHSFVRDPKTSLDINKTR---------QIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGK 574
Cdd:cd05061   79 SKgQPTLVVMELMAHG-DLKSYLRSLRPEAENNPGRppptlqemiQMAAEIADGMAYLNAKKFVHRDLAARNcMVAHDFT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 575 VVITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQArdwpFKHQP 654
Cdd:cd05061  158 VKIGDFGMTRDIYETDYYRKGGKGLLPVRW---MAPESLKDGV---------FTTSSDMWSFGVVLWEITS----LAEQP 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 655 AEALiwqigSGEGVRR-VLASVSLGK------EVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05061  222 YQGL-----SNEQVLKfVMDGGYLDQpdncpeRVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
437-709 6.66e-15

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: 75.49  E-value: 6.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 437 IPFEQVELGEPIGQGRWGRVHRGRWH--GE----VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPH 510
Cdd:cd05033    1 IDASYVTIEKVIGGGEFGEVCSGSLKlpGKkeidVAIKTLK-SGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVV 589
Cdd:cd05033   80 VMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCkVSDFGLSRRLEDS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGegv 668
Cdd:cd05033  160 EATYTTKGGKIPIRW---TAPEAIAYRK---------FTSASDVWSFGIVMWEVMSYgERPYWDMSNQDVIKAVEDG--- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 755537521 669 RRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05033  225 YRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
434-713 9.31e-15

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 76.17  E-value: 9.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGidktatcrTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNP--PhLAIITSFCKGRTLHSFVRDPKTSLDINKTR-----------------------QIAQ---------------- 544
Cdd:cd05103   81 TKPggP-LMVIVEFCKFGNLSAYLRSKRSEFVPYKTKgarfrqgkdyvgdisvdlkrrldSITSsqssassgfveeksls 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 ---------------------------EIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREER--R 594
Cdd:cd05103  160 dveeeeagqedlykdfltledlicysfQVAKGMEFLASRKCIHRDLAARNILLsENNVVKICDFGL--ARDIYKDPDyvR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 595 ENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYE---LQARDWPFKHQPaEALIWQIGSGEgvrRV 671
Cdd:cd05103  238 KGDARLPLKW---MAPETIFDRV---------YTIQSDVWSFGVLLWEifsLGASPYPGVKID-EEFCRRLKEGT---RM 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 755537521 672 LASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPKLN 713
Cdd:cd05103  302 RAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQAN 343
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
448-646 1.02e-14

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 75.46  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAIRLLemdgHNQDHLKLFKK-EVMNYRQTRHENVVLFMGACMNP----PHLAIITSFCKGR 521
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEkVAVKVF----FTTEEASWFREtEIYQTVLMRHENILGFIAADIKGtgswTQLYLITDYHENG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfgisgVVREE 592
Cdd:cd14220   79 SLYDFLK--CTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkKNGTCCIADLGL-----AVKFN 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 593 RRENQLKLSHDWLC----YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQAR 646
Cdd:cd14220  152 SDTNEVDVPLNTRVgtkrYMAPEVLDESL---NKNHFQAYIMADIYSFGLIIWEMARR 206
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-703 1.04e-14

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: 74.61  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHGE---VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd08225    3 EIIKKIGEGSFGKIYLAKAKSDsehCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSfvrdpktslDINKTR-------QIAQ---EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVviTDFGLFGISGV 588
Cdd:cd08225   83 GGDLMK---------RINRQRgvlfsedQILSwfvQISLGLKHIHDRKILHRDIKSQNIFLSkNGMV--AKLGDFGIARQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKLSHDWlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgv 668
Cdd:cd08225  152 LNDSMELAYTCVGTPY--YLSPEICQNR---------PYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGY-- 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 755537521 669 rrvLASVSLG--KEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd08225  219 ---FAPISPNfsRDLRSLISQLFKVSPRDRPSITSIL 252
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
443-665 1.06e-14

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: 74.61  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG--EVAIRLLEMDG-HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14161    6 EFLETLGKGTYGRVKKARDSSgrLVAIKSIRKDRiKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYAS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGISgvvreeRRENQL 598
Cdd:cd14161   86 RGDLYDYISE-RQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDaNGNIKIADFGLSNLY------NQDKFL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 599 KLSHDWLCYLAPEIVRemipGRdedqlPFS-KAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSG 665
Cdd:cd14161  159 QTYCGSPLYASPEIVN----GR-----PYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSG 217
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
443-643 1.34e-14

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: 74.43  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwhgE------VAIRLLEMD---GHNQDHLklFKKEVMNYRQTRHENVVLFMGACMNPPHLAI 513
Cdd:cd14007    3 EIGKPLGKGKFGNVYLAR---EkksgfiVALKVISKSqlqKSGLEHQ--LRREIEIQSHLRHPNILRLYGYFEDKKRIYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREE 592
Cdd:cd14007   78 ILEYAPNGELYKELKK-QKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGsNGELKLADFGW---SVHAPSN 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 593 RRENqlklshdwLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd14007  154 RRKT--------FCgtldYLPPEMVEGK---------EYDYKVDIWSLGVLCYEL 191
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
538-652 1.36e-14

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: 74.70  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 538 KTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlFGISGVVREERREnqlklshdwLC----YLAPEI 612
Cdd:cd14093  110 KTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDdNLNVKISDFG-FATRLDEGEKLRE---------LCgtpgYLAPEV 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755537521 613 VR-EMIPGRDEdqlpFSKAADVYAFGTVWYELQARDWPFKH 652
Cdd:cd14093  180 LKcSMYDNAPG----YGKEVDMWACGVIMYTLLAGCPPFWH 216
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
440-666 1.36e-14

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: 75.17  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRW----HGEVAIRLLEMDGHNQDHLKLFK-----KEVMNYRQTRHENVVLFMGACMNPPH 510
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVPlrntGKPVAIKVVRKADLSSDNLKGSSranilKEVQIMKRLSHPNIVKLLDFQESDEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTL-HSFVRDPKTSLDInkTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----------------- 572
Cdd:cd14096   81 YYIVLELADGGEIfHQIVRLTYFSEDL--SRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkaddde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 573 -----------------GKVVITDFGLfgiSGVVreerRENQLKLSHDWLCYLAPEIVremipgRDEDqlpFSKAADVYA 635
Cdd:cd14096  159 tkvdegefipgvggggiGIVKLADFGL---SKQV----WDSNTKTPCGTVGYTAPEVV------KDER---YSKKVDMWA 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 755537521 636 FGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14096  223 LGCVLYTLLCGFPPFYDESIETLTEKISRGD 253
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
439-703 1.78e-14

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: 74.76  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRVHRGRW--HGEVA-IRLLEMDGHNQDHLKlfkKEV-MNYRQTRHENVVLFMGACM--NPP--- 509
Cdd:cd06637    8 FELVEL---VGNGTYGQVYKGRHvkTGQLAaIKVMDVTGDEEEEIK---QEInMLKKYSHHRNIATYYGAFIkkNPPgmd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 -HLAIITSFCKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgIS 586
Cdd:cd06637   82 dQLWLVMEFCGAGSVTDLIKNTKgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLtENAEVKLVDFGV--SA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 GVVREERRENQLKLSHDWlcyLAPEIVremipGRDED-QLPFSKAADVYAFGTVWYELQARDWPF-KHQPAEALiWQIGS 664
Cdd:cd06637  160 QLDRTVGRRNTFIGTPYW---MAPEVI-----ACDENpDATYDFKSDLWSLGITAIEMAEGAPPLcDMHPMRAL-FLIPR 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 665 GEGVRrvLASVSLGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06637  231 NPAPR--LKSKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
448-707 1.81e-14

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: 73.80  E-value: 1.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQdhlKLFKKEVMNYRQTRHENVVLFMGACMNPPhLAIITSFCKGRTLHS 525
Cdd:cd14203    3 LGQGCFGEVWMGTWNGttKVAIKTLKPGTMSP---EAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 526 FVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGIsgVVREERRENQ-LKLSH 602
Cdd:cd14203   79 FLKDGEgKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCkIADFGLARL--IEDNEYTARQgAKFPI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 603 DWLcylAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELQARDW-PFKHQPAEALIWQIGSGegvRRVLASVSLGKEV 681
Cdd:cd14203  157 KWT---APEAA---LYGR------FTIKSDVWSFGILLTELVTKGRvPYPGMNNREVLEQVERG---YRMPCPPGCPESL 221
                        250       260
                 ....*....|....*....|....*.
gi 755537521 682 GEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14203  222 HELMCQCWRKDPEERPTFEYLQSFLE 247
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
438-658 1.92e-14

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: 74.31  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGR--WHGEVA-IRLLEMDghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKARnvNTGELAaIKVIKLE--PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWIC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSF--VRDPKTSLDInktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFG-ISGVVr 590
Cdd:cd06645   87 MEFCGGGSLQDIyhVTGPLSESQI---AYVSRETLQGLYYLHSKGKMHRDIKGANILLtDNGHVKLADFGVSAqITATI- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 591 eERRENQLKLSHdwlcYLAPEIVREmipgrdEDQLPFSKAADVYAFGTVWYELQARDWP-FKHQPAEAL 658
Cdd:cd06645  163 -AKRKSFIGTPY----WMAPEVAAV------ERKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRAL 220
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
448-637 1.93e-14

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: 74.13  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR---WHGEVAI------RLL------EMDGHNQDHLKLFKKEVMNYRQTRHENVV-LFmgACMNPP-- 509
Cdd:cd14008    1 LGRGSFGKVKLALdteTGQLYAIkifnksRLRkrregkNDRGKIKNALDDVRREIAIMKKLDHPNIVrLY--EVIDDPes 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 -HLAIITSFCKGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfglFGIS 586
Cdd:cd14008   79 dKLYLVLEYCEGGPVMELDSGDRVPpLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTaDGTVKISD---FGVS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755537521 587 GVVreERRENQLKLSHDWLCYLAPEIVremipgrDEDQLPFS-KAADVYAFG 637
Cdd:cd14008  156 EMF--EDGNDTLQKTAGTPAFLAPELC-------DGDSKTYSgKAADIWALG 198
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
448-666 2.25e-14

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: 74.17  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH--GEV-AIRLL---EMDGHNQDHLKLFKKEVMNyrQTRHENVVLFMGACMNPPHLAIITSFCKG- 520
Cdd:cd05579    1 ISRGAYGRVYLAKKKstGDLyAIKVIkkrDMIRKNQVDSVLAERNILS--QAQNPFVVKLYYSFQGKKNLYLVMEYLPGg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 ---RTLHSFvrdpkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL--FGISGVVREERR 594
Cdd:cd05579   79 dlySLLENV-----GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDaNGHLKLTDFGLskVGLVRRQIKLSI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 595 ENQLKLSHDWLC--------YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd05579  154 QKKSNGAPEKEDrrivgtpdYLAPEILLGQ---------GHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGK 224
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
440-706 2.25e-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: 74.02  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHGE------VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACM---NPPH 510
Cdd:cd05043    6 ERVTLSDLLQEGTFGRIFHGILRDEkgkeeeVLVKTVK-DHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIedgEKPM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAI-ITSFckgRTLHSFVRDPKTSLDIN----KTRQI---AQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDfg 581
Cdd:cd05043   85 VLYpYMNW---GNLKLFLQQCRLSEANNpqalSTQQLvhmALQIACGMSYLHRRGVIHKDIAARNCVIDDElQVKITD-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 582 lfgiSGVVREerrenqlKLSHDWLC----------YLAPE-IVREMipgrdedqlpFSKAADVYAFGTVWYELQA-RDWP 649
Cdd:cd05043  160 ----NALSRD-------LFPMDYHClgdnenrpikWMSLEsLVNKE----------YSSASDVWSFGVLLWELMTlGQTP 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 650 FKHQPAEALIWQIGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05043  219 YVEIDPFEMAAYLKDG---YRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
439-650 2.69e-14

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: 74.06  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRVHRGR--WHGE-VAIRLLEMDgHNQD--------HLKLFKKevMNyrqtrHENVVLFMGACMN 507
Cdd:cd07829    1 YEKLEK---LGEGTYGVVYKAKdkKTGEiVALKKIRLD-NEEEgipstalrEISLLKE--LK-----HPNIVKLLDVIHT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 508 PPHLAIITSFCKgRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL---F 583
Cdd:cd07829   70 ENKLYLVFEYCD-QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINrDGVLKLADFGLaraF 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 584 GIsgvvreerreNQLKLSHD----WlcYLAPEIvremIPGRDEdqlpFSKAADVYAFGTVWYELqARDWPF 650
Cdd:cd07829  149 GI----------PLRTYTHEvvtlW--YRAPEI----LLGSKH----YSTAVDIWSVGCIFAEL-ITGKPL 198
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
435-707 3.99e-14

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: 73.14  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRW--HGEVAIRLLEMDGHNqdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPhLA 512
Cdd:cd05073    6 WEIPRESLKLEKKLGAGQFGEVWMATYnkHTKVAVKTMKPGSMS---VEAFLAEANVMKTLQHDKLVKLHAVVTKEP-IY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVR-DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVR 590
Cdd:cd05073   82 IITEFMAKGSLLDFLKsDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCkIADFGLARVIEDNE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQlKLSHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARD-WPFKHQPAEALIWQIGSGEGVR 669
Cdd:cd05073  162 YTAREGA-KFPIKW---TAPEAI---------NFGSFTIKSDVWSFGILLMEIVTYGrIPYPGMSNPEVIRALERGYRMP 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 670 RvlaSVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd05073  229 R---PENCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
448-711 4.02e-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: 73.52  E-value: 4.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW--HGE-----VAIRLLEMDGHNQDHLKLFKKE-VMNYRQTRHenVVLFMGACMNPPhLAIITSFCK 519
Cdd:cd05109   15 LGSGAFGTVYKGIWipDGEnvkipVAIKVLRENTSPKANKEILDEAyVMAGVGSPY--VCRLLGICLTST-VQLVTQLMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISGVVREERRENQL 598
Cdd:cd05109   92 YGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSpNHVKITDFGLARLLDIDETEYHADGG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDWLCYlapeivrEMIPGRDedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVSL 677
Cdd:cd05109  172 KVPIKWMAL-------ESILHRR-----FTHQSDVWSYGvTVWELMTFGAKPYDGIPAREIPDLLEKGE---RLPQPPIC 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd05109  237 TIDVYMIMVKCWMIDSECRPRFRELVDEFSRMAR 270
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
492-697 4.30e-14

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: 73.31  E-value: 4.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 492 QTRHENVVLFMGACMNPPHLAIITSFCKG---RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLH-AKGIVHKDLKSKN 567
Cdd:cd08528   65 QLRHPNIVRYYKTFLENDRLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNN 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 568 VFY-DNGKVVITDFGLfgisgvVREERRE-NQLKLSHDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQA 645
Cdd:cd08528  145 IMLgEDDKVTITDFGL------AKQKGPEsSKMTSVVGTILYSCPEIVQ---------NEPYGEKADIWALGCILYQMCT 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755537521 646 RDWPFKHQPAEALIWQIgsGEGVRRVLASVSLGKEVGEILSACWAFDLQERP 697
Cdd:cd08528  210 LQPPFYSTNMLTLATKI--VEAEYEPLPEGMYSDDITFVIRSCLTPDPEARP 259
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
448-650 4.32e-14

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: 73.30  E-value: 4.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW--HGEVAIRLLEMDGhNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK----GR 521
Cdd:cd14664    1 IGRGGAGTVYKGVMpnGTLVAVKRLKGEG-TQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPngslGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSfvRDPKT-SLDINKTRQIAQEIIKGMGYLH---AKGIVHKDLKSKNVFYDNG-KVVITDFGLfgiSGVVREERREN 596
Cdd:cd14664   80 LLHS--RPESQpPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEfEAHVADFGL---AKLMDDKDSHV 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 597 QLKLSHDWlCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14664  155 MSSVAGSY-GYIAPEYA---------YTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
434-709 4.83e-14

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 74.25  E-value: 4.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRV--------HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd05102    1 QWEFPRDRLRLGKVLGHGAFGKVveasafgiDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNPPH-LAIITSFCKGRTLHSFVR------------DPKTSLDINKTRQIAQ---------------------------- 544
Cdd:cd05102   81 TKPNGpLMVIVEFCKYGNLSNFLRakregfspyrerSPRTRSQVRSMVEAVRadrrsrqgsdrvasftestsstnqprqe 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 -------------------EIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDW 604
Cdd:cd05102  161 vddlwqspltmedlicysfQVARGMEFLASRKCIHRDLAARNILLSENNVVkICDFGLARDIYKDPDYVRKGSARLPLKW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 605 LcylAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYE---LQARDWPfKHQPAEALIWQIGSGEgvrRVLASVSLGKEV 681
Cdd:cd05102  241 M---APESIFDKV---------YTTQSDVWSFGVLLWEifsLGASPYP-GVQINEEFCQRLKDGT---RMRAPEYATPEI 304
                        330       340
                 ....*....|....*....|....*...
gi 755537521 682 GEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05102  305 YRIMLSCWHGDPKERPTFSDLVEILGDL 332
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
476-666 4.98e-14

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: 73.10  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 476 NQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIaQEIIKGMGYLHA 555
Cdd:cd14166   40 PLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDASRVI-NQVLSAVKYLHE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 556 KGIVHKDLKSKNVFY----DNGKVVITDFGLFGIS--GVVREErrenqlklshdwlC----YLAPEIVRemipgrdedQL 625
Cdd:cd14166  119 NGIVHRDLKPENLLYltpdENSKIMITDFGLSKMEqnGIMSTA-------------CgtpgYVAPEVLA---------QK 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755537521 626 PFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14166  177 PYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGY 217
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
486-666 5.34e-14

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: 72.79  E-value: 5.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 486 EVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLhsFVRD-PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLK 564
Cdd:cd14083   51 EIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGEL--FDRIvEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 565 SKNVFY----DNGKVVITDFGLFGISGvvreerrENQLKLSHDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVW 640
Cdd:cd14083  129 PENLLYyspdEDSKIMISDFGLSKMED-------SGVMSTACGTPGYVAPEVLA---------QKPYGKAVDCWSIGVIS 192
                        170       180
                 ....*....|....*....|....*.
gi 755537521 641 YELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14083  193 YILLCGYPPFYDENDSKLFAQILKAE 218
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
448-658 5.62e-14

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: 72.73  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR------WhgEVAIRLLEMDGHNQDHLkLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd14201   14 VGHGAFAVVFKGRhrkktdW--EVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF--YDNGK--------VVITDFGLfgisgvvre 591
Cdd:cd14201   91 DLADYLQ-AKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKkssvsgirIKIADFGF--------- 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 592 eRRENQLKLSHDWLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd14201  161 -ARYLQSNMMAATLCgspmYMAPEVIMSQ---------HYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL 221
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
442-662 6.10e-14

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: 73.00  E-value: 6.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRGRWHGevAIRLLEMDGHNQDHLK----LFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERG--SQRLVALKCIPKKALRgkeaMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLFGISGvvreer 593
Cdd:cd14169   83 VTGGELFDRIIERGSYTEKDASQLIGQ-VLQAVKYLHQLGIVHRDLKPENLLYatpfEDSKIMISDFGLSKIEA------ 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 594 rENQLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd14169  156 -QGMLSTACGTPGYVAPELL---------EQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQI 214
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
445-643 8.30e-14

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: 72.53  E-value: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHGE-VAI-RLLEMDGHN-QDHLKLFKKEVMNYRQTRHENVVLFMG-ACMNPPHLAIITSFCKG 520
Cdd:cd14158   20 GNKLGEGGFGVVFKGYINDKnVAVkKLAAMVDIStEDLTKQFEQEIQVMAKCQHENLVELLGySCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFV-RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISG----VVREERR 594
Cdd:cd14158  100 SLLDRLAcLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPkISDFGLARASEkfsqTIMTERI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 595 ENQlklshdwLCYLAPEIVREMIpgrdedqlpfSKAADVYAFGTVWYEL 643
Cdd:cd14158  180 VGT-------TAYMAPEALRGEI----------TPKSDIFSFGVVLLEI 211
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
443-613 9.67e-14

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: 72.35  E-value: 9.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwH---GEVA-IRLLEMDGHNQDHLKLFKKEVMNYrqTRHENVVLFMGACM--NPP----HLA 512
Cdd:cd06636   19 ELVEVVGNGTYGQVYKGR-HvktGQLAaIKVMDVTEDEEEEIKLEINMLKKY--SHHRNIATYYGAFIkkSPPghddQLW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVR 590
Cdd:cd06636   96 LVMEFCGAGSVTDLVKNTKgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVDFGV--SAQLDR 173
                        170       180
                 ....*....|....*....|...
gi 755537521 591 EERRENQLKLSHDWlcyLAPEIV 613
Cdd:cd06636  174 TVGRRNTFIGTPYW---MAPEVI 193
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
448-703 1.04e-13

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: 72.75  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-------VAIRLL-EMDGHNQDHLKLFKKEVMnyRQTRHENVVLFMGACMNPPhLAIITSFCK 519
Cdd:cd05108   15 LGSGAFGTVYKGLWIPEgekvkipVAIKELrEATSPKANKEILDEAYVM--ASVDNPHVCRLLGICLTST-VQLITQLMP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK-VVITDFGLFGISGVVREERRENQL 598
Cdd:cd05108   92 FGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQhVKITDFGLAKLLGAEEKEYHAEGG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVSL 677
Cdd:cd05108  172 KVPIKW---MALESILHRI---------YTHQSDVWSYGvTVWELMTFGSKPYDGIPASEISSILEKGE---RLPQPPIC 236
                        250       260
                 ....*....|....*....|....*.
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd05108  237 TIDVYMIMVKCWMIDADSRPKFRELI 262
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
440-646 1.07e-13

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 72.77  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHGE-VAIRLLemdgHNQDHLKLFKK-EVMNYRQTRHENVVLFMGACMNP----PHLAI 513
Cdd:cd14219    5 KQIQMVKQIGKGRYGEVWMGKWRGEkVAVKVF----FTTEEASWFREtEIYQTVLMRHENILGFIAADIKGtgswTQLYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFYD-NGKVVITDFGLfg 584
Cdd:cd14219   81 ITDYHENGSLYDYLK--STTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKkNGTCCIADLGL-- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 585 isgVVREERRENQLKLSHDWLC----YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQAR 646
Cdd:cd14219  157 ---AVKFISDTNEVDIPPNTRVgtkrYMPPEVLDESL---NRNHFQSYIMADMYSFGLILWEVARR 216
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
475-652 1.11e-13

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: 71.95  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 475 HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP-PHLAIITSFCKGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYL 553
Cdd:cd13994   36 KRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLhGKWCLVMEYCPGGDLFTLIEKAD-SLSLEEKDCFFKQILRGVAYL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 554 HAKGIVHKDLKSKNV-FYDNGKVVITDFGlfgisgvVREERRENQLKLSHDW--LC----YLAPEIVremipgrdeDQLP 626
Cdd:cd13994  115 HSHGIAHRDLKPENIlLDEDGVLKLTDFG-------TAEVFGMPAEKESPMSagLCgsepYMAPEVF---------TSGS 178
                        170       180
                 ....*....|....*....|....*..
gi 755537521 627 FS-KAADVYAFGTVWYELQARDWPFKH 652
Cdd:cd13994  179 YDgRAVDVWSCGIVLFALFTGRFPWRS 205
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
436-699 1.20e-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: 72.33  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHGE-------------------VAIRLLEMDGhNQDHLKLFKKEVMNYRQTRHE 496
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMekfmdkdfalevsenqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 497 NVVLFMGACMNPPHLAIITSFCKGRTLHSFV---------RDPKTSLDINKT--RQIAQEIIKGMGYLHAKGIVHKDLKS 565
Cdd:cd05095   80 NIIRLLAVCITDDPLCMITEYMENGDLNQFLsrqqpegqlALPSNALTVSYSdlRFMAAQIASGMKYLSSLNFVHRDLAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 566 KNVFY-DNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYlapeivREMIPGRdedqlpFSKAADVYAFG-TVWYEL 643
Cdd:cd05095  160 RNCLVgKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSW------ESILLGK------FTTASDVWAFGvTLWETL 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 644 Q-ARDWPFKHQPAEALIWQIGS---GEGVRRVLASVSLGKE-VGEILSACWAFDLQERPSF 699
Cdd:cd05095  228 TfCREQPYSQLSDEQVIENTGEffrDQGRQTYLPQPALCPDsVYKLMLSCWRRDTKDRPSF 288
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
448-703 1.30e-13

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: 71.30  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH---RGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd08220    8 VGRGAYGTVYlcrRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTSL-DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITdFGLFGISGVVREERRENQLKLSHd 603
Cdd:cd08220   88 EYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVK-IGDFGISKILSSKSKAYTVVGTP- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 604 wlCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGegvRRVLASVSLGKEVGE 683
Cdd:cd08220  166 --CYISPELC---------EGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRG---TFAPISDRYSEELRH 231
                        250       260
                 ....*....|....*....|
gi 755537521 684 ILSACWAFDLQERPSFSLLM 703
Cdd:cd08220  232 LILSMLHLDPNKRPTLSEIM 251
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
448-665 1.49e-13

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: 71.16  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGR------VHRGRWHGEVAIRLLEMDGHNQDHlklfKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd08219    8 VGEGSFGRallvqhVNSDQKYAMKEIRLPKSSSAVEDS----RKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKT-RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGIsgvvreerrenqlk 599
Cdd:cd08219   84 DLMQKIKLQRGKLFPEDTiLQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLtQNGKVKLGDFGSARL-------------- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 600 LSH--DWLC-------YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSG 665
Cdd:cd08219  150 LTSpgAYACtyvgtpyYVPPEIWENM---------PYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQG 215
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
448-650 1.58e-13

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: 71.60  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG---EVAirLLEMDGHNQDHLKLFKKEVMNYRQ-TRHENVVLFMGACM----NPPHLAIITSFCK 519
Cdd:cd13985    8 LGEGGFSYVYLAHDVNtgrRYA--LKRMYFNDEEQLRVAIKEIEIMKRlCGHPNIVQYYDSAIlsseGRKEVLLLMEYCP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYDN-GKVVITDFGlfgisGVVRE----E 592
Cdd:cd13985   86 GSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNtGRFKLCDFG-----SATTEhyplE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 593 RRENQLKLSHDW-----LCYLAPEIVREMipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd13985  161 RAEEVNIIEEEIqknttPMYRAPEMIDLY------SKKPIGEKADIWALGCLLYKLCFFKLPF 217
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
448-709 1.60e-13

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: 71.44  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH--GE----VAIRLLEMdGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd05066   12 IGAGEFGEVCSGRLKlpGKreipVAIKTLKA-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERRENQL-- 598
Cdd:cd05066   91 SLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCkVSDFGL---SRVLEDDPEAAYTtr 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 --KLSHDWLcylAPEivreMIPGRDedqlpFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGegvRRVLASV 675
Cdd:cd05066  168 ggKIPIRWT---APE----AIAYRK-----FTSASDVWSYGIVMWEVMSYgERPYWEMSNQDVIKAIEEG---YRLPAPM 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05066  233 DCPAALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
483-614 2.06e-13

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: 71.05  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 483 FKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKD 562
Cdd:cd14099   48 LKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSLMELLKRRKA-LTEPEVRYFMRQILSGVKYLHSNRIIHRD 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 563 LKSKNVFYD-NGKVVITDFGLfgiSGVV--REERRENqlklshdwLC----YLAPEIVR 614
Cdd:cd14099  127 LKLGNLFLDeNMNVKIGDFGL---AARLeyDGERKKT--------LCgtpnYIAPEVLE 174
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
446-699 2.49e-13

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: 70.87  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG---RWHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06641   10 EKIGKGSFGEVFKGidnRTQKVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGisGVVREERRENQLKLS 601
Cdd:cd06641   89 ALDLLE--PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLsEHGEVKLADFGVAG--QLTDTQIKRN*FVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEV 681
Cdd:cd06641  165 PFW---MAPEVIK---------QSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNN---PPTLEGNYSKPL 229
                        250
                 ....*....|....*...
gi 755537521 682 GEILSACwafdLQERPSF 699
Cdd:cd06641  230 KEFVEAC----LNKEPSF 243
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
510-666 2.80e-13

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: 70.24  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgv 588
Cdd:cd05123   67 KLYLVLDYVPGGELFSHLS-KEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDsDGHIKLTDFGL------ 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKLShdwLC----YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGS 664
Cdd:cd05123  140 AKELSSDGDRTYT---FCgtpeYLAPEVLL---------GKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILK 207

                 ..
gi 755537521 665 GE 666
Cdd:cd05123  208 SP 209
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
448-715 2.81e-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: 71.25  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW--HGE-----VAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMNPPhLAIITSFCKG 520
Cdd:cd05110   15 LGSGAFGTVYKGIWvpEGEtvkipVAIKILNETTGPKANVE-FMDEALIMASMDHPHLVRLLGVCLSPT-IQLVTQLMPH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISGVVREERRENQLK 599
Cdd:cd05110   93 GCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSpNHVKITDFGLARLLEGDEKEYNADGGK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDWLCYlapeivrEMIPGRDedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEgvrRVLASVSLG 678
Cdd:cd05110  173 MPIKWMAL-------ECIHYRK-----FTHQSDVWSYGvTIWELMTFGGKPYDGIPTREIPDLLEKGE---RLPQPPICT 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 755537521 679 KEVGEILSACWAFDLQERPSFSLLMDMLERLPKLNRR 715
Cdd:cd05110  238 IDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQR 274
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
446-703 3.02e-13

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: 71.29  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06654   26 EKIGQGASGTVYTAMdvaTGQEVAIR--QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDpkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKLS 601
Cdd:cd06654  104 LTDVVTE--TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGF--CAQITPEQSKRSTMVGT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVSLGKEV 681
Cdd:cd06654  180 PYW---MAPEVV---------TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSAIF 246
                        250       260
                 ....*....|....*....|..
gi 755537521 682 GEILSACWAFDLQERPSFSLLM 703
Cdd:cd06654  247 RDFLNRCLEMDVEKRGSAKELL 268
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
436-709 3.16e-13

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: 70.67  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVElgEPIGQGRWGRVHRGRW------HGEVAIRLLEMdGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPP 509
Cdd:cd05065    2 DVSCVKIE--EVIGAGEFGEVCRGRLklpgkrEIFVAIKTLKS-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGV 588
Cdd:cd05065   79 PVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCkVSDFGL---SRF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQL------KLSHDWLcylAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQArdwpFKHQPAEALIWQ- 661
Cdd:cd05065  156 LEDDTSDPTYtsslggKIPIRWT---APEAIAYR---------KFTSASDVWSYGIVMWEVMS----YGERPYWDMSNQd 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 662 -IGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05065  220 vINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
448-651 3.52e-13

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: 70.98  E-value: 3.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH---GEVAIRLLEMDGHnQDHLKLFKKEVMNYRQTRHENVV-LF-MGACMNPPHLAIITSFCKGRT 522
Cdd:cd13988    1 LGQGATANVFRGRHKktgDLYAVKVFNNLSF-MRPLDVQMREFEVLKKLNHKNIVkLFaIEEELTTRHKVLVMELCPCGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIA--QEIIKGMGYLHAKGIVHKDLKSKN---VFYDNGKVV--ITDFglfgisGVVREERRE 595
Cdd:cd13988   80 LYTVLEEPSNAYGLPESEFLIvlRDVVAGMNHLRENGIVHRDIKPGNimrVIGEDGQSVykLTDF------GAARELEDD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 596 NQLKLSHDWLCYLAPEIVREMIPgRDEDQLPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd13988  154 EQFVSLYGTEEYLHPDMYERAVL-RKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
446-703 3.82e-13

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: 70.34  E-value: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG---RWHGEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06647   13 EKIGQGASGTVYTAidvATGQEVAIK--QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDpkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKLS 601
Cdd:cd06647   91 LTDVVTE--TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGF--CAQITPEQSKRSTMVGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVSLGKEV 681
Cdd:cd06647  167 PYW---MAPEVV---------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSAIF 233
                        250       260
                 ....*....|....*....|..
gi 755537521 682 GEILSACWAFDLQERPSFSLLM 703
Cdd:cd06647  234 RDFLNRCLEMDVEKRGSAKELL 255
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
446-650 4.03e-13

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: 69.95  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG--RWHG-EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPP--HLAIITSFCKG 520
Cdd:cd13983    7 EVLGRGSFKTVYRAfdTEEGiEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSkkEVIFITELMTS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLfgisgvvreerrEN 596
Cdd:cd13983   87 GTLKQYLKRFK-RLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgnTGEVKIGDLGL------------AT 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 597 QLKLSHDWLC-----YLAPEIVREmipGRDEdqlpfskAADVYAFGTVWYELQARDWPF 650
Cdd:cd13983  154 LLRQSFAKSVigtpeFMAPEMYEE---HYDE-------KVDIYAFGMCLLEMATGEYPY 202
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
484-666 4.10e-13

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: 70.06  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDL 563
Cdd:cd14167   49 ENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQ-ILDAVKYLHDMGIVHRDL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 564 KSKNVFY----DNGKVVITDFGLFGISGvvreerRENQLKLSHDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTV 639
Cdd:cd14167  128 KPENLLYysldEDSKIMISDFGLSKIEG------SGSVMSTACGTPGYVAPEVLA---------QKPYSKAVDCWSIGVI 192
                        170       180
                 ....*....|....*....|....*..
gi 755537521 640 WYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14167  193 AYILLCGYPPFYDENDAKLFEQILKAE 219
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
440-650 4.62e-13

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: 70.30  E-value: 4.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVH--RGRWHGE-VAIRLLEmdghnqdhlklfKKEVMNYRQTRH---ENVVL------FM----G 503
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRlvKHKDSGKyYALKILK------------KAKIIKLKQVEHvlnEKRILsevrhpFIvnllG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 ACMNPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 582
Cdd:cd05580   69 SFQDDRNLYMVMEYVPGGELFSLLRR-SGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDsDGHIKITDFGF 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 583 fgiSGVVREerrenqlklsHDW-LC----YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05580  148 ---AKRVKD----------RTYtLCgtpeYLAPEIIL---------SKGHGKAVDWWALGILIYEMLAGYPPF 198
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
479-702 5.42e-13

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: 69.70  E-value: 5.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 479 HLKLFKKEVMNYRQTRHENVVLFMGACMNPP------HLAIITSFCKGRTLHSFVrDPKTSLDINKTRQIAQEIIKGMGY 552
Cdd:cd14012   41 QIQLLEKELESLKKLRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSELL-DSVGSVPLDTARRWTLQLLEALEY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 553 LHAKGIVHKDLKSKNVFYDN----GKVVITDFGLfgisgvVREERREN--QLKLSHDWLCYLAPEIVREmipgrdedQLP 626
Cdd:cd14012  120 LHRNGVVHKSLHAGNVLLDRdagtGIVKLTDYSL------GKTLLDMCsrGSLDEFKQTYWLPPELAQG--------SKS 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 627 FSKAADVYAFGTVWYE-LQARDWPFKHQPAEAliwqigsgegvrrVLASVSLGKEVGEILSACWAFDLQERPS-FSLL 702
Cdd:cd14012  186 PTRKTDVWDLGLLFLQmLFGLDVLEKYTSPNP-------------VLVSLDLSASLQDFLSKCLSLDPKKRPTaLELL 250
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
443-666 7.03e-13

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: 69.34  E-value: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHN--QDHLKLfKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14073    4 ELLETLGKGTYGKVKLAIERAtgrEVAIKSIKKDKIEdeQDMVRI-RREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVrDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVREErren 596
Cdd:cd14073   83 ASGGELYDYI-SERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDqNGNAKIADFGL---SNLYSKD---- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 597 qlKLSHDWlC----YLAPEIVremipgrdeDQLPF-SKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14073  155 --KLLQTF-CgsplYASPEIV---------NGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGD 217
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
435-703 7.22e-13

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: 69.77  E-value: 7.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIpfeqveLGEpIGQGRWGRVHRGRwHGE----VAIRLLEMDGHNQdhLKLFKKEVMNYRQTRHENVVLFMGACMNPPH 510
Cdd:cd06611    7 WEI------IGE-LGDGAFGKVYKAQ-HKEtglfAAAKIIQIESEEE--LEDFMVEIDILSECKHPNIVGLYEAYFYENK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITDfglFGISGVV 589
Cdd:cd06611   77 LWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNIlLTLDGDVKLAD---FGVSAKN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REE--RRENQLKLSHdwlcYLAPEIVremIPGRDEDQlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEG 667
Cdd:cd06611  154 KSTlqKRDTFIGTPY----WMAPEVV---ACETFKDN-PYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEP 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755537521 668 vRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06611  226 -PTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELL 260
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
443-665 8.43e-13

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: 69.40  E-value: 8.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVH--RGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQT-------------RHENVVLFMGACM 506
Cdd:cd14077    4 EFVKTIGAGSMGKVKlaKHIRTGEkCAIKIIPRASNAGLKKEREKRLEKEISRDirtireaalssllNHPHICRLRDFLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 NPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGI 585
Cdd:cd14077   84 TPNHYYMLFEYVDGGQLLDYIIS-HGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISkSGNIKIIDFGLSNL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 586 SgvvreeRRENQLKLSHDWLCYLAPEIVremipgrdeDQLPFS-KAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGS 664
Cdd:cd14077  163 Y------DPRRLLRTFCGSLYFAAPELL---------QAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKK 227

                 .
gi 755537521 665 G 665
Cdd:cd14077  228 G 228
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
449-707 9.18e-13

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 69.68  E-value: 9.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 449 GQGRWGRVHRGRWHGE-VAIRLLEMdghnQDHLKLFKK-EVMNYRQTRHENVVLFMGACMNPPHLAI----ITSFCKGRT 522
Cdd:cd14141    4 ARGRFGCVWKAQLLNEyVAVKIFPI----QDKLSWQNEyEIYSLPGMKHENILQFIGAEKRGTNLDVdlwlITAFHEKGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLdiNKTRQIAQEIIKGMGYLHAK----------GIVHKDLKSKNVFYDNG-KVVITDFGLF-----GIS 586
Cdd:cd14141   80 LTDYLKANVVSW--NELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNlTACIADFGLAlkfeaGKS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 -----GVVREERrenqlklshdwlcYLAPEIVremipgrdEDQLPFSKAA----DVYAFGTVWYELQAR----DWPFKHQ 653
Cdd:cd14141  158 agdthGQVGTRR-------------YMAPEVL--------EGAINFQRDAflriDMYAMGLVLWELASRctasDGPVDEY 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 654 --PAEALIWQIGSGEGVRRVLASvslgKEVGEILSACWafdlQERPSFSLLMDMLE 707
Cdd:cd14141  217 mlPFEEEVGQHPSLEDMQEVVVH----KKKRPVLRECW----QKHAGMAMLCETIE 264
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
446-646 9.74e-13

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: 69.28  E-value: 9.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE-VAIRLLEMDGHN--QDHLKLFKKEVMNyrqtrHENVVLFMGA----CMNPPHLAIITSFC 518
Cdd:cd14053    1 EIKARGRFGAVWKAQYLNRlVAVKIFPLQEKQswLTEREIYSLPGMK-----HENILQFIGAekhgESLEAEYWLITEFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHA----------KGIVHKDLKSKNVFY-DNGKVVITDFGL---FG 584
Cdd:cd14053   76 ERGSLCDYLK--GNVISWNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLkSDLTACIADFGLalkFE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 585 ISGVVREE------RRenqlklshdwlcYLAPEIVremipgrdEDQLPFSKAA----DVYAFGTVWYELQAR 646
Cdd:cd14053  154 PGKSCGDThgqvgtRR------------YMAPEVL--------EGAINFTRDAflriDMYAMGLVLWELLSR 205
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
484-662 1.02e-12

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: 69.69  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDL 563
Cdd:cd14168   56 ENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQ-VLDAVYYLHRMGIVHRDL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 564 KSKNVFY----DNGKVVITDFGLFGISGvvreerRENQLKLSHDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTV 639
Cdd:cd14168  135 KPENLLYfsqdEESKIMISDFGLSKMEG------KGDVMSTACGTPGYVAPEVLA---------QKPYSKAVDCWSIGVI 199
                        170       180
                 ....*....|....*....|...
gi 755537521 640 WYELQARDWPFKHQPAEALIWQI 662
Cdd:cd14168  200 AYILLCGYPPFYDENDSKLFEQI 222
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
448-706 1.06e-12

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: 68.73  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW--HGEVAIRLLEMDGHNQDHlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHS 525
Cdd:cd05114   12 LGSGLFGVVRLGKWraQYKVAIKAIREGAMSEED---FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 526 FVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREERRENQ-LKLSHD 603
Cdd:cd05114   89 YLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVnDTGVVKVSDFGM--TRYVLDDQYTSSSgAKFPVK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 604 WlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQAR-DWPFKHQPAEALIWQIGSGEGVRRV-LASvslgKEV 681
Cdd:cd05114  167 W---SPPEVF---------NYSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSRGHRLYRPkLAS----KSV 230
                        250       260
                 ....*....|....*....|....*
gi 755537521 682 GEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05114  231 YEVMYSCWHEKPEGRPTFADLLRTI 255
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
448-650 1.06e-12

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: 68.71  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV----HRGRwHGEVAIRLLEMDghnQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14087    9 IGRGSFSRVvrveHRVT-RQPYAIKMIETK---CRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgisGVVREERRENQLK 599
Cdd:cd14087   85 FDRII-AKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIMITDFGL----ASTRKKGPNCLMK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755537521 600 LSHDWLCYLAPEI-VREmipgrdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14087  160 TTCGTPEYIAPEIlLRK----------PYTQSVDMWAVGVIAYILLSGTMPF 201
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
443-637 1.15e-12

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: 68.92  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNY------RQTRHENVVLFMGACMNPPHLAI 513
Cdd:cd13993    3 QLISPIGEGAYGVVylaVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQLReidlhrRVSRHPNIITLHDVFETEVAIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRD----PKTSLDInktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF--YDNGKVVITDFGLfgisg 587
Cdd:cd13993   83 VLEYCPNGDLFEAITEnriyVGKTELI---KNVFLQLIDAVKHCHSLGIYHRDIKPENILlsQDEGTVKLCDFGL----- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 588 vvreerrENQLKLSHDWLC----YLAPEIVREMIPGRDedqlPFS-KAADVYAFG 637
Cdd:cd13993  155 -------ATTEKISMDFGVgsefYMAPECFDEVGRSLK----GYPcAAGDIWSLG 198
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
495-704 1.16e-12

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: 68.56  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRD--PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN 572
Cdd:cd13997   59 HPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEElsPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 573 -GKVVITDFGL---FGISGVVREERREnqlklshdwlcYLAPEIVremipgrdEDQLPFSKAADVYAFGTVWYELqARDW 648
Cdd:cd13997  139 kGTCKIGDFGLatrLETSGDVEEGDSR-----------YLAPELL--------NENYTHLPKADIFSLGVTVYEA-ATGE 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 649 PFkhqPAEALIW-QIGSGEGVRRVLASVSLgkEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd13997  199 PL---PRNGQQWqQLRQGKLPLPPGLVLSQ--ELTRLLKVMLDPDPTRRPTADQLLA 250
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
446-703 1.26e-12

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: 69.37  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG---RWHGEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06656   25 EKIGQGASGTVYTAidiATGQEVAIK--QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDpkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKLS 601
Cdd:cd06656  103 LTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGF--CAQITPEQSKRSTMVGT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVSLGKEV 681
Cdd:cd06656  179 PYW---MAPEVV---------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSAVF 245
                        250       260
                 ....*....|....*....|..
gi 755537521 682 GEILSACWAFDLQERPSFSLLM 703
Cdd:cd06656  246 RDFLNRCLEMDVDRRGSAKELL 267
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
447-643 1.42e-12

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: 68.42  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 447 PIGQGRWGRVHRGRWH--GE-VAIRLLEMDGH----NQDHLKLFKKevMNyRQTRHENVV----LFMGACMNppHLAIIT 515
Cdd:cd05118    6 KIGEGAFGTVWLARDKvtGEkVAIKKIKNDFRhpkaALREIKLLKH--LN-DVEGHPNIVklldVFEHRGGN--HLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCkGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF--YDNGKVVITDFGLfgisgVVREER 593
Cdd:cd05118   81 ELM-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILinLELGQLKLADFGL-----ARSFTS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 RENQLKLSHDWlcYLAPEIVREMIpgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd05118  155 PPYTPYVATRW--YRAPEVLLGAK--------PYGSSIDIWSLGCILAEL 194
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
440-643 1.49e-12

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: 68.81  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRtnqVVAIKVIDLE-EAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKtsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDfglFGISGvvreERRE 595
Cdd:cd06609   80 YCGGGSVLDLLKPGP--LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLsEEGDVKLAD---FGVSG----QLTS 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 596 NQLKLSHD-----WlcyLAPEIVREmiPGRDEdqlpfskAADVYAFGTVWYEL 643
Cdd:cd06609  151 TMSKRNTFvgtpfW---MAPEVIKQ--SGYDE-------KADIWSLGITAIEL 191
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
531-666 1.52e-12

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: 68.84  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 531 KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGlFGISGVVREERREnqlklshdwLC--- 606
Cdd:cd14181  110 KVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLdDQLHIKLSDFG-FSCHLEPGEKLRE---------LCgtp 179
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 607 -YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14181  180 gYLAPEILKCSM---DETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGR 237
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
434-712 1.78e-12

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 69.26  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 434 EWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd14207    1 KWEFARERLKLGKSLGRGAFGKVVQASAFGikksptcrVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 M-NPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIK------------------------------------ 548
Cdd:cd14207   81 TkSGGPLMVIVEYCKYGNLSNYLKSKRDFFVTNKDTSLQEELIKekkeaeptggkkkrlesvtssesfassgfqedksls 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 549 -------------------------------GMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREERREN 596
Cdd:cd14207  161 dveeeeedsgdfykrpltmedlisysfqvarGMEFLSSRKCIHRDLAARNILLSENNVVkICDFGLARDIYKNPDYVRKG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYE---LQARDWPfKHQPAEALIWQIGSGegvRRVLA 673
Cdd:cd14207  241 DARLPLKW---MAPESIFDKI---------YSTKSDVWSYGVLLWEifsLGASPYP-GVQIDEDFCSKLKEG---IRMRA 304
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755537521 674 SVSLGKEVGEILSACWAFDLQERPSFSllmDMLERLPKL 712
Cdd:cd14207  305 PEFATSEIYQIMLDCWQGDPNERPRFS---ELVERLGDL 340
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
442-709 1.87e-12

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


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 68.41  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRG------RWHGEVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd05064    7 IKIERILGTGRFGELCRGclklpsKRELPVAIHTLR-AGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVfydngkVVITDFGLfGISGVVREERRE 595
Cdd:cd05064   86 EYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKV------LVNSDLVC-KISGFRRLQEDK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLS----HDWLCYLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYELQARD----WPFKHQPAealiwqIGSGEG 667
Cdd:cd05064  159 SEAIYTtmsgKSPVLWAAPEAIQY---HH------FSSASDVWSFGIVMWEVMSYGerpyWDMSGQDV------IKAVED 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755537521 668 VRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05064  224 GFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKM 265
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
435-699 1.98e-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: 68.52  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACM 506
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKGvvkdepetRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 NPPHLAIITSFCKGrTLHSFVRDPKTSLDIN---------KTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVV 576
Cdd:cd05062   81 GQPTLVIMELMTRG-DLKSYLRSLRPEMENNpvqappslkKMIQMAGEIADGMAYLNANKFVHRDLAARNcMVAEDFTVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 577 ITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQArdwpFKHQPAE 656
Cdd:cd05062  160 IGDFGMTRDIYETDYYRKGGKGLLPVRW---MSPESLKDGV---------FTTYSDVWSFGVVLWEIAT----LAEQPYQ 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 657 ALiwqigSGEGVRRVLASVSLGKE-------VGEILSACWAFDLQERPSF 699
Cdd:cd05062  224 GM-----SNEQVLRFVMEGGLLDKpdncpdmLFELMRMCWQYNPKMRPSF 268
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
436-708 1.99e-12

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 68.32  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHlKLFKKEVMNYRQTRHENVVLFMGAC-- 505
Cdd:cd05050    1 EYPRNNIEYVRDIGQGAFGRVFQARAPGllpyepftMVAVKMLKEEASADMQ-ADFQREAALMAEFDHPNIVKLLGVCav 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 ----------MNPPHLAIITSFCKGRTLHSFVRD-------PKTSLDINKTRQ--IAQEIIKGMGYLHAKGIVHKDLKSK 566
Cdd:cd05050   80 gkpmcllfeyMAYGDLNEFLRHRSPRAQCSLSHStssarkcGLNPLPLSCTEQlcIAKQVAAGMAYLSERKFVHRDLATR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 567 NVFY-DNGKVVITDFGLfgisgvvreerreNQLKLSHDWlcYLAPEivREMIPGRdedQLP--------FSKAADVYAFG 637
Cdd:cd05050  160 NCLVgENMVVKIADFGL-------------SRNIYSADY--YKASE--NDAIPIR---WMPpesifynrYTTESDVWAYG 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 638 TVWYELqardWPFKHQP-----AEALIWQIGSGEgvrrVLASV-SLGKEVGEILSACWAFDLQERPSFSLLMDMLER 708
Cdd:cd05050  220 VVLWEI----FSYGMQPyygmaHEEVIYYVRDGN----VLSCPdNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
431-709 2.05e-12

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 69.65  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKK-EVMNYRQTrHENVVLF 501
Cdd:cd05107   28 YDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGlshsqstmKVAVKMLKSTARSSEKQALMSElKIMSHLGP-HLNIVNL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 502 MGACMNPPHLAIITSFCK--------GRTLHSFV-------RDPKTSL-------------------------DINKTRQ 541
Cdd:cd05107  107 LGACTKGGPIYIITEYCRygdlvdylHRNKHTFLqyyldknRDDGSLIsggstplsqrkshvslgsesdggymDMSKDES 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 542 I--------------------------------AQE-------------------------IIKGMGYLHAKGIVHKDLK 564
Cdd:cd05107  187 AdyvpmqdmkgtvkyadiessnyespydqylpsAPErtrrdtlinespalsymdlvgfsyqVANGMEFLASKNCVHRDLA 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 565 SKNVFYDNGKVV-ITDFGLfgisgvVREERRE-NQLKLSHDWLC--YLAPEIVREMIpgrdedqlpFSKAADVYAFGTVW 640
Cdd:cd05107  267 ARNVLICEGKLVkICDFGL------ARDIMRDsNYISKGSTFLPlkWMAPESIFNNL---------YTTLSDVWSFGILL 331
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 641 YEL-QARDWPFKHQPAEALIWQ-IGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05107  332 WEIfTLGGTPYPELPMNEQFYNaIKRG---YRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDL 399
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
448-654 2.18e-12

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: 68.53  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV------HRGRwhgEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd06658   30 IGEGSTGIVciatekHTGK---QVAVK--KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVrdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREERRENQLKL 600
Cdd:cd06658  105 ALTDIV--THTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLtSDGRIKLSDFGF--CAQVSKEVPKRKSLVG 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 601 SHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQP 654
Cdd:cd06658  181 TPYW---MAPEVI---------SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEP 222
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
439-650 2.33e-12

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: 68.02  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLFKKEVMNyrQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14193    3 YYNVNKEEILGGGRFGQVHKCEEKSsglKLAAKIIKARSQKEKEEVKNEIEVMN--QLNHANLIQLYDAFESRNDIVLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGKVVITDFGLfgisgvVREE 592
Cdd:cd14193   81 EYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcvsREANQVKIIDFGL------ARRY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 593 RRENQLKLSHDWLCYLAPEIVremipgrDEDQLPFskAADVYAFGTVWYELQARDWPF 650
Cdd:cd14193  155 KPREKLRVNFGTPEFLAPEVV-------NYEFVSF--PTDMWSLGVIAYMLLSGLSPF 203
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
448-643 2.43e-12

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: 68.11  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHR------GRWhgeVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCkGR 521
Cdd:cd07833    9 VGEGAYGVVLKcrnkatGEI---VAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV-ER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQLKL 600
Cdd:cd07833   85 TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSeSGVLKLCDFGF------ARALTARPASPL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 601 ----SHDWlcYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd07833  159 tdyvATRW--YRAPELLV--------GDTNYGKPVDVWAIGCIMAEL 195
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
437-706 2.46e-12

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: 68.26  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 437 IPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP 508
Cdd:cd05049    2 IKRDTIVLKRELGEGAFGKVFLGECYNlepeqdkmLVAVKTLK-DASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 509 PHLAIITSFCKGRTLHSFVR-------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKV 575
Cdd:cd05049   81 DPLLMVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 576 V-ITDFGLFGISGVVREERRENQLKLSHDWlcyLAPEIVremIPGRdedqlpFSKAADVYAFGTVWYELqardWPFKHQP 654
Cdd:cd05049  161 VkIGDFGMSRDIYSTDYYRVGGHTMLPIRW---MPPESI---LYRK------FTTESDVWSFGVVLWEI----FTYGKQP 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 655 -----AEALIWQIGSGEGVRRVLASVSlgkEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05049  225 wfqlsNTEVIECITQGRLLQRPRTCPS---EVYAVMLGCWKREPQQRLNIKDIHKRL 278
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
440-650 2.47e-12

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: 67.58  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGR---WHGEVAIRLLEMDG-HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARslhTGLEVAIKMIDKKAmQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvreerr 594
Cdd:cd14186   81 EMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTrNMNIKIADFGL------------ 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 595 ENQLKLSHD---WLC----YLAPEIVRemipgRDEDQLPfskaADVYAFGTVWYELQARDWPF 650
Cdd:cd14186  149 ATQLKMPHEkhfTMCgtpnYISPEIAT-----RSAHGLE----SDVWSLGCMFYTLLVGRPPF 202
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
448-709 2.82e-12

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


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 67.51  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSF 526
Cdd:cd14057    3 INETHSGELWKGRWQGnDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDpKTSLDINKTRQI--AQEIIKGMGYLHA--KGIVHKDLKSKNVFYDNG---KVVITDfglfgisgvVREERRENQLK 599
Cdd:cd14057   83 LHE-GTGVVVDQSQAVkfALDIARGMAFLHTlePLIPRHHLNSKHVMIDEDmtaRINMAD---------VKFSFQEPGKM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDWlcyLAPEIVREmipgRDEDQlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIgSGEGVrRVLASVSLGK 679
Cdd:cd14057  153 YNPAW---MAPEALQK----KPEDI--NRRSADMWSFAILLWELVTREVPFADLSNMEIGMKI-ALEGL-RVTIPPGISP 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 755537521 680 EVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14057  222 HMCKLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
543-687 2.83e-12

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: 68.40  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgvVREERRENQLKLShdwLC----YLAPEIVREMi 617
Cdd:cd05570  102 AAEICLALQFLHERGIIYRDLKLDNVLLDAeGHIKIADFGM------CKEGIWGGNTTST---FCgtpdYIAPEILREQ- 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 618 pgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrrVLASVSLGKEVGEILSA 687
Cdd:cd05570  172 --------DYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDE----VLYPRWLSREAVSILKG 229
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
495-698 3.08e-12

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: 67.45  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQ---EIIKGMGYLHAKGIVHKDLKSKNVFYD 571
Cdd:cd08222   61 HPAIVKFHDSFVEKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDwfiQLLLAVQYMHERRILHRDLKAKNIFLK 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 572 NGKVVITDfglFGISGVvreerrenqLKLSHDWLC-------YLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQ 644
Cdd:cd08222  141 NNVIKVGD---FGISRI---------LMGTSDLATtftgtpyYMSPEVL---------KHEGYNSKSDIWSLGCILYEMC 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 645 ARDWPFKHQPAEALIWQIGSGEgvrrvLASVS--LGKEVGEILSACWAFDLQERPS 698
Cdd:cd08222  200 CLKHAFDGQNLLSVMYKIVEGE-----TPSLPdkYSKELNAIYSRMLNKDPALRPS 250
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
443-650 3.14e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 68.31  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVhrgrwhgevaiRLLEMDGHNQDH-LKLFKK-EVMNYRQTRHEN-------------VVLFMGACMN 507
Cdd:PTZ00263  21 EMGETLGTGSFGRV-----------RIAKHKGTGEYYaIKCLKKrEILKMKQVQHVAqeksilmelshpfIVNMMCSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 508 PPHLAIITSFCKGRTLHSFVRDP-KTSLDINKTrqIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgi 585
Cdd:PTZ00263  90 ENRVYFLLEFVVGGELFTHLRKAgRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPENLLLDNkGHVKVTDFGF--- 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 586 SGVVREERREnqlklshdwLC----YLAPEIVREmiPGRDedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:PTZ00263 165 AKKVPDRTFT---------LCgtpeYLAPEVIQS--KGHG-------KAVDWWTMGVLLYEFIAGYPPF 215
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
448-643 3.31e-12

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: 67.28  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-VAIRLLemdgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPhlAIITSFCKGRTLHSF 526
Cdd:cd14068    2 LGDGGFGSVYRAVYRGEdVAVKIF----NKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSLDAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV----FYDNGKVV--ITDFGL------FGIsgvvreerr 594
Cdd:cd14068   76 LQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVllftLYPNCAIIakIADYGIaqyccrMGI--------- 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 595 enqlKLSHDWLCYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd14068  147 ----KTSEGTPGFRAPEVAR--------GNVIYNQQADVYSFGLLLYDI 183
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
448-658 3.39e-12

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: 67.34  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG----EVAIRLLemdghNQDHL----KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14202   10 IGHGAFAVVFKGRHKEkhdlEVAVKCI-----NKKNLaksqTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----------DNGKVVITDFGLfgisgvv 589
Cdd:cd14202   85 GGDLADYLHTMRT-LSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrksnpNNIRIKIADFGF------- 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 590 reeRRENQLKLSHDWLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd14202  157 ---ARYLQNNMMAATLCgspmYMAPEVIMSQ---------HYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL 217
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
448-699 3.49e-12

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: 67.25  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRwH----GEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14009    1 IGRGSFATVWKGR-HkqtgEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV----FYDNGKVVITDFGLfgisgvvreERRENQLK 599
Cdd:cd14009   80 SQYIRKRGR-LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLllstSGDDPVLKIADFGF---------ARSLQPAS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LSHDwLC----YLAPEIVRemipGRDEDqlpfSKaADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASV 675
Cdd:cd14009  150 MAET-LCgsplYMAPEILQ----FQKYD----AK-ADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAA 219
                        250       260
                 ....*....|....*....|....
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSF 699
Cdd:cd14009  220 QLSPDCKDLLRRLLRRDPAERISF 243
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
448-658 3.55e-12

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: 67.47  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV------HRGRwhgEVAIRllEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd06648   15 IGEGSTGIVciatdkSTGR---QVAVK--KMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVrdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGisGVVREERRENQLKL 600
Cdd:cd06648   90 ALTDIV--THTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLtSDGRVKLSDFGFCA--QVSKEVPRRKSLVG 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 601 SHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWP-FKHQPAEAL 658
Cdd:cd06648  166 TPYW---MAPEVI---------SRLPYGTEVDIWSLGIMVIEMVDGEPPyFNEPPLQAM 212
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
438-704 4.01e-12

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: 67.33  E-value: 4.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHRGRwHGE----VAIRLLEMDGHNQDHLKLfkkEVMNYRQ-TRHENVVLFMGACMNPPH-- 510
Cdd:cd06608    4 PAGIFELVEVIGEGTYGKVYKAR-HKKtgqlAAIKIMDIIEDEEEEIKL---EINILRKfSNHPNIATFYGAFIKKDPpg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 ----LAIITSFCKGRTLHSFV---RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL 582
Cdd:cd06608   80 gddqLWLVMEYCGGGSVTDLVkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLtEEAEVKLVDFGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 583 fgISGVVREERRENQLKLSHDWlcyLAPEIVR-EMIPGRDEDQlpfskAADVYAFGTVWYELQARDWPFKHQPAEALIWQ 661
Cdd:cd06608  160 --SAQLDSTLGRRNTFIGTPYW---MAPEVIAcDQQPDASYDA-----RCDVWSLGITAIELADGKPPLCDMHPMRALFK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 662 IgsgegVR----RVLASVSLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06608  230 I-----PRnpppTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLE 271
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
443-643 4.02e-12

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: 67.29  E-value: 4.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRG---RWHGEVAIRLL--EMDGHNQ--DHLKLFkkEVMNYRQTR-HENVVLFMGACMNPPHLAII 514
Cdd:cd14133    2 EVLEVLGKGTFGQVVKCydlLTGEEVALKIIknNKDYLDQslDEIRLL--ELLNKKDKAdKYHIVRLKDVFYFKNHLCIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCkGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGKVVITDFGlfgisGVVR 590
Cdd:cd14133   80 FELL-SQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILlasYSRCQIKIIDFG-----SSCF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 591 EERRENQLKLShdwLCYLAPEIvremIPGrdedqLPFSKAADVYAFGTVWYEL 643
Cdd:cd14133  154 LTQRLYSYIQS---RYYRAPEV----ILG-----LPYDEKIDMWSLGCILAEL 194
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
446-703 4.08e-12

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: 67.83  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRLLEMdgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06655   25 EKIGQGASGTVFTAIdvaTGQEVAIKQINL--QKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDpkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKLS 601
Cdd:cd06655  103 LTDVVTE--TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGmDGSVKLTDFGF--CAQITPEQSKRSTMVGT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASVSLGKEV 681
Cdd:cd06655  179 PYW---MAPEVV---------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPEKLSPIF 245
                        250       260
                 ....*....|....*....|..
gi 755537521 682 GEILSACWAFDLQERPSFSLLM 703
Cdd:cd06655  246 RDFLNRCLEMDVEKRGSAKELL 267
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
444-664 5.16e-12

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: 66.99  E-value: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVH------RGRwhgEVAIRLLEMDGHNQDHLK---LFKKEVMNYRQTRHENVVLFMGACMNPPH--LA 512
Cdd:cd06652    6 LGKLLGQGAFGRVYlcydadTGR---ELAVKQVQFDPESPETSKevnALECEIQLLKNLLHERIVQYYGCLRDPQErtLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGlfgisgvvrE 591
Cdd:cd06652   83 IFMEYMPGGSIKDQLK-SYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSvGNVKLGDFG---------A 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ERRENQLKLSHDWL-------CYLAPEIvremIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGS 664
Cdd:cd06652  153 SKRLQTICLSGTGMksvtgtpYWMSPEV----ISGEG-----YGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIAT 223
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
439-653 5.45e-12

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: 66.52  E-value: 5.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPIGQGRWGRVHRGRWHGE---VAIRLL---EMDGHNQDHLklFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSkfiLALKVLfkaQLEKAGVEHQ--LRREVEIQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgisGVVRE 591
Cdd:cd14116   82 LILEYAPLGTVYRELQK-LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLgSAGELKIADFGW----SVHAP 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 592 ERRENQLKLSHDwlcYLAPeivrEMIPGRDEDQlpfskAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14116  157 SSRRTTLCGTLD---YLPP----EMIEGRMHDE-----KVDLWSLGVLCYEFLVGKPPFEAN 206
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
433-653 5.48e-12

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: 67.36  E-value: 5.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 433 QEWDIpfeqveLGEpIGQGRWGRVHRG--RWHGEVAIRLLeMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPH 510
Cdd:cd06644   12 EVWEI------IGE-LGDGAFGKVYKAknKETGALAAAKV-IETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfGISGVV 589
Cdd:cd06644   84 LWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTlDGDIKLADFGV-SAKNVK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 590 REERRENQLKLSHdwlcYLAPEIVreMIPGRDEDqlPFSKAADVYAFGTVWYELqARDWPFKHQ 653
Cdd:cd06644  163 TLQRRDSFIGTPY----WMAPEVV--MCETMKDT--PYDYKADIWSLGITLIEM-AQIEPPHHE 217
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
471-654 5.67e-12

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: 67.36  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 471 EMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVrdPKTSLDINKTRQIAQEIIKGM 550
Cdd:cd06657   52 KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIV--THTRMNEEQIAAVCLAVLKAL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 551 GYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKLSHDWlcyLAPEIVremipgrdeDQLPFSK 629
Cdd:cd06657  130 SVLHAQGVIHRDIKSDSILLThDGRVKLSDFGF--CAQVSKEVPRRKSLVGTPYW---MAPELI---------SRLPYGP 195
                        170       180
                 ....*....|....*....|....*
gi 755537521 630 AADVYAFGTVWYELQARDWPFKHQP 654
Cdd:cd06657  196 EVDIWSLGIMVIEMVDGEPPYFNEP 220
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
436-709 6.14e-12

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 67.33  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVelgepIGQGRWGRVHRGRWHGE-----VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPH 510
Cdd:cd05089    3 DIKFEDV-----IGEGNFGQVIKAMIKKDglkmnAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVR-------DP--------KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGK 574
Cdd:cd05089   78 LYIAIEYAPYGNLLDFLRksrvletDPafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVgENLV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 575 VVITDFGLfgisgvVREER---RENQLKLSHDWLcylAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARD-WPF 650
Cdd:cd05089  158 SKIADFGL------SRGEEvyvKKTMGRLPVRWM---AIESLNYSV---------YTTKSDVWSFGVLLWEIVSLGgTPY 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 651 KHQPAEALIWQIGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05089  220 CGMTCAELYEKLPQG---YRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRM 275
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
448-646 6.75e-12

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: 67.02  E-value: 6.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-------VAIRLLEMDghnQDHLKLFKKEVMNYRQTRHENVVLFMGACMN----PPHLAIITS 516
Cdd:cd14055    3 VGKGRFAEVWKAKLKQNasgqyetVAVKIFPYE---EYASWKNEKDIFTDASLKHENILQFLTAEERgvglDRQYWLITA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK---------GIVHKDLKSKNVFY-DNGKVVITDFGL---- 582
Cdd:cd14055   80 YHENGSLQDYLT--RHILSWEDLCKMAGSLARGLAHLHSDrtpcgrpkiPIAHRDLKSSNILVkNDGTCVLADFGLalrl 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 583 --------FGISGVVREERrenqlklshdwlcYLAPEIVREMIpgRDEDQLPFsKAADVYAFGTVWYELQAR 646
Cdd:cd14055  158 dpslsvdeLANSGQVGTAR-------------YMAPEALESRV--NLEDLESF-KQIDVYSMALVLWEMASR 213
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
446-650 6.76e-12

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: 66.48  E-value: 6.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHR---GRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNyrQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd14190   10 EVLGGGKFGKVHTcteKRTGLKLAAKVINKQNSKDKEMVLLEIQVMN--QLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG---KVVITDFGLfgisgvVREERRENQLK 599
Cdd:cd14190   88 LFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRtghQVKIIDFGL------ARRYNPREKLK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 600 LSHDWLCYLAPEIVremipgrDEDQLPFSkaADVYAFGTVWYELQARDWPF 650
Cdd:cd14190  162 VNFGTPEFLSPEVV-------NYDQVSFP--TDMWSMGVITYMLLSGLSPF 203
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
495-665 6.83e-12

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: 66.26  E-value: 6.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKtsldiNKTRQIAQEII--------KGMGYLHAKGIVHKDLKSK 566
Cdd:cd08530   58 HPNIIRYKEAFLDGNRLCIVMEYAPFGDLSKLISKRK-----KKRRLFPEDDIwrifiqmlRGLKALHDQKILHRDLKSA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 567 NVF-YDNGKVVITDfglFGISGVVREERRENQLKLSHdwlcYLAPEIVRemipGRdedqlPFSKAADVYAFGTVWYELQA 645
Cdd:cd08530  133 NILlSAGDLVKIGD---LGISKVLKKNLAKTQIGTPL----YAAPEVWK----GR-----PYDYKSDIWSLGCLLYEMAT 196
                        170       180
                 ....*....|....*....|
gi 755537521 646 RDWPFKHQPAEALIWQIGSG 665
Cdd:cd08530  197 FRPPFEARTMQELRYKVCRG 216
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
448-582 7.48e-12

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: 66.82  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR--WHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGacmnpphlaIITSF----CKG 520
Cdd:cd07840    7 IGEGTYGQVYKARnkKTGElVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKE---------IVTSKgsakYKG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 521 RT----------LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGL 582
Cdd:cd07840   78 SIymvfeymdhdLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLkLADFGL 150
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
436-706 1.05e-11

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: 66.50  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVH--------------------RGRwHGEVAIRLLEMDGhNQDHLKLFKKEVMNYRQTRH 495
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEVHlcevvnpqdlptlqfpfnvrKGR-PLLVAVKILRPDA-NKNARNDFLKEVKILSRLKD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 496 ENVVLFMGACMNPPHLAIITSFCKGRTLHSFVR----DPKTSLDINKTRQ--------------IAQEIIKGMGYLHAKG 557
Cdd:cd05096   79 PNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSshhlDDKEENGNDAVPPahclpaisyssllhVALQIASGMKYLSSLN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 558 IVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLApeivreMIPGRdedqlpFSKAADVYAF 636
Cdd:cd05096  159 FVHRDLATRNCLVgENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWEC------ILMGK------FTTASDVWAF 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 637 G-TVWYELQ-ARDWPFKHQPAEALIWQigSGEGVRRVLASVSLGKE------VGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05096  227 GvTLWEILMlCKEQPYGELTDEQVIEN--AGEFFRDQGRQVYLFRPppcpqgLYELMLQCWSRDCRERPSFSDIHAFL 302
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
448-641 1.05e-11

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: 65.81  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV----HRGRWHgEVAIRLLEmdgHNQDHLKLFKKE-VMNYRQTRHENVV-LFMGACMNPPHLAIITSFCKGR 521
Cdd:cd13987    1 LGEGTYGKVllavHKGSGT-KMALKFVP---KPSTKLKDFLREyNISLELSVHPHIIkTYDVAFETEDYYVFAQEYAPYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNG--KVVITDFGLfgisgvvrEERRENQL 598
Cdd:cd13987   77 DLFSIIP-PQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLlFDKDcrRVKLCDFGL--------TRRVGSTV 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755537521 599 KLSHDWLCYLAPEiVREMIPgrdEDQLPFSKAADVYAFGTVWY 641
Cdd:cd13987  148 KRVSGTIPYTAPE-VCEAKK---NEGFVVDPSIDVWAFGVLLF 186
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
444-664 1.10e-11

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: 65.82  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVH------RGRwhgEVAIRLLEMDGHNQDHLK---LFKKEVMNYRQTRHENVVLFMGaCMNPPH---L 511
Cdd:cd06653    6 LGKLLGRGAFGEVYlcydadTGR---ELAVKQVPFDPDSQETSKevnALECEIQLLKNLRHDRIVQYYG-CLRDPEekkL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFG-ISGVV 589
Cdd:cd06653   82 SIFVEYMPGGSVKDQLK-AYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSaGNVKLGDFGASKrIQTIC 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 590 REERRENQLKLSHDWlcyLAPEIvremIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGS 664
Cdd:cd06653  161 MSGTGIKSVTGTPYW---MSPEV----ISGEG-----YGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIAT 223
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
435-653 1.33e-11

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: 65.82  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIpfeqveLGEpIGQGRWGRVHRGRwHGEVAIRLLE--MDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd06643    7 WEI------VGE-LGDGAFGKVYKAQ-NKETGILAAAkvIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITDFGLFGISgvVRE 591
Cdd:cd06643   79 ILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNIlFTLDGDIKLADFGVSAKN--TRT 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 592 ERRENQLKLSHDWlcyLAPEIVR-EMIPGRdedqlPFSKAADVYAFGTVWYELqARDWPFKHQ 653
Cdd:cd06643  157 LQRRDSFIGTPYW---MAPEVVMcETSKDR-----PYDYKADVWSLGVTLIEM-AQIEPPHHE 210
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
448-709 1.59e-11

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 65.45  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE-----VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd05047    3 IGEGNFGQVLKARIKKDglrmdAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVR-------DPK--------TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgis 586
Cdd:cd05047   83 LLDFLRksrvletDPAfaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVgENYVAKIADFGL---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 gvVREER---RENQLKLSHDWLcylAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARD-WPFKHQPAEALIWQI 662
Cdd:cd05047  159 --SRGQEvyvKKTMGRLPVRWM---AIESLNYSV---------YTTNSDVWSYGVLLWEIVSLGgTPYCGMTCAELYEKL 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 663 GSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05047  225 PQG---YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
448-654 1.63e-11

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: 65.85  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR--WHGE-VAIRLLEMDgHNQDHLKLFK-KEVMNYRQTRHENVV----LFMGACMNPPHLaiITSFCK 519
Cdd:cd07845   15 IGEGTYGIVYRARdtTSGEiVALKKVRMD-NERDGIPISSlREITLLLNLRHPNIVelkeVVVGKHLDSIFL--VMEYCE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 gRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVREERRENQL 598
Cdd:cd07845   92 -QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLtDKGCLKIADFGLARTYGLPAKPMTPKVV 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 599 KLshdWlcYLAPEIVRemipGRDEdqlpFSKAADVYAFGTVWYELqardwpFKHQP 654
Cdd:cd07845  171 TL---W--YRAPELLL----GCTT----YTTAIDMWAVGCILAEL------LAHKP 207
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
446-709 1.67e-11

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 65.19  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE------VAIRLLEMDGHNQDhLKLFKKEVMNYRQTRHENVVLFMGACMNP---PHlaIITS 516
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSdgqkihCAVKSLNRITDIEE-VEQFLKEGIIMKDFSHPNVLSLLGICLPSegsPL--VVLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgISGVVREE--- 592
Cdd:cd05058   78 YMKHGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVkVADFGL--ARDIYDKEyys 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 -RRENQLKLSHDWLcylAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDW-PFKHQPAEALIWQIGSGegvRR 670
Cdd:cd05058  156 vHNHTGAKLPVKWM---ALESLQ---------TQKFTTKSDVWSFGVLLWELMTRGApPYPDVDSFDITVYLLQG---RR 220
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 671 VLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05058  221 LLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQI 259
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
448-714 2.06e-11

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: 65.32  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR---WHGEVAIRLLEMD---GHNQDHLKLFKKEVMNyrQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd14026    5 LSRGAFGTVSRARhadWRVTVAIKCLKLDspvGDSERNCLLKEAEILH--KARFSYILPILGICNEPEFLGIVTEYMTNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDIN---KTRqIAQEIIKGMGYLH--AKGIVHKDLKSKNVFYDNG-KVVITDFGLFGISGVVREERRE 595
Cdd:cd14026   83 SLNELLHEKDIYPDVAwplRLR-ILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEfHVKIADFGLSKWRQLSISQSRS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDWLCYLAPEivrEMIPGRDEDQlpfSKAADVYAFGTVWYELQARDWPFKhQPAEALIWQIGSGEGVRRVLASV 675
Cdd:cd14026  162 SKSAPEGGTIIYMPPE---EYEPSQKRRA---SVKHDIYSYAIIMWEVLSRKIPFE-EVTNPLQIMYSVSQGHRPDTGED 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 676 SLGKEVGE------ILSACWAFDLQERPSFslLMDMLERLPKLNR 714
Cdd:cd14026  235 SLPVDIPHratlinLIESGWAQNPDERPSF--LKCLIELEPVLRT 277
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
446-700 2.12e-11

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: 65.21  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIR---LLEMDghNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPphLAIITSFCK 519
Cdd:cd14025    2 EKVGSGGFGQVYKVRhkhWKTWLAIKcppSLHVD--DSERMELLE-EAKKMEMAKFRHILPVYGICSEP--VGLVMEYME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVrdPKTSLDINKTRQIAQEIIKGMGYLH--AKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERREN 596
Cdd:cd14025   77 TGSLEKLL--ASEPLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDaHYHVKISDFGL------AKWNGLSH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWLC----YLAPEIVREmipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIwQIGSGEGVRRVL 672
Cdd:cd14025  149 SHDLSRDGLRgtiaYLPPERFKE-------KNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHI-MVKVVKGHRPSL 220
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 673 ASVSLGK-----EVGEILSACWAFDLQERPSFS 700
Cdd:cd14025  221 SPIPRQRpsecqQMICLMKRCWDQDPRKRPTFQ 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
543-662 2.16e-11

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: 65.79  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFgisgvvreerRENQLK-LSHDWLC----YLAPEIVREM 616
Cdd:cd05616  107 AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSeGHIKIADFGMC----------KENIWDgVTTKTFCgtpdYIAPEIIAYQ 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 617 ipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05616  177 ---------PYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSI 213
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
448-658 2.63e-11

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: 65.39  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV------HRGRwhgEVAIRLleMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd06659   29 IGEGSTGVVciarekHSGR---QVAVKM--MDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGVVREERRENQLKL 600
Cdd:cd06659  104 ALTDIVS--QTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTlDGRVKLSDFGF--CAQISKDVPKRKSLVG 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 601 SHDWlcyLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWP-FKHQPAEAL 658
Cdd:cd06659  180 TPYW---MAPEVI---------SRCPYGTEVDIWSLGIMVIEMVDGEPPyFSDSPVQAM 226
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
448-696 2.83e-11

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: 64.99  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE--------VAIRLLEMDGHN--QDhlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd05092   13 LGEGAFGKVFLAECHNLlpeqdkmlVAVKALKEATESarQD----FQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRD--------------PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGL 582
Cdd:cd05092   89 MRHGDLNRFLRShgpdakildggegqAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVkIGDFGM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 583 fgisgvVREERRENQLKLSHdwlcylapeivREMIPGR---DEDQL--PFSKAADVYAFGTVWYELqardWPFKHQPAea 657
Cdd:cd05092  169 ------SRDIYSTDYYRVGG-----------RTMLPIRwmpPESILyrKFTTESDIWSFGVVLWEI----FTYGKQPW-- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 658 liWQIGSGEGVRRVLASVSLGK------EVGEILSACWAFDLQER 696
Cdd:cd05092  226 --YQLSNTEAIECITQGRELERprtcppEVYAIMQGCWQREPQQR 268
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
484-705 3.07e-11

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: 64.45  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSfvrdpktslDINKTRQIA----------QEIIKGMGYL 553
Cdd:cd08218   47 RKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYK---------RINAQRGVLfpedqildwfVQLCLALKHV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 554 HAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVReerreNQLKLSHDWL---CYLAPEIVremipgrdeDQLPFSKA 630
Cdd:cd08218  118 HDRKILHRDIKSQNIFLTKDGII--KLGDFGIARVLN-----STVELARTCIgtpYYLSPEIC---------ENKPYNNK 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 631 ADVYAFGTVWYELQARDWPFKHQPAEALIWQI--GSGEGVrrvlaSVSLGKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd08218  182 SDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIirGSYPPV-----PSRYSYDLRSLVSQLFKRNPRDRPSINSILEK 253
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
444-698 3.23e-11

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: 64.51  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGRW-----HGEVAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14080    4 LGKTIGEGSYSKVKLAEYtksglKEKVACKIIDKKKAPKDFLeKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlFGisgvvREERREN 596
Cdd:cd14080   84 AEHGDLLEYIQK-RGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDsNNNVKLSDFG-FA-----RLCPDDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLShDWLC----YLAPEIVRemipGRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIW-QIGSGEGVRRV 671
Cdd:cd14080  157 GDVLS-KTFCgsaaYAAPEILQ----GIPYD----PKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKdQQNRKVRFPSS 227
                        250       260
                 ....*....|....*....|....*..
gi 755537521 672 LASVSLgkEVGEILSACWAFDLQERPS 698
Cdd:cd14080  228 VKKLSP--ECKDLIDQLLEPDPTKRAT 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
448-658 3.40e-11

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: 64.31  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW----HGEVAIRLLEmdghNQDHLK---LFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd14120    1 IGHGAFAVVFKGRHrkkpDLPVAIKCIT----KKNLSKsqnLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG----------KVVITDFGL--FGISGV 588
Cdd:cd14120   77 GDLADYLQA-KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspndiRLKIADFGFarFLQDGM 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 589 VREErrenqlklshdwLC----YLAPEIvremIPGRDEDqlpfSKaADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd14120  156 MAAT------------LCgspmYMAPEV----IMSLQYD----AK-ADLWSIGTIVYQCLTGKAPFQAQTPQEL 208
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
456-698 3.76e-11

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: 64.22  E-value: 3.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 456 VHRGRWHG-EVAI-RLLemdghnQDHLKLFKKEVMNYRQT-RHENVVLFMGACMNPPHLAIITSFCKGrTLHSFVRDPKT 532
Cdd:cd13982   18 VFRGTFDGrPVAVkRLL------PEFFDFADREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCAA-SLQDLVESPRE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 533 S-LDINKTRQ---IAQEIIKGMGYLHAKGIVHKDLKSKNVFYD------NGKVVITDFGL-----FGISGVvreeRRENQ 597
Cdd:cd13982   91 SkLFLRPGLEpvrLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahgNVRAMISDFGLckkldVGRSSF----SRRSG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDWlcyLAPEIVREMIPGRdedqlpFSKAADVYAFGTV-WYELQARDWPF-KHQPAEAliwQIGSGE-GVRRVLAS 674
Cdd:cd13982  167 VAGTSGW---IAPEMLSGSTKRR------QTRAVDIFSLGCVfYYVLSGGSHPFgDKLEREA---NILKGKySLDKLLSL 234
                        250       260
                 ....*....|....*....|....
gi 755537521 675 VSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd13982  235 GEHGPEAQDLIERMIDFDPEKRPS 258
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
537-662 3.94e-11

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: 65.03  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 537 NKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLF--GISGvvreerrENQLKLSHDWLCYLAPEIV 613
Cdd:cd05595   95 DRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKdGHIKITDFGLCkeGITD-------GATMKTFCGTPEYLAPEVL 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 614 remipgRDEDqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05595  168 ------EDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELI 207
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
448-643 3.98e-11

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: 64.98  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV--HRGRWHGEV-AIRLLEmdghnqdhlklfKKEVMNYRQTRH----ENVVLfmgacMNPPHLAIIT---SF 517
Cdd:cd05604    4 IGKGSFGKVllAKRKRDGKYyAVKVLQ------------KKVILNRKEQKHimaeRNVLL-----KNVKHPFLVGlhySF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLH---SFVRDPKTSLDINKTRQIAQ--------EIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgi 585
Cdd:cd05604   67 QTTDKLYfvlDFVNGGELFFHLQRERSFPEprarfyaaEIASALGYLHSINIVYRDLKPENILLDSqGHIVLTDFGL--- 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 586 sgvVREERRENQLKLShdwLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd05604  144 ---CKEGISNSDTTTT---FCgtpeYLAPEVIRKQ---------PYDNTVDWWCLGSVLYEM 190
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
439-711 4.42e-11

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: 64.21  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVEL--GEPIGQGRWGRVHRGRWHGE-------VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPp 509
Cdd:cd05111    4 FKETELrkLKVLGSGVFGTVHKGIWIPEgdsikipVAIKVIQ-DRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGA- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGV 588
Cdd:cd05111   82 SLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVqVADFGVADLLYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 VREERRENQLKLSHDWLCylapeiVREMIPGRdedqlpFSKAADVYAFG-TVWYELQARDWPFKHQPAEALIWQIGSGEg 667
Cdd:cd05111  162 DDKKYFYSEAKTPIKWMA------LESIHFGK------YTHQSDVWSYGvTVWEMMTFGAEPYAGMRLAEVPDLLEKGE- 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 755537521 668 vrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd05111  229 --RLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMAR 270
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
531-666 4.43e-11

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: 64.17  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 531 KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGlFGISGVVREERREnqlklshdwLC--- 606
Cdd:cd14182  104 KVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLdDDMNIKLTDFG-FSCQLDPGEKLRE---------VCgtp 173
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 607 -YLAPEIVREMIpgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14182  174 gYLAPEIIECSM---DDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGN 231
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
443-648 4.92e-11

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: 64.52  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAI-------RLLEMDGHNQDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd07841    3 EKGKKLGEGTYAVVYKARDKEtgrIVAIkkiklgeRKEAKDGINFTALR----EIKLLQELKHPNIIGLLDVFGHKSNIN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGrTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL---FGISGV 588
Cdd:cd07841   79 LVFEFMET-DLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIAsDGVLKLADFGLarsFGSPNR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 589 vreerrenqlKLSHD----WlcYLAPEIV---REmipgrdedqlpFSKAADVYAFGTVWYELQARDW 648
Cdd:cd07841  158 ----------KMTHQvvtrW--YRAPELLfgaRH-----------YGVGVDMWSVGCIFAELLLRVP 201
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
446-649 5.63e-11

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: 63.92  E-value: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG---RWHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06640   10 ERIGKGSFGEVFKGidnRTQQVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGisGVVREERRENQLKLS 601
Cdd:cd06640   89 ALDLLR--AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLsEQGDVKLADFGVAG--QLTDTQIKRNTFVGT 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 602 HDWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWP 649
Cdd:cd06640  165 PFW---MAPEVIQ---------QSAYDSKADIWSLGITAIELAKGEPP 200
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
448-708 5.73e-11

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: 64.29  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGE-VAIRLLEMDGhNQDHLKL--FKKEVMNYRQTRHENVVLFMGaCMNPPHLA-IITSFCKGr 521
Cdd:cd06633   29 IGHGSFGAVYfaTNSHTNEvVAIKKMSYSG-KQTNEKWqdIIKEVKFLQQLKHPNTIEYKG-CYLKDHTAwLVMEYCLG- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVreerreNQLKL 600
Cdd:cd06633  106 SASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLtEPGQVKLADFGSASIASPA------NSFVG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWlcyLAPEIVREMipgrDEDQlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGvrRVLASVSLGKE 680
Cdd:cd06633  180 TPYW---MAPEVILAM----DEGQ--YDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDS--PTLQSNEWTDS 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 755537521 681 VGEILSACWAFDLQERPSFSLLM--DMLER 708
Cdd:cd06633  249 FRGFVDYCLQKIPQERPSSAELLrhDFVRR 278
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
436-643 7.42e-11

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: 63.88  E-value: 7.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 436 DIPFEQVELGEPIGQGRWGRVHRGRW------HGE-VAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP 508
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKGHLylpgmdHAQlVAIKTLK-DYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 509 PHLAIITSFCKGRTLHSFV--RDP--------------KTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-D 571
Cdd:cd05090   80 QPVCMLFEFMNQGDLHEFLimRSPhsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVgE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 572 NGKVVITDFGLfgisgvvreeRREnqlKLSHDWLCYLAPEI--VREMIP-----GRdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd05090  160 QLHVKISDLGL----------SRE---IYSSDYYRVQNKSLlpIRWMPPeaimyGK------FSSDSDIWSFGVVLWEI 219
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
448-643 7.57e-11

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: 64.22  E-value: 7.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE---VAIRLLE----MDGHNQDHLkLFKKEVMnYRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDgkfYAVKVLQkktiLKKKEQNHI-MAERNVL-LKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTSLDiNKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGiSGVVREERRENqlk 599
Cdd:cd05603   81 GELFFHLQRERCFLE-PRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDcQGHVVLTDFGLCK-EGMEPEETTST--- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 600 lshdwLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd05603  156 -----FCgtpeYLAPEVLRKE---------PYDRTVDWWCLGAVLYEM 189
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
448-704 1.01e-10

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: 63.10  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNP--PHLAII--TSFCKG 520
Cdd:cd14033    9 IGRGSFKTVYRGldtETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTvrGHKCIIlvTELMTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLFGIsgvvreeRREN 596
Cdd:cd14033   89 GTLKTYLKRFR-EMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWLCYLAPEIVREmipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKH-QPAEALIWQIGSGegvrrvLASV 675
Cdd:cd14033  161 FAKSVIGTPEFMAPEMYEE----------KYDEAVDVYAFGMCILEMATSEYPYSEcQNAAQIYRKVTSG------IKPD 224
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 676 SLGK----EVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14033  225 SFYKvkvpELKEIIEGCIRTDKDERFTIQDLLE 257
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
445-706 1.14e-10

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: 63.02  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHGEVAIRLLEMD--GHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAI-ITSFCKGR 521
Cdd:cd14000   17 GEPVAVKIFNKHTSSNFANVPADTMLRHLraTDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIHPLMLVLeLAPLGSLD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGKVVITDFGLFGISgvvREERRENqL 598
Cdd:cd14000   97 HLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSAIIIKIADYGIS---RQCCRMG-A 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHDWLCYLAPEIVREMIpgrdedqlPFSKAADVYAFGTVWYELQARDWPFK--HQPAEAliwqIGSGEGVRRVLA--S 674
Cdd:cd14000  173 KGSEGTPGFRAPEIARGNV--------IYNEKVDVFSFGMLLYEILSGGAPMVghLKFPNE----FDIHGGLRPPLKqyE 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 755537521 675 VSLGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd14000  241 CAPWPEVEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
448-704 1.16e-10

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: 63.15  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPH----LAIITSFCKG 520
Cdd:cd14030   33 IGRGSFKTVYKGldtETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLFGIsgvvreeRREN 596
Cdd:cd14030  113 GTLKTYLKRFKV-MKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRAS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWLCYLAPEIVREmipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWqigsgegvRRVLASVS 676
Cdd:cd14030  185 FAKSVIGTPEFMAPEMYEE----------KYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY--------RRVTSGVK 246
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 677 LGK-------EVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14030  247 PASfdkvaipEVKEIIEGCIRQNKDERYAIKDLLN 281
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
446-650 1.20e-10

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: 63.15  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG---RWHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd06642   10 ERIGKGSFGEVYKGidnRTKEVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGisGVVREERRENQLKLS 601
Cdd:cd06642   89 ALDLLK--PGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLsEQGDVKLADFGVAG--QLTDTQIKRNTFVGT 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 602 HDWlcyLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd06642  165 PFW---MAPEVIK---------QSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
443-719 1.21e-10

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: 62.79  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwH---GE-VAIRLleMDGHN-QDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14078    6 ELHETIGSGGFAKVKLAT-HiltGEkVAIKI--MDKKAlGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD---NGKVVitDFGLFGISgvvrEERR 594
Cdd:cd14078   83 CPGGELFDYIVA-KDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDedqNLKLI--DFGLCAKP----KGGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 595 ENQLKLSHDWLCYLAPeivrEMIPGRDEdqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrrvlas 674
Cdd:cd14078  156 DHHLETCCGSPAYAAP----ELIQGKPY----IGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGK-------- 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 675 vslgKEVGEILSacwafdlqeRPSFSLLMDMLERLPK----LNRRLSHP 719
Cdd:cd14078  220 ----YEEPEWLS---------PSSKLLLDQMLQVDPKkritVKELLNHP 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
443-650 1.76e-10

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: 62.05  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR--WHGE-VAIRLLE---MDGHNQDHLKlfkKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14074    6 DLEETLGRGHFAVVKLARhvFTGEkVAVKVIDktkLDDVSKAHLF---QEVRCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV--FYDNGKVVITDFGLfgisgvVREERR 594
Cdd:cd14074   83 LGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVvfFEKQGLVKLTDFGF------SNKFQP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 595 ENQLKLSHDWLCYLAPEIVREmipgrDEDQLPfskAADVYAFGTVWYELQARDWPF 650
Cdd:cd14074  157 GEKLETSCGSLAYSAPEILLG-----DEYDAP---AVDIWSLGVILYMLVCGQPPF 204
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
443-650 1.82e-10

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: 62.33  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMD-------GHNQDHLKlfkKEVMNYRQTRHENVVLFMGACMNPPHLA 512
Cdd:cd14195    8 EMGEELGSGQFAIVRKCREKGtgkEYAAKFIKKRrlsssrrGVSREEIE---REVNILREIQHPNIITLHDIFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-----DNGKVVITDFglfgisG 587
Cdd:cd14195   85 LILELVSGGELFDFLAE-KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknvPNPRIKLIDF------G 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 588 VVREERRENQLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14195  158 IAHKIEAGNEFKNIFGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
543-650 1.90e-10

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: 62.79  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLF--GISGVVREERrenqlklshdwLC----YLAPEIVRE 615
Cdd:cd05587  103 AAEIAVGLFFLHSKGIIYRDLKLDNVMLDaEGHIKIADFGMCkeGIFGGKTTRT-----------FCgtpdYIAPEIIAY 171
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755537521 616 MipgrdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05587  172 Q---------PYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
445-650 2.00e-10

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: 61.98  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRwHG----EVAIRLLEMDGHNQDhlklFKKEVMnyrqtrHENVVLFMgaCMNPPH---------- 510
Cdd:cd14106   13 STPLGRGKFAVVRKCI-HKetgkEYAAKFLRKRRRGQD----CRNEIL------HEIAVLEL--CKDCPRvvnlhevyet 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 ---LAIITSFCKGRTLHSfVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF----YDNGKVVITDfglF 583
Cdd:cd14106   80 rseLILILELAAGGELQT-LLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILltseFPLGDIKLCD---F 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 584 GISGVVREERRENQLKLSHDwlcYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14106  156 GISRVIGEGEEIREILGTPD---YVAPEIL---------SYEPISLATDMWSIGVLTYVLLTGHSPF 210
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
486-651 2.04e-10

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: 61.87  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 486 EVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDiNKTRQIAQEIIKGMGYLHAKGIVHKDLKS 565
Cdd:cd14189   51 EIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSLAHIWKARHTLLE-PEVRYYLKQIISGLKYLHLKGILHRDLKL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 566 KNVFY-DNGKVVITDFGLfgisgVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDedqlpfskaADVYAFGTVWYELQ 644
Cdd:cd14189  130 GNFFInENMELKVGDFGL-----AARLEPPEQRKKTICGTPNYLAPEVLLRQGHGPE---------SDVWSLGCVMYTLL 195

                 ....*..
gi 755537521 645 ARDWPFK 651
Cdd:cd14189  196 CGNPPFE 202
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
448-718 2.35e-10

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: 62.76  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV---HRGRWHGEVAIRLLEMDG-HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT- 522
Cdd:cd06635   33 IGHGSFGAVyfaRDVRTSEVVAIKKMSYSGkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSAs 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 -LHSFVRDPKTSLDInktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVreerreNQLKL 600
Cdd:cd06635  113 dLLEVHKKPLQEIEI---AAITHGALQGLAYLHSHNMIHRDIKAGNILLtEPGQVKLADFGSASIASPA------NSFVG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 SHDWlcyLAPEIVREMipgrDEDQlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGvrRVLASVSLGKE 680
Cdd:cd06635  184 TPYW---MAPEVILAM----DEGQ--YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PTLQSNEWSDY 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 681 VGEILSACW----------------AFDLQERPSfSLLMDMLERLPKLNRRLSH 718
Cdd:cd06635  253 FRNFVDSCLqkipqdrptseellkhMFVLRERPE-TVLIDLIQRTKDAVRELDN 305
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
468-650 2.75e-10

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: 61.58  E-value: 2.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 468 RLLEMDGHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEII 547
Cdd:cd14088   33 KFLKRDGRKVR--KAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILD-QGYYSERDTSNVIRQVL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 548 KGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLFGI-SGVVREERRENQlklshdwlcYLAPEIVremipGRDE 622
Cdd:cd14088  110 EAVAYLHSLKIVHRNLKLENLVYynrlKNSKIVISDFHLAKLeNGLIKEPCGTPE---------YLAPEVV-----GRQR 175
                        170       180
                 ....*....|....*....|....*...
gi 755537521 623 dqlpFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14088  176 ----YGRPVDCWAIGVIMYILLSGNPPF 199
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
431-708 3.03e-10

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 62.61  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKK-EVMNYRqTRHENVVLF 501
Cdd:cd05104   26 YDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGlakadsamTVAVKMLKPSAHSTEREALMSElKVLSYL-GNHINIVNL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 502 MGAC-MNPPHLAIITSFCKGRTLH-----------------------------------------------SFVRDPKT- 532
Cdd:cd05104  105 LGACtVGGPTLVITEYCCYGDLLNflrrkrdsficpkfedlaeaalyrnllhqremacdslneymdmkpsvSYVVPTKAd 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 533 -------------------------SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgis 586
Cdd:cd05104  185 krrgvrsgsyvdqdvtseileedelALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITkICDFGL---- 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 gvVREERRENQL------KLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QARDWPFKHQPAEALI 659
Cdd:cd05104  261 --ARDIRNDSNYvvkgnaRLPVKW---MAPESIFECV---------YTFESDVWSYGILLWEIfSLGSSPYPGMPVDSKF 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 660 WQIgSGEGVrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLER 708
Cdd:cd05104  327 YKM-IKEGY-RMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQ 373
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
448-662 3.11e-10

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: 62.40  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHrgrwhgevairLLEMDGHNQDH-LKLFKKEV----------MNYRQ-----TRHENVVLFMGACMNPPHL 511
Cdd:cd05592    3 LGKGSFGKVM-----------LAELKGTNQYFaIKALKKDVvledddvectMIERRvlalaSQHPFLTHLFCTFQTESHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgVVR 590
Cdd:cd05592   72 FFVMEYLNGGDLMFHIQQ-SGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDrEGHIKIADFGM-----CKE 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 591 EERRENQLklshDWLC----YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05592  146 NIYGENKA----STFCgtpdYIAPEILK---------GQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSI 208
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
441-650 3.39e-10

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: 61.27  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRVHRG--RWHG-EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14082    4 QIFPDEVLGSGQFGIVYGGkhRKTGrDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG----KVVITDFGLFGISGvvreer 593
Cdd:cd14082   84 LHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAepfpQVKLCDFGFARIIG------ 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 594 rENQLKLS-HDWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14082  158 -EKSFRRSvVGTPAYLAPEVLRNK---------GYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
491-666 3.63e-10

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: 61.58  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 491 RQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY 570
Cdd:cd14175   50 RYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKF-FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 -----DNGKVVITDFGLfgisgvVREERRENQLKLSHdwlCY----LAPEIVREMipGRDEdqlpfskAADVYAFGTVWY 641
Cdd:cd14175  129 vdesgNPESLRICDFGF------AKQLRAENGLLMTP---CYtanfVAPEVLKRQ--GYDE-------GCDIWSLGILLY 190
                        170       180
                 ....*....|....*....|....*...
gi 755537521 642 ELQARDWPFKHQPA---EALIWQIGSGE 666
Cdd:cd14175  191 TMLAGYTPFANGPSdtpEEILTRIGSGK 218
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
510-650 3.63e-10

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: 61.88  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgISGV 588
Cdd:cd05620   70 HLFFVMEFLNGGDLMFHIQD-KGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDrDGHIKIADFGM--CKEN 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 589 VREERRENQLKLSHDwlcYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05620  147 VFGDNRASTFCGTPD---YIAPEILQ---------GLKYTFSVDWWSFGVLLYEMLIGQSPF 196
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
443-650 5.16e-10

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: 61.86  E-value: 5.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwhgevairllEMDGHNQDHL---KLFKKEVMNYR-----QTRHENVVL-------FM----G 503
Cdd:cd05614    3 ELLKVLGTGAYGKVFLVR----------KVSGHDANKLyamKVLRKAALVQKaktveHTRTERNVLehvrqspFLvtlhY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 ACMNPPHLAIITSFCKGRTL--HSFVRDpktSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDF 580
Cdd:cd05614   73 AFQTDAKLHLILDYVSGGELftHLYQRD---HFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSeGHVVLTDF 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 581 GLfgiSGVVREERRENQLKlshdwLC----YLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05614  150 GL---SKEFLTEEKERTYS-----FCgtieYMAPEIIR--------GKSGHGKAVDWWSLGILMFELLTGASPF 207
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
477-643 5.31e-10

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: 60.70  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 477 QDHLKLfKKEVMnyRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAK 556
Cdd:cd05572   37 QEHIFS-EKEIL--EECNSPFIVKLYRTFKDKKYLYMLMEYCLGGELWTILRD-RGLFDEYTARFYTACVVLAFEYLHSR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 557 GIVHKDLKSKNVFYD-NGKVVITDFGLFGISGVVREErrenqlklshdW-LC----YLAPEIvremIPGRDEDQlpfskA 630
Cdd:cd05572  113 GIIYRDLKPENLLLDsNGYVKLVDFGFAKKLGSGRKT-----------WtFCgtpeYVAPEI----ILNKGYDF-----S 172
                        170
                 ....*....|...
gi 755537521 631 ADVYAFGTVWYEL 643
Cdd:cd05572  173 VDYWSLGILLYEL 185
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
448-654 5.49e-10

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: 61.09  E-value: 5.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV--HRGRWHGE-VAIRL--LEMDGHNQDHlklFKKEVMNYRQTRHENVVlfmGACMNP----------PHLA 512
Cdd:cd14039    1 LGTGGFGNVclYQNQETGEkIAIKScrLELSVKNKDR---WCHEIQIMKKLNHPNVV---KACDVPeemnflvndvPLLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IitSFCKGRTLHSFVRDPKTSLDINKTR--QIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVV--ITDFGLfgis 586
Cdd:cd14039   75 M--EYCSGGDLRKLLNKPENCCGLKESQvlSLLSDIGSGIQYLHENKIIHRDLKPENIVLQeiNGKIVhkIIDLGY---- 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 587 gvvreERRENQLKLSHDW---LCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKH--QP 654
Cdd:cd14039  149 -----AKDLDQGSLCTSFvgtLQYLAPELF---------ENKSYTVTVDYWSFGTMVFECIAGFRPFLHnlQP 207
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
513-666 6.26e-10

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: 60.87  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLFGISGv 588
Cdd:cd14084   88 IVLELMEGGELFDRVVSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqeEECLIKITDFGLSKILG- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 589 vreerrENQLKLShdwLC----YLAPEIVremipgRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQ-PAEALIWQIG 663
Cdd:cd14084  166 ------ETSLMKT---LCgtptYLAPEVL------RSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQIL 230

                 ...
gi 755537521 664 SGE 666
Cdd:cd14084  231 SGK 233
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
448-704 6.51e-10

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: 60.89  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG----RWHgEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGA----CMNPPHLAIITSFCK 519
Cdd:cd14031   18 LGRGAFKTVYKGldteTWV-EVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSwesvLKGKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLfgiSGVVREERRE 595
Cdd:cd14031   97 SGTLKTYLKRFKV-MKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGL---ATLMRTSFAK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHdwlcYLAPEIVREMipgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSgEGVRRVLASV 675
Cdd:cd14031  173 SVIGTPE----FMAPEMYEEH----------YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVT-SGIKPASFNK 237
                        250       260
                 ....*....|....*....|....*....
gi 755537521 676 SLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14031  238 VTDPEVKEIIEGCIRQNKSERLSIKDLLN 266
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
443-650 6.61e-10

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: 60.58  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLFK----KEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14105    8 DIGEELGSGQFAVVKKCREKStglEYAAKFIKKRRSKASRRGVSRedieREVSILRQVLHPNIITLHDVFENKTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-----DNGKVVITDFGLfgisgvVR 590
Cdd:cd14105   88 ELVAGGELFDFLAE-KESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldknvPIPRIKLIDFGL------AH 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 591 EERRENQLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14105  161 KIEDGNEFKNIFGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
443-666 6.87e-10

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: 60.80  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGR----VHRGRwHGEVAIRLLEMDGHN-QDHLKLfkkeVMNYRQtrHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14177    7 ELKEDIGVGSYSVckrcIHRAT-NMEFAVKIIDKSKRDpSEEIEI----LMRYGQ--HPNIITLKDVYDDGRYVYLVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY--DNGK---VVITDFGLfgisgvVREE 592
Cdd:cd14177   80 MKGGELLDRILRQKF-FSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmdDSANadsIRICDFGF------AKQL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 RRENQLKLSHdwlCY----LAPEIVreMIPGRDedqlpfsKAADVYAFGTVWYELQARDWPFKHQP---AEALIWQIGSG 665
Cdd:cd14177  153 RGENGLLLTP---CYtanfVAPEVL--MRQGYD-------AACDIWSLGVLLYTMLAGYTPFANGPndtPEEILLRIGSG 220

                 .
gi 755537521 666 E 666
Cdd:cd14177  221 K 221
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
431-643 6.99e-10

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: 61.22  E-value: 6.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQE-----WDIPfEQVELGEPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVV--- 499
Cdd:cd07878    2 YRQElnktvWEVP-ERYQNLTPVGSGAYGSVcsaYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIgll 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 500 -LFMGACM--NPPHLAIITSFcKGRTLHSFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKV 575
Cdd:cd07878   81 dVFTPATSieNFNEVYLVTNL-MGADLNNIVKCQKLSDE--HVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVaVNEDCEL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 576 VITDFGLfgisgvVREERRENQLKLSHDWlcYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd07878  158 RILDFGL------ARQADDEMTGYVATRW--YRAPEIML--------NWMHYNQTVDIWSVGCIMAEL 209
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
546-666 7.33e-10

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: 60.80  E-value: 7.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 546 IIKGMGYLHAKGIVHKDLKSKNVFY-----DNGKVVITDFGLfgisgvVREERRENQLKLSHdwlCY----LAPEIVREM 616
Cdd:cd14178  106 ITKTVEYLHSQGVVHRDLKPSNILYmdesgNPESIRICDFGF------AKQLRAENGLLMTP---CYtanfVAPEVLKRQ 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 617 ipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQP---AEALIWQIGSGE 666
Cdd:cd14178  177 ---------GYDAACDIWSLGILLYTMLAGFTPFANGPddtPEEILARIGSGK 220
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
443-698 7.92e-10

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: 60.39  E-value: 7.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLF-KKEVMNYRQTRHENVV-LFMGACMNPPHLAIITSF 517
Cdd:cd14163    3 QLGKTIGEGTYSKVKEAFSKKhqrKVAIKIIDKSGGPEEFIQRFlPRELQIVERLDHKNIIhVYEMLESADGKIYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLfgiSGVVREERREnq 597
Cdd:cd14163   83 AEDGDVFDCVLH-GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTLKLTDFGF---AKQLPKGGRE-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 lkLSHDW---LCYLAPEIVRemipGRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRrvlAS 674
Cdd:cd14163  157 --LSQTFcgsTAYAAPEVLQ----GVPHD----SRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKGVSLP---GH 223
                        250       260
                 ....*....|....*....|....
gi 755537521 675 VSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd14163  224 LGVSRTCQDLLKRLLEPDMVLRPS 247
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
448-698 9.01e-10

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: 60.39  E-value: 9.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-----EVAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC---- 518
Cdd:cd05087    5 IGHGWFGKVFLGEVNSglsstQVVVKELKASASVQDQMQ-FLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCplgd 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 -KG-----RTLHSFVRDPKTsldinkTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLFGISgvVRE 591
Cdd:cd05087   84 lKGylrscRAAESMAPDPLT------LQRMACEVACGLLHLHRNNFVHSDLALRNcLLTADLTVKIGDYGLSHCK--YKE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ER--RENQLKLSHDWlcyLAPEIVREmIPGR--DEDQlpfSKAADVYAFG-TVW--YELQARDWPfKHQPAEALIWQIGS 664
Cdd:cd05087  156 DYfvTADQLWVPLRW---IAPELVDE-VHGNllVVDQ---TKQSNVWSLGvTIWelFELGNQPYR-HYSDRQVLTYTVRE 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755537521 665 GE-GVRRVLASVSLGKEVGEILSACWaFDLQERPS 698
Cdd:cd05087  228 QQlKLPKPQLKLSLAERWYEVMQFCW-LQPEQRPT 261
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
443-698 9.10e-10

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: 60.37  E-value: 9.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHGE---VAIRLLEMDGhNQDHLKLFK-KEVMNYRQTR---HENVVLFMGACMNPP-----H 510
Cdd:cd07838    2 EEVAEIGEGAYGTVYKARDLQDgrfVALKKVRVPL-SEEGIPLSTiREIALLKQLEsfeHPNVVRLLDVCHGPRtdrelK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKgRTLHSFVRD-PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGI--- 585
Cdd:cd07838   81 LTLVFEHVD-QDLATYLDKcPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSdGQVKLADFGLARIysf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 586 -----SGVVReerrenqlklshdwLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQAR-------------- 646
Cdd:cd07838  160 emaltSVVVT--------------LWYRAPEVLL---------QSSYATPVDMWSVGCIFAELFNRrplfrgsseadqlg 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 647 ------------DWPfkhqPAEALIWQIGSGEGVRRVLASV-SLGKEVGEILSACWAFDLQERPS 698
Cdd:cd07838  217 kifdviglpseeEWP----RNSALPRSSFPSYTPRPFKSFVpEIDEEGLDLLKKMLTFNPHKRIS 277
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
448-656 9.26e-10

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: 60.54  E-value: 9.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG---EVAIRL--LEMDGHNQdHLKLFKKEVMNYRQTRHENVVlfmGACMNPPHLAIIT------- 515
Cdd:cd13989    1 LGSGGFGYVTLWKHQDtgeYVAIKKcrQELSPSDK-NRERWCLEVQIMKKLNHPNVV---SARDVPPELEKLSpndlpll 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 --SFCKGRTLHSFVRDPKTS--LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVV--ITDFGLfgisg 587
Cdd:cd13989   77 amEYCSGGDLRKVLNQPENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQqgGGRVIykLIDLGY----- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 588 vVREerrenqlkLSHDWLC--------YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKH--QPAE 656
Cdd:cd13989  152 -AKE--------LDQGSLCtsfvgtlqYLAPELFE---------SKKYTCTVDYWSFGTLAFECITGYRPFLPnwQPVQ 212
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
495-645 1.06e-09

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: 60.13  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRD--PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD- 571
Cdd:cd14052   62 HDNIVQLIDSWEYHGHLYIQTELCENGSLDVFLSElgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITf 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 572 NGKVVITDFGLFG----ISGVVREERREnqlklshdwlcYLAPEIVREMIPGrdedqlpfsKAADVYAFGTVWYELQA 645
Cdd:cd14052  142 EGTLKIGDFGMATvwplIRGIEREGDRE-----------YIAPEILSEHMYD---------KPADIFSLGLILLEAAA 199
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
446-709 1.20e-09

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: 59.87  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHR---GRWHGEVAIRLLEMDGHNQdhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd14104    6 EELGRGQFGIVHRcveTSSKKTYMAKFVKVKGADQ---VLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLD----INKTRQIAQeiikGMGYLHAKGIVHKDLKSKNVFYDNGK---VVITDFGLfgisgvVREERRE 595
Cdd:cd14104   83 IFERITTARFELNereiVSYVRQVCE----ALEFLHSKNIGHFDIRPENIIYCTRRgsyIKIIEFGQ------SRQLKPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDWLCYLAPEIVR-EMIpgrdedqlpfSKAADVYAFGTVWYELQARDWPFkhqpaealiwqigSGEGVRRVLAS 674
Cdd:cd14104  153 DKFRLQYTSAEFYAPEVHQhESV----------STATDMWSLGCLVYVLLSGINPF-------------EAETNQQTIEN 209
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755537521 675 vslgkevgeILSACWAFDLQERPSFSL-LMDMLERL 709
Cdd:cd14104  210 ---------IRNAEYAFDDEAFKNISIeALDFVDRL 236
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
450-689 1.22e-09

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 60.04  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 450 QGRWGRVHRGRWHGE-VAIRLLEMdghnQDHLKL-FKKEVMNYRQTRHENVVLFMGACMNPPHLA----IITSFCKGRTL 523
Cdd:cd14140    5 RGRFGCVWKAQLMNEyVAVKIFPI----QDKQSWqSEREIFSTPGMKHENLLQFIAAEKRGSNLEmelwLITAFHDKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDpkTSLDINKTRQIAQEIIKGMGYLH-----AKG------IVHKDLKSKNVFYDNG-KVVITDFGLfgisgVVRE 591
Cdd:cd14140   81 TDYLKG--NIVSWNELCHIAETMARGLSYLHedvprCKGeghkpaIAHRDFKSKNVLLKNDlTAVLADFGL-----AVRF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 E------RRENQLKLSHdwlcYLAPEIVremipgrdEDQLPFSKAA----DVYAFGTVWYELQAR----DWPFKHQ--PA 655
Cdd:cd14140  154 EpgkppgDTHGQVGTRR----YMAPEVL--------EGAINFQRDSflriDMYAMGLVLWELVSRckaaDGPVDEYmlPF 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 656 EALIWQIGSGEGVRRVLASvslgKEVGEILSACW 689
Cdd:cd14140  222 EEEIGQHPSLEDLQEVVVH----KKMRPVFKDHW 251
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
446-651 1.23e-09

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: 60.33  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVH--RGRWHGEV-AIRLL---EMDGHNQDHLKLFKKEVMnyRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd05574    7 KLLGKGDVGRVYlvRLKGTGKLfAMKVLdkeEMIKRNKVKRVLTEREIL--ATLDHPFLPTLYASFQTSTHLCFVMDYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFV-RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLFGISGVV-------- 589
Cdd:cd05574   85 GGELFRLLqKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILlHESGHIMLTDFDLSKQSSVTpppvrksl 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 590 -REERRENQLKLSHDWLC---------------YLAPEIVRemipGRDEdqlpfSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd05574  165 rKGSRRSSVKSIEKETFVaepsarsnsfvgteeYIAPEVIK----GDGH-----GSAVDWWTLGILLYEMLYGTTPFK 233
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
545-650 1.26e-09

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: 60.01  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvREERRENQLKLSHDW---LCYLAPEIVREMIPGR 620
Cdd:cd05613  113 EIVLALEHLHKLGIIYRDIKLENILLDsSGHVVLTDFGL-------SKEFLLDENERAYSFcgtIEYMAPEIVRGGDSGH 185
                         90       100       110
                 ....*....|....*....|....*....|
gi 755537521 621 DedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05613  186 D-------KAVDWWSLGVLMYELLTGASPF 208
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
543-643 1.28e-09

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: 60.41  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQlklSHDWLC----YLAPEIVREMi 617
Cdd:cd05575  102 AAEIASALGYLHSLNIIYRDLKPENILLDsQGHVVLTDFGL------CKEGIEPSD---TTSTFCgtpeYLAPEVLRKQ- 171
                         90       100
                 ....*....|....*....|....*.
gi 755537521 618 pgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd05575  172 --------PYDRTVDWWCLGAVLYEM 189
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
448-687 1.29e-09

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: 60.31  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW---HGEVAIRLLEMDGHNQD---HLKLFKKEVMNYRQTrHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd05590    3 LGKGSFGKVMLARLkesGRLYAVKVLKKDVILQDddvECTMTEKRILSLARN-HPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgvVREERRENQLKL 600
Cdd:cd05590   82 DLMFHIQKSR-RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHeGHCKLADFGM------CKEGIFNGKTTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 601 ShdwLC----YLAPEIVREMIPGRDedqlpfskaADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrrVLASVS 676
Cdd:cd05590  155 T---FCgtpdYIAPEILQEMLYGPS---------VDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDE----VVYPTW 218
                        250
                 ....*....|.
gi 755537521 677 LGKEVGEILSA 687
Cdd:cd05590  219 LSQDAVDILKA 229
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
448-704 1.50e-09

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: 60.04  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR---WHGEVAIRLLEMDG-HNQDHLKLFKKEVMNYRQTRHENVVLFMGaCMNPPHLA-IITSFCKGrT 522
Cdd:cd06634   23 IGHGSFGAVYFARdvrNNEVVAIKKMSYSGkQSNEKWQDIIKEVKFLQKLRHPNTIEYRG-CYLREHTAwLVMEYCLG-S 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVreerreNQLKLS 601
Cdd:cd06634  101 ASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLtEPGLVKLGDFGSASIMAPA------NSFVGT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 602 HDWlcyLAPEIVREMipgrDEDQlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGvrRVLASVSLGKEV 681
Cdd:cd06634  175 PYW---MAPEVILAM----DEGQ--YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNES--PALQSGHWSEYF 243
                        250       260
                 ....*....|....*....|...
gi 755537521 682 GEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06634  244 RNFVDSCLQKIPQDRPTSDVLLK 266
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
428-582 1.52e-09

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: 59.83  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 428 TSVYLQEwdipFEQVELgepIGQGRWGRVH--RGRWHGEV-AIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd14049    1 TSRYLNE----FEEIAR---LGKGGYGKVYkvRNKLDGQYyAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLA--IITSFCKgRTLHSFVRD-------------PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd14049   74 WMEHVQLMlyIQMQLCE-LSLWDWIVErnkrpceeefksaPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIF 152
                        170
                 ....*....|....*
gi 755537521 570 Y--DNGKVVITDFGL 582
Cdd:cd14049  153 LhgSDIHVRIGDFGL 167
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
431-709 1.75e-09

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 60.42  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM 502
Cdd:cd05105   28 YDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGlsrsqpvmKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHLAIITSFCKGRTLHSFV---RD---------PKTSLDI-------NKTRQ---------------------- 541
Cdd:cd05105  108 GACTKSGPIYIITEYCFYGDLVNYLhknRDnflsrhpekPKKDLDIfginpadESTRSyvilsfenkgdymdmkqadttq 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 542 ------------------------------------------------------IAQEIIKGMGYLHAKGIVHKDLKSKN 567
Cdd:cd05105  188 yvpmleikeaskysdiqrsnydrpasykgsndsevknllsddgseglttldllsFTYQVARGMEFLASKNCVHRDLAARN 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 568 VFYDNGKVV-ITDFGLfgisgvVREERRE-NQLKLSHDWLcylaPeiVREMIPGRDEDQLpFSKAADVYAFGTVWYEL-Q 644
Cdd:cd05105  268 VLLAQGKIVkICDFGL------ARDIMHDsNYVSKGSTFL----P--VKWMAPESIFDNL-YTTLSDVWSYGILLWEIfS 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 645 ARDWPFKHQPAEALIW-QIGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05105  335 LGGTPYPGMIVDSTFYnKIKSG---YRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
449-653 1.83e-09

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: 59.07  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 449 GQGRWGRVH--RGRWHGEV---AIRLLEMDGHNQdhlklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT- 522
Cdd:cd14111   12 ARGRFGVIRrcRENATGKNfpaKIVPYQAEEKQG-----VLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKEl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIaqEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFG---LFGISGVVREERRENQL 598
Cdd:cd14111   87 LHSLIDRFRYSEDDVVGYLV--QILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIkIVDFGsaqSFNPLSLRQLGRRTGTL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 599 KlshdwlcYLAPeivrEMIPGRdedqlPFSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14111  165 E-------YMAP----EMVKGE-----PVGPPADIWSIGVLTYIMLSGRSPFEDQ 203
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
464-703 1.93e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 59.18  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 464 EVAIRLLEMD-GHNQDHLKLFKKEVMnYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQI 542
Cdd:cd05077   36 EIKVILKVLDpSHRDISLAFFETASM-MRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDVLTTPWKFKV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFY-------DNGKVV-ITDFGLfGISGVVREERRENqlklshdwLCYLAPEIVr 614
Cdd:cd05077  115 AKQLASALSYLEDKDLVHGNVCTKNILLaregidgECGPFIkLSDPGI-PITVLSRQECVER--------IPWIAPECV- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 615 emipgrdEDQLPFSKAADVYAFGTVWYELQAR-DWPFKHQpaeALIWQIGSGEGvRRVLASVSLgKEVGEILSACWAFDL 693
Cdd:cd05077  185 -------EDSKNLSIAADKWSFGTTLWEICYNgEIPLKDK---TLAEKERFYEG-QCMLVTPSC-KELADLMTHCMNYDP 252
                        250
                 ....*....|
gi 755537521 694 QERPSFSLLM 703
Cdd:cd05077  253 NQRPFFRAIM 262
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
446-650 1.99e-09

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: 59.21  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE---VAIRLLEMDGHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTgltLAAKIIKVKGAKER--EEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPK---TSLD-INKTRQIAQeiikGMGYLHAKGIVHKDLKSKNVFYDN---GKVVITDFGLfgisgvVREERRE 595
Cdd:cd14192   88 LFDRITDESyqlTELDaILFTRQICE----GVHYLHQHYILHLDLKPENILCVNstgNQIKIIDFGL------ARRYKPR 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 596 NQLKLSHDWLCYLAPEIVremipgrDEDQLPFskAADVYAFGTVWYELQARDWPF 650
Cdd:cd14192  158 EKLKVNFGTPEFLAPEVV-------NYDFVSF--PTDMWSVGVITYMLLSGLSPF 203
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
439-712 2.21e-09

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: 59.09  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRVH--RGRWHGEV----AIRLLEMDGHNQDHLKlfkKEVMNYRQTRHENVVLFMGACMNPPH-- 510
Cdd:cd08217    2 YEVLET---IGKGSFGTVRkvRRKSDGKIlvwkEIDYGKMSEKEKQQLV---SEVNILRELKHPNIVRYYDRIVDRANtt 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPK---TSLDINKTRQIAQEIIKGMGYLHAKG-----IVHKDLKSKNVFYDNGKVV-ITDFG 581
Cdd:cd08217   76 LYIVMEYCEGGDLAQLIKKCKkenQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVkLGDFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 582 LfgisgvVREERRENQLklSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd08217  156 L------ARVLSHDSSF--AKTYVgtpYYMSPELLNEQ---------SYDEKSDIWSLGCLIYELCALHPPFQAANQLEL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 659 IWQIGSGEgVRRVLASVSlgKEVGEILSACWAFDLQERPSfsllMDMLERLPKL 712
Cdd:cd08217  219 AKKIKEGK-FPRIPSRYS--SELNEVIKSMLNVDPDKRPS----VEELLQLPLI 265
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-698 2.28e-09

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: 58.99  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRV----HRgRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPP-HLAIITSF 517
Cdd:cd08223    3 QFLRVIGKGSYGEVwlvrHK-RDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVreerrEN 596
Cdd:cd08223   82 CEGGDLYTRLKEQKgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNII--KVGDLGIARVL-----ES 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGegvRRVLA 673
Cdd:cd08223  155 SSDMATTLIgtpYYMSPELFSNK---------PYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEG---KLPPM 222
                        250       260
                 ....*....|....*....|....*
gi 755537521 674 SVSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd08223  223 PKQYSPELGELIKAMLHQDPEKRPS 247
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
431-643 2.33e-09

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: 59.67  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQE-----WDIPfEQVELGEPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM 502
Cdd:cd07877    4 YRQElnktiWEVP-ERYQNLSPVGSGAYGSVcaaFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHL-----AIITSFCKGRTLHSFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVV 576
Cdd:cd07877   83 DVFTPARSLeefndVYLVTHLMGADLNNIVKCQKLTDD--HVQFLIYQILRGLKYIHSADIIHRDLKPSNLaVNEDCELK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 577 ITDFGLfgisgvVREERRENQLKLSHDWlcYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd07877  161 ILDFGL------ARHTDDEMTGYVATRW--YRAPEIML--------NWMHYNQTVDIWSVGCIMAEL 211
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
444-665 2.48e-09

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: 58.82  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRV----HRGRWHgEVAIRLL--------EMDGhnqdhlKLfKKEVMNYRQTRHENVVLFMGACMNPPHL 511
Cdd:cd14079    6 LGKTLGVGSFGKVklaeHELTGH-KVAVKILnrqkikslDMEE------KI-RREIQILKLFRHPHIIRLYEVIETPTDI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVR 590
Cdd:cd14079   78 FMVMEYVSGGELFDYIVQ-KGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVkIADFGL---SNIMR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 591 EerrENQLKLShdwlC----YLAPEIvremIPGRdedqLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSG 665
Cdd:cd14079  154 D---GEFLKTS----CgspnYAAPEV----ISGK----LYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSG 217
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
465-661 2.52e-09

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: 59.50  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 465 VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSlDINKT--RQI 542
Cdd:cd08226   28 VTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLLKTYFPE-GMNEAliGNI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYdNGKVVITDFGLFGISGVVREERREnqlKLSHDW-------LCYLAPEIVRE 615
Cdd:cd08226  107 LYGAIKALNYLHQNGCIHRSVKASHILI-SGDGLVSLSGLSHLYSMVTNGQRS---KVVYDFpqfstsvLPWLSPELLRQ 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 616 MIPGrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQ 661
Cdd:cd08226  183 DLHG-------YNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQ 221
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
448-643 2.64e-09

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: 59.65  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGE---VAIRLLemdghnQDHLKLFKKE---VMNYRQT-----RHENVVLFMGACMNPPHLAIITS 516
Cdd:cd05602   15 IGKGSFGKVLLARHKSDekfYAVKVL------QKKAILKKKEekhIMSERNVllknvKHPFLVGLHFSFQTTDKLYFVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTSLDiNKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgvVREERRE 595
Cdd:cd05602   89 YINGGELFYHLQRERCFLE-PRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSqGHIVLTDFGL------CKENIEP 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755537521 596 NQLKLShdwLC----YLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd05602  162 NGTTST---FCgtpeYLAPEVLHKQ---------PYDRTVDWWCLGAVLYEM 201
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
538-658 2.67e-09

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: 59.29  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 538 KTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQLKLShdwLC----YLAPEI 612
Cdd:cd05571   96 RTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDkDGHIKITDFGL------CKEEISYGATTKT---FCgtpeYLAPEV 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 613 VremipgRDEDqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd05571  167 L------EDND---YGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVL 203
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
446-614 2.69e-09

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: 58.45  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGE----VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGarevVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLS 601
Cdd:cd14121   81 DLSRFIRSRRT-LPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLRGS 159
                        170
                 ....*....|...
gi 755537521 602 HdwlCYLAPEIVR 614
Cdd:cd14121  160 P---LYMAPEMIL 169
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
442-656 2.81e-09

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: 58.97  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEpIGQGRWGRVHRGRWHGE---VAIRLLEMDGHNQDHLKLFKKEVMNyRQTRHENVVLFMGACMN--PPHLAIITS 516
Cdd:cd06621    4 VELSS-LGEGAGGSVTKCRLRNTktiFALKTITTDPNPDVQKQILRELEIN-KSCASPYIVKYYGAFLDeqDSSIGIAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRD-PKTSLDINKT--RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfglFGISGVVREE 592
Cdd:cd06621   82 YCEGGSLDSIYKKvKKKGGRIGEKvlGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTrKGQVKLCD---FGVSGELVNS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 593 RRENQLKLSHdwlcYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFkhqPAE 656
Cdd:cd06621  159 LAGTFTGTSY----YMAPERIQ---------GGPYSITSDVWSLGLTLLEVAQNRFPF---PPE 206
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
448-656 2.82e-09

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: 59.22  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW-----HGEVAIRLLEMDGHNQDHLKLFK-KEVMNYRQTRHENVVLFMGACMNPPHLAI--ITSFCK 519
Cdd:cd07842    8 IGRGTYGRVYKAKRkngkdGKEYAIKKFKGDKEQYTGISQSAcREIALLRELKHENVVSLVEVFLEHADKSVylLFDYAE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLH--SFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-----YDNGKVVITDFGLFGISgvvre 591
Cdd:cd07842   88 HDLWQiiKFHRQAKrVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILvmgegPERGVVKIGDLGLARLF----- 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 592 errENQLKLSHD--------WlcYLAPEIvreMIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAE 656
Cdd:cd07842  163 ---NAPLKPLADldpvvvtiW--YRAPEL---LLGARH-----YTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
443-650 2.86e-09

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: 58.81  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLFK----KEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14196    8 DIGEELGSGQFAIVKKCREKStglEYAAKFIKKRQSRASRRGVSReeieREVSILRQVLHPNIITLHDVYENRTDVVLIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGL--FGISGVVREER 593
Cdd:cd14196   88 ELVSGGELFDFLAQ-KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLidFGLAHEIEDGV 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 594 RENQLKLSHDwlcYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14196  167 EFKNIFGTPE---FVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF 211
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
545-650 3.00e-09

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: 58.56  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGISGVVREERrenqlklSHDWlC----YLAPEIVREMIPG 619
Cdd:cd05583  107 EIVLALEHLHKLGIIYRDIKLENILLDsEGHVVLTDFGLSKEFLPGENDR-------AYSF-CgtieYMAPEVVRGGSDG 178
                         90       100       110
                 ....*....|....*....|....*....|.
gi 755537521 620 RDedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05583  179 HD-------KAVDWWSLGVLTYELLTGASPF 202
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
545-650 3.01e-09

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: 59.34  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQlkLSHDWlC----YLAPEIVreMIPG 619
Cdd:cd05584  108 EITLALGHLHSLGIIYRDLKPENILLDaQGHVKLTDFGL------CKESIHDGT--VTHTF-CgtieYMAPEIL--TRSG 176
                         90       100       110
                 ....*....|....*....|....*....|.
gi 755537521 620 RDedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05584  177 HG-------KAVDWWSLGALMYDMLTGAPPF 200
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
199-242 3.10e-09

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 53.18  E-value: 3.10e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 199 HRFSTKS-WLSQVCNVCQKSMIFG---VKCKHCRLKCHNKCTKEAP-AC 242
Cdd:cd20821    3 HRFVSKTvIKPETCVVCGKRIKFGkkaLKCKDCRVVCHPDCKDKLPlPC 51
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
443-643 3.16e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 60.19  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRG---RWHGEVAIRLLEMD-GHNQDHLKLFKKEVMNYRQTRHENVV-------------LFMgac 505
Cdd:NF033483  10 EIGERIGRGGMAEVYLAkdtRLDRDVAVKVLRPDlARDPEFVARFRREAQSAASLSHPNIVsvydvgedggipyIVM--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 mnpphlaiitSFCKGRTLHSFVRD-----PKTSLDInkTRQIAQeiikGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITD 579
Cdd:NF033483  87 ----------EYVDGRTLKDYIREhgplsPEEAVEI--MIQILS----ALEHAHRNGIVHRDIKPQNILITkDGRVKVTD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 580 FGLF------------GISGVVreerrenqlklsHdwlcYLAPEIVR-EMIPGRdedqlpfskaADVYAFGTVWYEL 643
Cdd:NF033483 151 FGIAralssttmtqtnSVLGTV------------H----YLSPEQARgGTVDAR----------SDIYSLGIVLYEM 201
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
481-711 3.30e-09

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: 58.87  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 481 KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVR---------------DPKTSLDINKTRQIAQE 545
Cdd:cd05094   52 KDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRahgpdamilvdgqprQAKGELGLSQMLHIATQ 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 546 IIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLFGISGVVREERRENQLKLSHDWLcylAPEIVREMipgrdedq 624
Cdd:cd05094  132 IASGMVYLASQHFVHRDLATRNCLVGANLLVkIGDFGMSRDVYSTDYYRVGGHTMLPIRWM---PPESIMYR-------- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 625 lPFSKAADVYAFGTVWYELqardWPFKHQPAealiWQIGSGEGVR-----RVLASVSL-GKEVGEILSACWAFDLQERPS 698
Cdd:cd05094  201 -KFTTESDVWSFGVILWEI----FTYGKQPW----FQLSNTEVIEcitqgRVLERPRVcPKEVYDIMLGCWQREPQQRLN 271
                        250
                 ....*....|...
gi 755537521 699 FSLLMDMLERLPK 711
Cdd:cd05094  272 IKEIYKILHALGK 284
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
495-705 3.46e-09

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: 58.21  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKtsldinktRQIAQE---------IIKGMGYLHAKGIVHKDLKS 565
Cdd:cd08221   58 HDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQK--------NQLFPEevvlwylyqIVSAVSHIHKAGILHRDIKT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 566 KNVFYDngKVVITDFGLFGISGVVREERRENQLKLSHDWlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQA 645
Cdd:cd08221  130 LNIFLT--KADLVKLGDFGISKVLDSESSMAESIVGTPY--YMSPELVQGV---------KYNFKSDIWAVGCVLYELLT 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 646 RDWPFKHQPAEALIWQIGSGEgvrRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd08221  197 LKRTFDATNPLRLAVKIVQGE---YEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLER 253
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
455-709 3.55e-09

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


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 58.36  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 455 RVHRGRWHGEVAI--RLLEMDGHNQDHLKLfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDP-- 530
Cdd:cd14044   23 RLRQGKYDKKVVIlkDLKNNEGNFTEKQKI---ELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKis 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 531 ---KTSLDINKTRQIAQEIIKGMGYLHAKGI-VHKDLKSKNVFYDNGKVV-ITDFGLFGIsgvvreerrenqLKLSHDwl 605
Cdd:cd14044  100 ypdGTFMDWEFKISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVkITDFGCNSI------------LPPSKD-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 606 CYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPF---KHQPAEALIWQIGSGEGVRRVLASVSLG---- 678
Cdd:cd14044  166 LWTAPEHLR---------QAGTSQKGDVYSYGIIAQEIILRKETFytaACSDRKEKIYRVQNPKGMKPFRPDLNLEsage 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 755537521 679 --KEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd14044  237 reREVYGLVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
539-719 3.59e-09

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: 58.04  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 539 TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDfglFGISGVVREERRENQLKLShdwLCYLAPEIVREMI 617
Cdd:cd05578  102 VKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEqGHVHITD---FNIATKLTDGTLATSTSGT---KPYMAPEVFMRAG 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 618 pgrdedqlpFSKAADVYAFGTVWYELQARDWPFKhqpaealiwqIGSGEGVRRVLASVslgKEVGEILSACWAFDLqerp 697
Cdd:cd05578  176 ---------YSFAVDWWSLGVTAYEMLRGKRPYE----------IHSRTSIEEIRAKF---ETASVLYPAGWSEEA---- 229
                        170       180
                 ....*....|....*....|..
gi 755537521 698 sFSLLMDMLERLPKlnRRLSHP 719
Cdd:cd05578  230 -IDLINKLLERDPQ--KRLGDL 248
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
486-704 3.77e-09

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: 58.09  E-value: 3.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 486 EVMNYRQ-TRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSldINKTRQIAQEIIKGMGYLHAKGIVHKDLK 564
Cdd:cd14050   50 EVERHEKlGEHPNCVRFIKAWEEKGILYIQTELCDTSLQQYCEETHSLP--ESEVWNILLDLLKGLKHLHDHGLIHLDIK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 565 SKNVFYDNGKVV-ITDFGLfgisgvVREERRENQLKLSHDWLCYLAPEIVRemipGRdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd14050  128 PANIFLSKDGVCkLGDFGL------VVELDKEDIHDAQEGDPRYMAPELLQ----GS------FTKAADIFSLGITILEL 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 644 qARDWpfkHQPAEALIW-QIGSGEGVRRVLASVSlgKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14050  192 -ACNL---ELPSGGDGWhQLRQGYLPEEFTAGLS--PELRSIIKLMMDPDPERRPTAEDLLA 247
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
445-703 3.83e-09

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: 58.56  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVH------RGRwhgEVAIRLLEMDGHNQDHLK---LFKKEVMNYRQTRHENVVLFMGACMNPPH--LAI 513
Cdd:cd06651   12 GKLLGQGAFGRVYlcydvdTGR---ELAAKQVQFDPESPETSKevsALECEIQLLKNLQHERIVQYYGCLRDRAEktLTI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 514 ITSFCKGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGlfgisgvvrEE 592
Cdd:cd06651   89 FMEYMPGGSVKDQLK-AYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSaGNVKLGDFG---------AS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 593 RRENQLKLSHDWL-------CYLAPEIVREMIPGRDedqlpfskaADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSG 665
Cdd:cd06651  159 KRLQTICMSGTGIrsvtgtpYWMSPEVISGEGYGRK---------ADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQ 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755537521 666 EGVRRVLASVSlgkEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06651  230 PTNPQLPSHIS---EHARDFLGCIFVEARHRPSAEELL 264
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
485-651 4.08e-09

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: 58.10  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 485 KEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDiNKTRQIAQEIIKGMGYLHAKGIVHKDLK 564
Cdd:cd14188   50 KEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTE-PEVRYYLRQIVSGLKYLHEQEILHRDLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 565 SKNVFY-DNGKVVITDFGLfgisgVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDedqlpfskaADVYAFGTVWYEL 643
Cdd:cd14188  129 LGNFFInENMELKVGDFGL-----AARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCE---------SDIWALGCVMYTM 194

                 ....*...
gi 755537521 644 QARDWPFK 651
Cdd:cd14188  195 LLGRPPFE 202
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
522-650 4.65e-09

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 58.66  E-value: 4.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSF--VRDPKTSldiNKTRQIAQeIIKGMGYLHAKGIVHKDLKSKNVF--YDNG---KVVITDFGLfgisgVVREERR 594
Cdd:cd14018  125 TLRQYlwVNTPSYR---LARVMILQ-LLEGVDHLVRHGIAHRDLKSDNILleLDFDgcpWLVIADFGC-----CLADDSI 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 595 ENQLKLSHDWL------CYLAPEIVREMiPGRDEdQLPFSKaADVYAFGTVWYELQARDWPF 650
Cdd:cd14018  196 GLQLPFSSWYVdrggnaCLMAPEVSTAV-PGPGV-VINYSK-ADAWAVGAIAYEIFGLSNPF 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
440-676 4.80e-09

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: 58.11  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHG---EVAIRLLEMD-------GHNQDHLKlfkKEVMNYRQTRHENVVLFMGACMNPP 509
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKStglQYAAKFIKKRrtkssrrGVSREDIE---REVSILKEIQHPNVITLHEVYENKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-----KVVITDFGL-- 582
Cdd:cd14194   82 DVILILELVAGGELFDFLAE-KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnvpkpRIKIIDFGLah 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 583 ---FGisgvvreerreNQLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFkhqpaeali 659
Cdd:cd14194  161 kidFG-----------NEFKNIFGTPEFVAPEIV---------NYEPLGLEADMWSIGVITYILLSGASPF--------- 211
                        250
                 ....*....|....*..
gi 755537521 660 wqigSGEGVRRVLASVS 676
Cdd:cd14194  212 ----LGDTKQETLANVS 224
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
534-662 4.98e-09

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: 58.78  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 534 LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFgisgvvreerRENQL-KLSHDWLC----Y 607
Cdd:cd05619  103 FDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKdGHIKIADFGMC----------KENMLgDAKTSTFCgtpdY 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 608 LAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05619  173 IAPEILLGQ---------KYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI 218
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
431-709 5.20e-09

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


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 58.70  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHG--------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM 502
Cdd:cd05106   29 YNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGlgkednvlRVAVKMLKASAHTDEREALMSELKILSHLGQHKNIVNLL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHLAIITSFCKGRTLHSFVR------------------------------------------------------ 528
Cdd:cd05106  109 GACTHGGPVLVITEYCCYGDLLNFLRkkaetflnfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvemrpvs 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 529 ---------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLF-----GISG 587
Cdd:cd05106  189 ssssqssdskdeedtEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAkICDFGLArdimnDSNY 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 588 VVREERRenqlkLSHDWlcyLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYEL-QARDWPFKHQPAEALIWQ-IGSG 665
Cdd:cd05106  269 VVKGNAR-----LPVKW---MAPESIFDCV---------YTVQSDVWSYGILLWEIfSLGKSPYPGILVNSKFYKmVKRG 331
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 666 EGVRR-VLASvslgKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05106  332 YQMSRpDFAP----PEIYSIMKMCWNLEPTERPTFSQISQLIQRQ 372
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
495-666 5.48e-09

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: 58.47  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY---- 570
Cdd:cd14092   58 HPNIVKLHEVFQDELHTYLVMELLRGGELLERIR-KKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtded 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 DNGKVVITDFGLfgisgvVREERRENQLKLSHDWLCYLAPEIVREMI--PGRDEdqlpfskAADVYAFGTVWYELQARDW 648
Cdd:cd14092  137 DDAEIKIVDFGF------ARLKPENQPLKTPCFTLPYAAPEVLKQALstQGYDE-------SCDLWSLGVILYTMLSGQV 203
                        170       180
                 ....*....|....*....|..
gi 755537521 649 PFKH----QPAEALIWQIGSGE 666
Cdd:cd14092  204 PFQSpsrnESAAEIMKRIKSGD 225
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
520-643 6.10e-09

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: 57.72  E-value: 6.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgisGVVREERRENQl 598
Cdd:cd07832   83 LSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIsSTGVLKIADFGL----ARLFSEEDPRL- 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 599 kLSHD----WlcYLAPEIvreMIPGRDEDQlpfskAADVYAFGTVWYEL 643
Cdd:cd07832  158 -YSHQvatrW--YRAPEL---LYGSRKYDE-----GVDLWAVGCIFAEL 195
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
432-709 6.31e-09

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 58.09  E-value: 6.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 432 LQEWDIPFEQVelgepIGQGRWGRVHRGR-----WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACM 506
Cdd:cd05088    4 LEWNDIKFQDV-----IGEGNFGQVLKARikkdgLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 NPPHLAIITSFCKGRTLHSFVR-------DPK--------TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYd 571
Cdd:cd05088   79 HRGYLYLAIEYAPHGNLLDFLRksrvletDPAfaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 572 nGKVVITDFGLFGISGVVREERRENQLKLSHDWLcylAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARD-WPF 650
Cdd:cd05088  158 -GENYVAKIADFGLSRGQEVYVKKTMGRLPVRWM---AIESLNYSV---------YTTNSDVWSYGVLLWEIVSLGgTPY 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 651 KHQPAEALIWQIGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd05088  225 CGMTCAELYEKLPQG---YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 280
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
448-581 6.67e-09

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: 57.90  E-value: 6.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH--GE-VAIRLLEMDGHnqdhlklFK-KEVMNYRQTRHENVVLFMGAC---MNPPH---LAIITSF 517
Cdd:cd14137   12 IGSGSFGVVYQAKLLetGEvVAIKKVLQDKR-------YKnRELQIMRRLKHPNIVKLKYFFyssGEKKDevyLNLVMEY 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 518 CKGrTLHSFVRD---PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFG 581
Cdd:cd14137   85 MPE-TLYRVIRHyskNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpeTGVLKLCDFG 152
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
506-643 7.07e-09

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: 57.58  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNPPHLAIITSFCKGRTLHSFVRDPKT--SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 582
Cdd:cd14048   85 MDEVYLYIQMQLCRKENLKDWMNRRCTmeSRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSlDDVVKVGDFGL 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 583 FGISGVVREERRENQLKLSHD-------WLCYLAPeivrEMIPGRDedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd14048  165 VTAMDQGEPEQTVLTPMPAYAkhtgqvgTRLYMSP----EQIHGNQ-----YSEKVDIFALGLILFEL 223
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
480-658 8.31e-09

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: 58.17  E-value: 8.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 480 LKLFKKEVM--------------NYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHsFVRDPKTSLDINKTRQIAQE 545
Cdd:cd05593   45 MKILKKEVIiakdevahtltesrVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELF-FHLSRERVFSEDRTRFYGAE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 546 IIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLF--GISGVVreerrenQLKLSHDWLCYLAPEIVremipgRDE 622
Cdd:cd05593  124 IVSALDYLHSGKIVYRDLKLENLMLDkDGHIKITDFGLCkeGITDAA-------TMKTFCGTPEYLAPEVL------EDN 190
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755537521 623 DqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd05593  191 D---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 223
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
444-711 8.32e-09

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: 57.36  E-value: 8.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGRWHG------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd05093    9 LKRELGEGAFGKVFLAECYNlcpeqdKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVR------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYdnGKVVITDFGLFGI 585
Cdd:cd05093   89 MKHGDLNKFLRahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIGDFGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 586 SGVVREE---RRENQLKLSHDWLcylAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELqardWPFKHQPAealiWQI 662
Cdd:cd05093  167 SRDVYSTdyyRVGGHTMLPIRWM---PPESIMYR---------KFTTESDVWSLGVVLWEI----FTYGKQPW----YQL 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 663 GSGEGVR-----RVLASV-SLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPK 711
Cdd:cd05093  227 SNNEVIEcitqgRVLQRPrTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAK 281
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
443-643 9.10e-09

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: 57.16  E-value: 9.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWH--GE-VAIRLLEMDGHN-QDHLKLfkKEVMNYRQ-TRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd07830    2 KVIKQLGDGTFGSVYLARNKetGElVAIKKMKKKFYSwEECMNL--REVKSLRKlNEHPNIVKLKEVFRENDELYFVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgisgvVREERREN 596
Cdd:cd07830   80 MEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVkIADFGL------AREIRSRP 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 597 QLK--LSHDWlcYLAPEIVRemipgRDEDqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07830  154 PYTdyVSTRW--YRAPEILL-----RSTS---YSSPVDIWALGCIMAEL 192
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
443-719 9.44e-09

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: 56.88  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwHGE----VAIRLLEMDGHNQDHLKLF-KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14081    4 RLGKTLGKGQTGLVKLAK-HCVtgqkVAIKIVNKEKLSKESVLMKvEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGIsgvvreERREN 596
Cdd:cd14081   83 VSGGELFDYLVK-KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDeKNNIKIADFGMASL------QPEGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 QLKLSHDWLCYLAPEIVRemipGRDEDqlpfSKAADVYAFGTVWYELQARDWPFkhqpaealiwqigSGEGVRRVLASVS 676
Cdd:cd14081  156 LLETSCGSPHYACPEVIK----GEKYD----GRKADIWSCGVILYALLVGALPF-------------DDDNLRQLLEKVK 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 677 LGKevgeilsacwaFDLqerPSF------SLLMDMLERLPKlnRRLS------HP 719
Cdd:cd14081  215 RGV-----------FHI---PHFispdaqDLLRRMLEVNPE--KRITieeikkHP 253
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
495-666 1.08e-08

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: 57.36  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 495 HENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRqIAQEIIKGMGYLHAKGIVHKDLKSKNVFY---- 570
Cdd:cd14179   61 HPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFSETEASH-IMRKLVSAVSHMHDVGVVHRDLKPENLLFtdes 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 DNGKVVITDFGLfgisgvVREERRENQ-LKLSHDWLCYLAPEIVREmiPGRDEdqlpfskAADVYAFGTVWYEL------ 643
Cdd:cd14179  140 DNSEIKIIDFGF------ARLKPPDNQpLKTPCFTLHYAAPELLNY--NGYDE-------SCDLWSLGVILYTMlsgqvp 204
                        170       180
                 ....*....|....*....|....
gi 755537521 644 -QARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14179  205 fQCHDKSLTCTSAEEIMKKIKQGD 228
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
475-710 1.09e-08

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: 56.92  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 475 HNQDHLKLFKKEVMNYRQTRHENVVLFMGACM----NPPHLA-IITSFCKGRTLHSFV---RDPKTSLDINKTRQIAQEI 546
Cdd:cd13986   36 HSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkeaGGKKEVyLLLPYYKRGSLQDEIerrLVKGTFFPEDRILHIFLGI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 547 IKGMGYLHA---KGIVHKDLKSKNV-FYDNGKVVITDFGLFGISGVVREERRENQLKlsHDW------LCYLAPEI--VR 614
Cdd:cd13986  116 CRGLKAMHEpelVPYAHRDIKPGNVlLSEDDEPILMDLGSMNPARIEIEGRREALAL--QDWaaehctMPYRAPELfdVK 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 615 emiPGRDEDQlpfskAADVYAFGTVWYELQARDWPFK--HQPAEALIWQIGSGEGVRRVLASVSLgkEVGEILSACWAFD 692
Cdd:cd13986  194 ---SHCTIDE-----KTDIWSLGCTLYALMYGESPFEriFQKGDSLALAVLSGNYSFPDNSRYSE--ELHQLVKSMLVVN 263
                        250
                 ....*....|....*...
gi 755537521 693 LQERPSFSLLMDMLERLP 710
Cdd:cd13986  264 PAERPSIDDLLSRVHDLI 281
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
448-650 1.14e-08

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: 57.06  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGE-VAIRLLEM----DGHNQDHLKlFKKEVMnyRQTRHENVVLFMGACMNPPHLAIITSFCKG 520
Cdd:cd05612    9 IGTGTFGRVHlvRDRISEHyYALKVMAIpeviRLKQEQHVH-NEKRVL--KEVSHPFIIRLFWTEHDQRFLYMLMEYVPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvreerrenqLK 599
Cdd:cd05612   86 GELFSYLRNSGR-FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDkEGHIKLTDFGF---------------AK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 600 LSHD--W-LC----YLAPEIVREmiPGRDedqlpfsKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05612  150 KLRDrtWtLCgtpeYLAPEVIQS--KGHN-------KAVDWWALGILIYEMLVGYPPF 198
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
491-666 1.16e-08

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: 57.72  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 491 RQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY 570
Cdd:cd14176   68 RYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 --DNGK---VVITDFGLfgisgvVREERRENQLKLSHdwlCY----LAPEIVREMipgrdedqlPFSKAADVYAFGTVWY 641
Cdd:cd14176  147 vdESGNpesIRICDFGF------AKQLRAENGLLMTP---CYtanfVAPEVLERQ---------GYDAACDIWSLGVLLY 208
                        170       180
                 ....*....|....*....|....*...
gi 755537521 642 ELQARDWPFKHQP---AEALIWQIGSGE 666
Cdd:cd14176  209 TMLTGYTPFANGPddtPEEILARIGSGK 236
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
444-587 1.22e-08

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: 56.75  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGrWH---GE-VAIRLLEMDGHNQDH--LKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSF 517
Cdd:cd14070    6 IGRKLGEGSFAKVREG-LHavtGEkVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMEL 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 518 CKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL---FGISG 587
Cdd:cd14070   85 CPGGNLMHRIYD-KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDeNDNIKLIDFGLsncAGILG 157
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
448-703 1.22e-08

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: 56.69  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGE-VAIRLLEMDGHN-----QDHLKlfkkEVMNYRQTRHENVVLFMGaCMNPPHLA-IITSFC 518
Cdd:cd06607    9 IGHGSFGAVYyaRNKRTSEvVAIKKMSYSGKQstekwQDIIK----EVKFLRQLRHPNTIEYKG-CYLREHTAwLVMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGrTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVreerreNQ 597
Cdd:cd06607   84 LG-SASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLtEPGTVKLADFGSASLVCPA------NS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLSHDWlcyLAPEIVREMipgrDEDQlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGvrRVLASVSL 677
Cdd:cd06607  157 FVGTPYW---MAPEVILAM----DEGQ--YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDS--PTLSSGEW 225
                        250       260
                 ....*....|....*....|....*.
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06607  226 SDDFRNFVDSCLQKIPQDRPSAEDLL 251
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
545-705 1.24e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 57.96  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGI-SGVVREERRENqlklshdwLC----YLAPEIVRemip 618
Cdd:PTZ00283 151 QVLLAVHHVHSKHMIHRDIKSANILLcSNGLVKLGDFGFSKMyAATVSDDVGRT--------FCgtpyYVAPEIWR---- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 619 grdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGegvRRVLASVSLGKEVGEILSACWAFDLQERPS 698
Cdd:PTZ00283 219 -----RKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAG---RYDPLPPSISPEMQEIVTALLSSDPKRRPS 290

                 ....*..
gi 755537521 699 FSLLMDM 705
Cdd:PTZ00283 291 SSKLLNM 297
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
508-651 1.52e-08

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: 56.77  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 508 PPHLAIITSFCKGRTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgi 585
Cdd:cd05577   65 KDKLCLVLTLMNGGDLKYHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDhGHVRISDLGL--- 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 586 sgvVREERRENQLKLSHDWLCYLAPEIVREmipgrdedQLPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd05577  142 ---AVEFKGGKKIKGRVGTHGYMAPEVLQK--------EVAYDFSVDWFALGCMLYEMIAGRSPFR 196
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
440-581 1.55e-08

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: 56.66  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRwHGE----VAI-RLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCR-HKEtgqiVAIkKFLESE-DDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 515 TSFCKGRTLHSFVRDPkTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFG 581
Cdd:cd07846   79 FEFVDHTVLDDLEKYP-NGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVkLCDFG 145
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
443-707 1.59e-08

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: 56.34  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHR-GRWHGEVAIRLLEMDGHNQDHlklFKKEVMNYRQTR----HENVVLFMGACMN--------PP 509
Cdd:cd13975    3 KLGRELGRGQYGVVYAcDSWGGHFPCALKSVVPPDDKH---WNDLALEFHYTRslpkHERIVSLHGSVIDysygggssIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFckGRTLHSFVrdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFG---- 584
Cdd:cd13975   80 VLLIMERL--HRDLYTGI---KAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDkKNRAKITDLGFCKpeam 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 585 ISGVVREERrenqlklshdwlCYLAPeivrEMIPGRdedqlpFSKAADVYAFGTV-WYELQAR---DWPFKHQPAEALIW 660
Cdd:cd13975  155 MSGSIVGTP------------IHMAP----ELFSGK------YDNSVDVYAFGILfWYLCAGHvklPEAFEQCASKDHLW 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 661 Q-IGSGEGVRRVlasVSLGKEVGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd13975  213 NnVRKGVRPERL---PVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQ 257
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
486-645 1.72e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 57.19  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 486 EVMNYRQTRHENVV-----LFMGA--CMNPPHLAiitsfckgRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGI 558
Cdd:PHA03209 107 EAMLLQNVNHPSVIrmkdtLVSGAitCMVLPHYS--------SDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRI 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 559 VHKDLKSKNVFYDN-GKVVITDFG----------LFGISGVVREErrenqlklshdwlcylAPEIVremipGRDEdqlpF 627
Cdd:PHA03209 179 IHRDVKTENIFINDvDQVCIGDLGaaqfpvvapaFLGLAGTVETN----------------APEVL-----ARDK----Y 233
                        170
                 ....*....|....*...
gi 755537521 628 SKAADVYAFGTVWYELQA 645
Cdd:PHA03209 234 NSKADIWSAGIVLFEMLA 251
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
444-650 2.17e-08

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: 56.02  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVVlfmgacmnppHLAIITSFCK 519
Cdd:cd14164    4 LGTTIGEGSFSKVKLAtsqKYCCKVAIKIVDRRRASPDFVqKFLPRELSILRRVNHPNIV----------QMFECIEVAN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GR---TLHSFVRDPKTSLDINK------TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY--DNGKVVITDFGlFGisgv 588
Cdd:cd14164   74 GRlyiVMEAAATDLLQKIQEVHhipkdlARDMFAQMVGAVNYLHDMNIVHRDLKCENILLsaDDRKIKIADFG-FA---- 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 589 vreERRENQLKLSHDWL---CYLAPeivrEMIPGRDEDqlpfSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14164  149 ---RFVEDYPELSTTFCgsrAYTPP----EVILGTPYD----PKKYDVWSLGVVLYVMVTGTMPF 202
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
465-655 2.20e-08

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: 56.53  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 465 VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCkgrtlhsfvrDPKTSLDINKT----- 539
Cdd:cd08216   28 VAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLM----------AYGSCRDLLKThfpeg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 540 ------RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITdfGLFGISGVVREERRenqLKLSHDW-------L 605
Cdd:cd08216   98 lpelaiAFILRDVLNALEYIHSKGYIHRSVKASHILISgDGKVVLS--GLRYAYSMVKHGKR---QRVVHDFpksseknL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 606 CYLAPEIVREMIPGRDEDqlpfskaADVYAFGTVWYELQARDWPFKHQPA 655
Cdd:cd08216  173 PWLSPEVLQQNLLGYNEK-------SDIYSVGITACELANGVVPFSDMPA 215
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
443-653 2.23e-08

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: 55.60  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRwH----GEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14072    3 RLLKTIGKGNFAKVKLAR-HvltgREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQ 597
Cdd:cd14072   82 SGGEVFDYLV-AHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDaDMNIKIADFGF------SNEFTPGNK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 598 LklshDWLCYLAPEIVREMIPGRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14072  155 L----DTFCGSPPYAAPELFQGKKYD----GPEVDVWSLGVILYTLVSGSLPFDGQ 202
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
435-582 2.34e-08

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: 56.53  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELgEPIGQGRWGRVHRGRWHG---EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHL 511
Cdd:cd07851   11 WEVPDRYQNL-SPVGSGAYGQVCSAFDTKtgrKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSL 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 512 A------IITSFCkGRTLHSFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITDFGL 582
Cdd:cd07851   90 EdfqdvyLVTHLM-GADLNNIVKCQKLSDD--HIQFLVYQILRGLKYIHSAGIIHRDLKPSNLaVNEDCELKILDFGL 164
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
543-662 3.00e-08

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: 56.16  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFG---ISGVVREErrenqlklshdwLC----YLAPEIVR 614
Cdd:cd05615  117 AAEISVGLFFLHKKGIIYRDLKLDNVMLDsEGHIKIADFGMCKehmVEGVTTRT------------FCgtpdYIAPEIIA 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 615 EMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05615  185 YQ---------PYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSI 223
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
439-666 3.06e-08

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: 55.87  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRVHRGRwHGEVAIRLlEMDGHNQDHLKLFK--KEVMNYRQ--TRHEN--VVLFMGACMNPPHLA 512
Cdd:cd05609    2 FETIKL---ISNGAYGAVYLVR-HRETRQRF-AMKKINKQNLILRNqiQQVFVERDilTFAENpfVVSMYCSFETKRHLC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGI------ 585
Cdd:cd05609   77 MVMEYVEGGDCATLLKN-IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSmGHIKLTDFGLSKIglmslt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 586 ----SGVVREERRENQLKLSHDWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQ 661
Cdd:cd05609  156 tnlyEGHIEKDTREFLDKQVCGTPEYIAPEVIL---------RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQ 226

                 ....*
gi 755537521 662 IGSGE 666
Cdd:cd05609  227 VISDE 231
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
507-658 3.80e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 55.25  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 NPPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK--VVITDFGLFG 584
Cdd:PHA03390  80 TLKGHVLIMDYIKDGDLFDLLKK-EGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKdrIYLCDYGLCK 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 585 ISGVvreerrenqlKLSHD-WLCYLAPE-IVREmipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:PHA03390 159 IIGT----------PSCYDgTLDYFSPEkIKGH----------NYDVSFDWWAVGVLTYELLTGKHPFKEDEDEEL 214
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
448-698 3.87e-08

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: 55.29  E-value: 3.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH-----GEVAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd05042    3 IGNGWFGKVLLGEIYsgtsvAQVVVKELKASANPKEQDT-FLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSL----DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLfGISGvVREERRENQ 597
Cdd:cd05042   82 LKAYLRSEREHErgdsDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDlTVKIGDYGL-AHSR-YKEDYIETD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 598 LKLshdW--LCYLAPEIVREmIPGR--DEDQlpfSKAADVYAFG-TVW--YELQARdwPFKHQPAEALIWQIGSGEGVR- 669
Cdd:cd05042  160 DKL---WfpLRWTAPELVTE-FHDRllVVDQ---TKYSNIWSLGvTLWelFENGAQ--PYSNLSDLDVLAQVVREQDTKl 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 755537521 670 -RVLASVSLGKEVGEILSACWaFDLQERPS 698
Cdd:cd05042  231 pKPQLELPYSDRWYEVLQFCW-LSPEQRPA 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
543-654 4.17e-08

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: 55.49  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvreERRENqlklSHDW-LC----YLAPEIvrem 616
Cdd:cd14209  107 AAQIVLAFEYLHSLDLIYRDLKPENLLIDqQGYIKVTDFGF---------AKRVK----GRTWtLCgtpeYLAPEI---- 169
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755537521 617 IPGRdedqlPFSKAADVYAFGTVWYELQARDWPF-KHQP 654
Cdd:cd14209  170 ILSK-----GYNKAVDWWALGVLIYEMAAGYPPFfADQP 203
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
431-643 4.20e-08

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: 55.73  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQE-----WDIPFEQVELgEPIGQGRWGRVHR---GRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM 502
Cdd:cd07880    2 YRQEvnktiWEVPDRYRDL-KQVGSGAYGTVCSaldRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 503 GACMNPPHLAIITSF-----CKGRTLHSFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVV 576
Cdd:cd07880   81 DVFTPDLSLDRFHDFylvmpFMGTDLGKLMKHEKLSED--RIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLaVNEDCELK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 577 ITDFGLfgisgvVREERRENQLKLSHDWlcYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd07880  159 ILDFGL------ARQTDSEMTGYVVTRW--YRAPEVIL--------NWMHYTQTVDIWSVGCIMAEM 209
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
448-696 4.78e-08

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: 55.08  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG----RWHgEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFM----GACMNPPHLAIITSFCK 519
Cdd:cd14032    9 LGRGSFKTVYKGldteTWV-EVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYdfweSCAKGKRCIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKG--IVHKDLKSKNVFYD--NGKVVITDFGLFGIsgvvreeRRE 595
Cdd:cd14032   88 SGTLKTYLKRFKV-MKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLATL-------KRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDWLCYLAPEIVREMipgrdedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGeGVRRVLASV 675
Cdd:cd14032  160 SFAKSVIGTPEFMAPEMYEEH----------YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTC-GIKPASFEK 228
                        250       260
                 ....*....|....*....|.
gi 755537521 676 SLGKEVGEILSACWAFDLQER 696
Cdd:cd14032  229 VTDPEIKEIIGECICKNKEER 249
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
440-653 4.79e-08

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: 55.04  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHR--GRWHG-EVAIRLLEMDG-HNQDHLklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIIT 515
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKEcvERSTGkEFALKIIDKAKcCGKEHL--IENEVSILRRVKHPNIIMLIEEMDTPAELYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGKVVITdFGLFGISGVVree 592
Cdd:cd14184   79 ELVKGGDLFDAITS-STKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvceYPDGTKSLK-LGDFGLATVV--- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 593 rrENQLKLSHDWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14184  154 --EGPLYTVCGTPTYVAPEIIAET---------GYGLKVDIWAAGVITYILLCGFPPFRSE 203
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
484-698 4.92e-08

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: 54.57  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPP--HLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHK 561
Cdd:cd14119   42 KREIQILRRLNHRNVIKLVDVLYNEEkqKLYMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 562 DLKSKNVFYDNGKVV-ITDFGlfgisgvVREerrenQLKL--SHDWLC-------YLAPEIVR--EMIPGRdedqlpfsk 629
Cdd:cd14119  122 DIKPGNLLLTTDGTLkISDFG-------VAE-----ALDLfaEDDTCTtsqgspaFQPPEIANgqDSFSGF--------- 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 630 AADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrrVLASVSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd14119  181 KVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGE----YTIPDDVDPDLQDLLRGMLEKDPEKRFT 245
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
463-651 5.04e-08

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: 54.94  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 463 GEVAIRLLEMDGHNQDHLKLfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKtSLDINKTRQI 542
Cdd:cd14187   37 GKIVPKSLLLKPHQKEKMSM---EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRK-ALTEPEARYY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGVVREERRENQLKLSHDwlcYLAPEIVremipgrd 621
Cdd:cd14187  113 LRQIILGCQYLHRNRVIHRDLKLGNLFLnDDMEVKIGDFGL--ATKVEYDGERKKTLCGTPN---YIAPEVL-------- 179
                        170       180       190
                 ....*....|....*....|....*....|
gi 755537521 622 eDQLPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14187  180 -SKKGHSFEVDIWSIGCIMYTLLVGKPPFE 208
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
484-641 5.32e-08

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: 54.52  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDL 563
Cdd:cd14108   46 RRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELLERITK--RPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 564 KSKNVFYDNGK---VVITDFGlfgisgvvreerreNQLKLSHDWLCY--------LAPEIVremipgrdeDQLPFSKAAD 632
Cdd:cd14108  124 KPENLLMADQKtdqVRICDFG--------------NAQELTPNEPQYckygtpefVAPEIV---------NQSPVSKVTD 180

                 ....*....
gi 755537521 633 VYAFGTVWY 641
Cdd:cd14108  181 IWPVGVIAY 189
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
442-643 5.45e-08

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 55.54  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHLKLFKK------------EVMNYRQTRHENVvlfMGAcm 506
Cdd:PTZ00024  11 IQKGAHLGEGTYGKVEKAydtLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENI---MGL-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 npphlaiITSFCKG-------RTLHSFVR---DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKV 575
Cdd:PTZ00024  86 -------VDVYVEGdfinlvmDIMASDLKkvvDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSkGIC 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 576 VITDFGL---FGISGVVREERRENQLKLSHDW------LCYLAPeivrEMIPGRDEdqlpFSKAADVYAFGTVWYEL 643
Cdd:PTZ00024 159 KIADFGLarrYGYPPYSDTLSKDETMQRREEMtskvvtLWYRAP----ELLMGAEK----YHFAVDMWSVGCIFAEL 227
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
544-665 6.57e-08

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: 54.74  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 544 QEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGL-----------FGISGVVreerrenqlklshdwlCYL 608
Cdd:cd14086  107 QQILESVNHCHQNGIVHRDLKPENLLLasksKGAAVKLADFGLaievqgdqqawFGFAGTP----------------GYL 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 609 APEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSG 665
Cdd:cd14086  171 SPEVLRKD---------PYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAG 218
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
510-651 6.97e-08

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: 54.53  E-value: 6.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDPKT-SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSG 587
Cdd:cd05607   76 HLCLVMSLMNGGDLKYHIYNVGErGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDdNGNCRLSDLGL---AV 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 588 VVREERRENQLKLSHDwlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd05607  153 EVKEGKPITQRAGTNG---YMAPEILKEE---------SYSYPVDWFAMGCSIYEMVAGRTPFR 204
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
527-651 8.02e-08

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: 54.29  E-value: 8.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 527 VRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGlfgisgvVREERRENQLKLSHD- 603
Cdd:cd14118  104 MEVPTDNpLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLgDDGHVKIADFG-------VSNEFEGDDALLSSTa 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 755537521 604 -WLCYLAPEIVremIPGRDEdqlpFS-KAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14118  177 gTPAFMAPEAL---SESRKK----FSgKALDIWAMGVTLYCFVFGRCPFE 219
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
491-650 8.18e-08

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: 54.15  E-value: 8.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 491 RQTRHENVVLFMGACMNPPHLAIITSFCKGRTL-HSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV- 568
Cdd:cd14110   54 RRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELlYNLAE--RNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMi 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 569 ----------------FYDNGKVVITD-FGlfgisgvvreerrenqlklshDWLCYLAPEIVREmipgrdEDQLPfskAA 631
Cdd:cd14110  132 iteknllkivdlgnaqPFNQGKVLMTDkKG---------------------DYVETMAPELLEG------QGAGP---QT 181
                        170
                 ....*....|....*....
gi 755537521 632 DVYAFGTVWYELQARDWPF 650
Cdd:cd14110  182 DIWAIGVTAFIMLSADYPV 200
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
446-652 9.22e-08

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: 54.14  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHG--EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHE-NVVLFMGA--CMNPPHLAIITSFckG 520
Cdd:cd14131    7 KQLGKGGSSKVYKVLNPKkkIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDYevTDEDDYLYMVMEC--G 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RT-LHSFV--RDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDfglFGISGVVREER---- 593
Cdd:cd14131   85 EIdLATILkkKRPKP-IDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLID---FGIAKAIQNDTtsiv 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 RENQLKLshdwLCYLAPE-IVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKH 652
Cdd:cd14131  161 RDSQVGT----LNYMSPEaIKDTSASGEGKPKSKIGRPSDVWSLGCILYQMVYGKTPFQH 216
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
199-241 1.05e-07

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 49.00  E-value: 1.05e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755537521   199 HRFSTKSW-LSQVCNVCQKSMIF----GVKCKHCRLKCHNKCTKEAPA 241
Cdd:smart00109   1 HKHVFRTFtKPTFCCVCRKSIWGsfkqGLRCSECKVKCHKKCADKVPK 48
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
448-662 1.20e-07

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: 54.33  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRwhgevairllEMDGHNQDHL---KLFKKEVMNYR-------------QTRHENVVLFMGACMNPPHL 511
Cdd:cd05582    3 LGQGSFGKVFLVR----------KITGPDAGTLyamKVLKKATLKVRdrvrtkmerdilaDVNHPFIVKLHYAFQTEGKL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLhsFVRdpkTSLDINKTRQIAQ----EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgis 586
Cdd:cd05582   73 YLILDFLRGGDL--FTR---LSKEVMFTEEDVKfylaELALALDHLHSLGIIYRDLKPENILLDeDGHIKLTDFGL---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 587 gvVREERRENQLKLShdwLC----YLAPEIVREmipgRDEDQlpfskAADVYAFGTVWYELQARDWPFKHQPAEALIWQI 662
Cdd:cd05582  144 --SKESIDHEKKAYS---FCgtveYMAPEVVNR----RGHTQ-----SADWWSFGVLMFEMLTGSLPFQGKDRKETMTMI 209
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
443-661 1.24e-07

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: 54.06  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRWHG---EVAIRLLEmdghNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14085    6 EIESELGRGATSVVYRCRQKGtqkPYAVKKLK----KTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgiSGVVREErre 595
Cdd:cd14085   82 GGELFDRIVEKGYYSERDAADAVKQ-ILEAVAYLHENGIVHRDLKPENLLYatpaPDAPLKIADFGL---SKIVDQQ--- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 nqlkLSHDWLC----YLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQ 661
Cdd:cd14085  155 ----VTMKTVCgtpgYCAPEILR---------GCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFK 211
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
535-687 1.24e-07

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: 54.04  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 535 DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQLKLShdwLC----YLA 609
Cdd:cd05591   94 DEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDaEGHCKLADFGM------CKEGILNGKTTTT---FCgtpdYIA 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 610 PEIVREmipgrdedqLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEgvrrVLASVSLGKEVGEILSA 687
Cdd:cd05591  165 PEILQE---------LEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDD----VLYPVWLSKEAVSILKA 229
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
446-703 1.31e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 53.41  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGrwhgevaIRLlEMDGHNQDH-----LKLFKKEVMNY-----------RQTRHENVVLFMGACMNPP 509
Cdd:cd05078    5 ESLGQGTFTKIFKG-------IRR-EVGDYGQLHetevlLKVLDKAHRNYsesffeaasmmSQLSHKHLVLNYGVCVCGD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFydngkvvitdfglfgisgVV 589
Cdd:cd05078   77 ENILVQEYVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNIL------------------LI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 590 REERRENQ----LKLSHDW--LCYLAPEIVREMIPGRD----EDQLPFSKAADVYAFGTVWYELQARDwpfkHQPAEALI 659
Cdd:cd05078  139 REEDRKTGnppfIKLSDPGisITVLPKDILLERIPWVPpeciENPKNLSLATDKWSFGTTLWEICSGG----DKPLSALD 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 755537521 660 WQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd05078  215 SQRKLQFYEDRHQLPAPKWTELANLINNCMDYEPDHRPSFRAII 258
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
541-665 1.41e-07

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: 53.79  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 541 QIAQEIIKGMGYLHAKGIVHKDLKSKNVFY--DNGK---VVITDFGLfgisgvVREERRENQLKLSHdwlCY----LAPE 611
Cdd:cd14091   98 AVMKTLTKTVEYLHSQGVVHRDLKPSNILYadESGDpesLRICDFGF------AKQLRAENGLLMTP---CYtanfVAPE 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 612 IVREMipGRDedqlpfsKAADVYAFGTVWYELQARDWPFKHQP---AEALIWQIGSG 665
Cdd:cd14091  169 VLKKQ--GYD-------AACDIWSLGVLLYTMLAGYTPFASGPndtPEVILARIGSG 216
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
448-584 1.60e-07

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: 53.16  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRwH----GEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd14071    8 IGKGNFAVVKLAR-HritkTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEI 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 524 HSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlFG 584
Cdd:cd14071   87 FDYLAQ-HGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDaNMNIKIADFG-FS 146
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
448-582 1.66e-07

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: 53.91  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPP--------HLAIITS 516
Cdd:cd07865   20 IGQGTFGEVFkaRHRKTGQiVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKAtpynrykgSIYLVFE 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 517 FCKgRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 582
Cdd:cd07865  100 FCE-HDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITkDGVLKLADFGL 165
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
539-650 1.82e-07

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: 53.39  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 539 TRQIAQeIIKGMGYLHAKGIVHKDLKSKNVF----YDNGKVVITDFGL---FGISGVVREERRENQlklshdwlcYLAPE 611
Cdd:cd14198  113 IRLIRQ-ILEGVYYLHQNNIVHLDLKPQNILlssiYPLGDIKIVDFGMsrkIGHACELREIMGTPE---------YLAPE 182
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755537521 612 IVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14198  183 IL---------NYDPITTATDMWNIGVIAYMLLTHESPF 212
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
458-655 1.83e-07

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 53.79  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 458 RGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFV----RDPKT 532
Cdd:cd08227   20 RYKPTGEyVTVRRINLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLIcthfMDGMS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 533 SLDInktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITdfGLFGISGVVREERRenqLKLSHDW------- 604
Cdd:cd08227  100 ELAI---AYILQGVLKALDYIHHMGYVHRSVKASHILISvDGKVYLS--GLRSNLSMINHGQR---LRVVHDFpkysvkv 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 605 LCYLAPEIVREMIPGRDedqlpfsKAADVYAFGTVWYELQARDWPFKHQPA 655
Cdd:cd08227  172 LPWLSPEVLQQNLQGYD-------AKSDIYSVGITACELANGHVPFKDMPA 215
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
199-240 1.92e-07

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 48.28  E-value: 1.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 199 HRFSTKSWLS-QVCNVCQKSMIF----GVKCKHCRLKCHNKCTKEAP 240
Cdd:cd00029    1 HRFVPTTFSSpTFCDVCGKLIWGlfkqGLKCSDCGLVCHKKCLDKAP 47
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
463-581 1.96e-07

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: 50.52  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 463 GEVAIRLleMDGHNQDHLKLFKKEVMNYRQTR-HE-NVVLFMGACMNPPHLAIITSFCKGRTLHSFVRdpKTSLDINKTR 540
Cdd:cd13968   19 IGVAVKI--GDDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTLIAYTQ--EEELDEKDVE 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755537521 541 QIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFG 581
Cdd:cd13968   95 SIMYQLAECMRLLHSFHLIHRDLNNDNILLsEDGNVKLIDFG 136
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
431-702 2.08e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 53.03  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQEwdipfeqvelgepIGQGRWGRVHRGRWH-----GEVAIRLLEMDGHNQDHLKlFKKEVMNYRQTRHENVVLFMGAC 505
Cdd:cd14206    1 YLQE-------------IGNGWFGKVILGEIFsdytpAQVVVKELRVSAGPLEQRK-FISEAQPYRSLQHPNILQCLGLC 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNPPHLAIITSFCKGRTLHSFVRDPKT---------SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV 576
Cdd:cd14206   67 TETIPFLLIMEFCQLGDLKRYLRAQRKadgmtpdlpTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 577 -ITDFGLfgisgvvREERRENQLKLSHD--W--LCYLAPEIVREMipgRDE----DQlpfSKAADVYAFG-TVWYELQAR 646
Cdd:cd14206  147 rIGDYGL-------SHNNYKEDYYLTPDrlWipLRWVAPELLDEL---HGNlivvDQ---SKESNVWSLGvTIWELFEFG 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 647 DWPFKHQPAEALIWQIGSGEGVRrvLASVSLGKEVG----EILSACWaFDLQERPSFSLL 702
Cdd:cd14206  214 AQPYRHLSDEEVLTFVVREQQMK--LAKPRLKLPYAdywyEIMQSCW-LPPSQRPSVEEL 270
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
465-651 2.40e-07

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: 52.73  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 465 VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQ 544
Cdd:cd14075   30 VAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELYTKISTEGKLSESEAKPLFAQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 eIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVREERRENQlklshdwLC----YLAPEIVRemipgr 620
Cdd:cd14075  110 -IVSAVKHMHENNIIHRDLKAENVFYASNNCV--KVGDFGFSTHAKRGETLNT-------FCgsppYAAPELFK------ 173
                        170       180       190
                 ....*....|....*....|....*....|.
gi 755537521 621 deDQLPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14075  174 --DEHYIGIYVDIWALGVLLYFMVTGVMPFR 202
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
537-696 2.45e-07

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: 53.49  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 537 NKTRQIAQEIIKGMGYLHA-KGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQlklSHDWLC----YLAP 610
Cdd:cd05594  125 DRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDkDGHIKITDFGL------CKEGIKDGA---TMKTFCgtpeYLAP 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 611 EIVRemipgrDEDqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALiWQIGSGEGVRrvlASVSLGKEVGEILSACWA 690
Cdd:cd05594  196 EVLE------DND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL-FELILMEEIR---FPRTLSPEAKSLLSGLLK 262

                 ....*.
gi 755537521 691 FDLQER 696
Cdd:cd05594  263 KDPKQR 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
543-651 2.64e-07

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: 52.96  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgVVREERRENQLKLSHDWLCYLAPEIVremipgRD 621
Cdd:cd05608  111 TAQIISGLEHLHQRRIIYRDLKPENVLLDDdGNVRISDLGL-----AVELKDGQTKTKGYAGTPGFMAPELL------LG 179
                         90       100       110
                 ....*....|....*....|....*....|
gi 755537521 622 EDqlpFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd05608  180 EE---YDYSVDYFTLGVTLYEMIAARGPFR 206
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
446-654 2.73e-07

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: 53.04  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EP---IGQGRWGRVHRGR--WHGE-VAIRLLEMDgHNQDHLKLFK-KEVMNYR---QTRHENVVLFMGACMNP---PHLA 512
Cdd:cd07863    3 EPvaeIGVGAYGTVYKARdpHSGHfVALKSVRVQ-TNEDGLPLSTvREVALLKrleAFDHPNIVRLMDVCATSrtdRETK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IITSFCK-GRTLHSFV-RDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISGVv 589
Cdd:cd07863   82 VTLVFEHvDQDLRTYLdKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSgGQVKLADFGLARIYSC- 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 590 reerrenQLKLSH--DWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELqardwpFKHQP 654
Cdd:cd07863  161 -------QMALTPvvVTLWYRAPEVLL---------QSTYATPVDMWSVGCIFAEM------FRRKP 205
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
446-711 3.08e-07

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: 52.39  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRWHGEVAIRLLEMdghnqdhlkLFKKEVM---------------------NYRQTRHENVVLFMGA 504
Cdd:cd14004    6 KEMGEGAYGQVNLAIYKSKGKEVVIKF---------IFKERILvdtwvrdrklgtvpleihildTLNKRSHPNIVKLLDF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSfCKGRTLHSFVR-DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGl 582
Cdd:cd14004   77 FEDDEFYYLVME-KHGSGMDLFDFiERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDgNGTIKLIDFG- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 583 fgiSGVVREERRENQLKLSHDwlcYLAPEIVR-EMIPGrdedqlpfsKAADVYAFGTVWYELQARDWPFkhqpaealiwq 661
Cdd:cd14004  155 ---SAAYIKSGPFDTFVGTID---YAAPEVLRgNPYGG---------KEQDIWALGVLLYTLVFKENPF----------- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 662 igsgegvrrvlasvslgKEVGEILSACWAFD-LQERPSFSLLMDMLERLPK 711
Cdd:cd14004  209 -----------------YNIEEILEADLRIPyAVSEDLIDLISRMLNRDVG 242
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
448-643 3.59e-07

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: 52.52  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHG-EVAIRLLEMDGH-NQDHLK-LFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC-KGRT- 522
Cdd:cd14159    1 IGEGGFGCVYQAVMRNtEYAVKRLKEDSElDWSVVKnSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLpNGSLe 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 --LHSFVRDPKtsLDINKTRQIAQEIIKGMGYLH--AKGIVHKDLKSKNVFYD---NGKvvITDFGLfgisgvVREERRE 595
Cdd:cd14159   81 drLHCQVSCPC--LSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDaalNPK--LGDFGL------ARFSRRP 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 596 NQLKLS---------HDWLCYLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd14159  151 KQPGMSstlartqtvRGTLAYLPEEYVKT---GT------LSVEIDVYSFGVVLLEL 198
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
435-643 4.22e-07

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: 52.60  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPFEQVELgEPIGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFmgacmnpphL 511
Cdd:cd07879   11 WELPERYTSL-KQVGSGAYGSVCSAidkRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGL---------L 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 AIITSFCKGRTLHSF-VRDPKTSLDINKTRQ----------IAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVITD 579
Cdd:cd07879   81 DVFTSAVSGDEFQDFyLVMPYMQTDLQKIMGhplsedkvqyLVYQMLCGLKYIHSAGIIHRDLKPGNLaVNEDCELKILD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 580 FGLfgisgvVREERRENQLKLSHDWlcYLAPEIVRemipgrdeDQLPFSKAADVYAFGTVWYEL 643
Cdd:cd07879  161 FGL------ARHADAEMTGYVVTRW--YRAPEVIL--------NWMHYNQTVDIWSVGCIMAEM 208
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
448-705 4.31e-07

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: 51.96  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVH--RGRWHGEV-AIRLLEMDGHnqdhLKLFKKEVMNY---RQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd06605    9 LGEGNGGVVSkvRHRPSGQImAVKVIRLEID----EALQKQILRELdvlHKCNSPYIVGFYGAFYSEGDISICMEYMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAK-GIVHKDLKSKNVFYDN-GKVVITDfglFGISGVVreerrENQLK 599
Cdd:cd06605   85 SLDKILKEVGR-IPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSrGQVKLCD---FGVSGQL-----VDSLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 600 LShDWLC--YLAPeivrEMIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEA------LIWQIGSGEGVRrv 671
Cdd:cd06605  156 KT-FVGTrsYMAP----ERISGGK-----YTVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmifeLLSYIVDEPPPL-- 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 755537521 672 LASVSLGKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd06605  224 LPSGKFSPDFQDFVSQCLQKDPTERPSYKELMEH 257
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
448-697 6.12e-07

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: 51.89  E-value: 6.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRV-HRGRWHGE-VAIRLLEM-------DGHNQDHLKL------------FKKEVMNYRQTRHENVVLFMGACM 506
Cdd:cd14067    1 LGQGGSGTViYRARYQGQpVAVKRFHIkkckkrtDGSADTMLKHlraadamknfseFRQEASMLHSLQHPCIVYLIGISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 NP--------PHLAIITSFCKGRTLHSFVrdpktSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF---YDNGKV 575
Cdd:cd14067   81 HPlcfalelaPLGSLNTVLEENHKGSSFM-----PLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 576 VITDFGLFGISgvvREERRENQLKLSHDwLCYLAPEIVREMIpgrdedqlpFSKAADVYAFGTVWYELQARDWPF--KHQ 653
Cdd:cd14067  156 INIKLSDYGIS---RQSFHEGALGVEGT-PGYQAPEIRPRIV---------YDEKVDMFSYGMVLYELLSGQRPSlgHHQ 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 654 paealiWQIGS--GEGVRRVLAS---VSLgKEVGEILSACWAFDLQERP 697
Cdd:cd14067  223 ------LQIAKklSKGIRPVLGQpeeVQF-FRLQALMMECWDTKPEKRP 264
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
544-698 6.40e-07

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: 51.43  E-value: 6.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 544 QEIIKGMGYLHAKGIVHKDLKSKN---VFYDNGKVVITDFGLfgisgvvreerRENQLKLSHDWLCYLAPEIVREMIPgr 620
Cdd:cd14107  105 QQVLEGIGYLHGMNILHLDIKPDNilmVSPTREDIKICDFGF-----------AQEITPSEHQFSKYGSPEFVAPEIV-- 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 621 deDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd14107  172 --HQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQPDPEKRPS 247
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
439-650 6.50e-07

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: 51.43  E-value: 6.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPIGQGRWGRVHR--GRWHGEVAIRLLEMDGHNQDHlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRctERATGNNFAAKFIMTPHESDK-ETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK---VVITDFGLfgisgVVREER 593
Cdd:cd14114   80 FLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRsneVKLIDFGL-----ATHLDP 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 594 RENqLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14114  155 KES-VKVTTGTAEFAAPEIV---------EREPVGFYTDMWAVGVLSYVLLSGLSPF 201
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
438-704 6.96e-07

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: 51.53  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRVHR---GRWHGEVAIRLLE----MDGHNQDHLKLFKKevmnyrQTRHENVVLFMGACMNPPH 510
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYKvtnKKDGSLAAVKILDpisdVDEEIEAEYNILRS------LPNHPNVVKFYGMFYKADQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 -----LAIITSFCKGRTLHSFVRD---PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDfg 581
Cdd:cd06639   94 yvggqLWLVLELCNGGSVTELVKGllkCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTtEGGVKLVD-- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 582 lFGISGVVREER-RENQLKLSHDWlcyLAPEIVremipgRDEDQLPFSKAA--DVYAFGTVWYELQARDWP-FKHQPAEA 657
Cdd:cd06639  172 -FGVSAQLTSARlRRNTSVGTPFW---MAPEVI------ACEQQYDYSYDArcDVWSLGITAIELADGDPPlFDMHPVKA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 658 LiWQIGSGEGvRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd06639  242 L-FKIPRNPP-PTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLE 286
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
440-666 7.00e-07

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: 51.53  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGRWHG---EVAIRLLEmDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERStgrEYALKIIN-KSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHsfvrDPKTSLDINKTRQIA---QEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVitDFGLFGISGVV 589
Cdd:cd14183   85 LVKGGDLF----DAITSTNKYTERDASgmlYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSL--KLGDFGLATVV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 590 reerrENQLKLSHDWLCYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFK--HQPAEALIWQIGSGE 666
Cdd:cd14183  159 -----DGPLYTVCGTPTYVAPEIIAET---------GYGLKVDIWAAGVITYILLCGFPPFRgsGDDQEVLFDQILMGQ 223
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
443-651 7.31e-07

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: 51.40  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGRW---HGEVAIRLL---EMDGHNQDHLklFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:cd14117    9 DIGRPLGKGKFGNVYLAREkqsKFIVALKVLfksQIEKEGVEHQ--LRREIEIQSHLRHPNILRLYNYFHDRKRIYLILE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGISGVVREERRE 595
Cdd:cd14117   87 YAPRGELYKELQKHGR-FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGyKGELKIADFGWSVHAPSLRRRTMC 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 596 NQLKlshdwlcYLAPeivrEMIPGRDEDQlpfskAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14117  166 GTLD-------YLPP----EMIEGRTHDE-----KVDLWCIGVLCYELLVGMPPFE 205
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
540-650 7.61e-07

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: 51.65  E-value: 7.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 540 RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQLKLShdwLC----YLAPEIVR 614
Cdd:cd05588   99 RFYSAEISLALNFLHEKGIIYRDLKLDNVLLDsEGHIKLTDYGM------CKEGLRPGDTTST---FCgtpnYIAPEILR 169
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755537521 615 emipGRDEDqlpFSkaADVYAFGTVWYELQARDWPF 650
Cdd:cd05588  170 ----GEDYG---FS--VDWWALGVLMFEMLAGRSPF 196
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
439-582 7.66e-07

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: 51.55  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELGEPIGQGRWGRVHRGRwHGE----VAIRLLEMdgHNQD---------HLKLFKKevmnyrqTRHENVVlfmgac 505
Cdd:cd07866    7 LRDYEILGKLGEGTFGEVYKAR-QIKtgrvVALKKILM--HNEKdgfpitalrEIKILKK-------LKHPNVV------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 mNPPHLAIITSFCKGRTLHSF--------------VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD 571
Cdd:cd07866   71 -PLIDMAVERPDKSKRKRGSVymvtpymdhdlsglLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILID 149
                        170
                 ....*....|..
gi 755537521 572 N-GKVVITDFGL 582
Cdd:cd07866  150 NqGILKIADFGL 161
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
485-641 9.15e-07

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: 51.12  E-value: 9.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 485 KEVMNYRQTRHENVVLFMGACMNPP--HLAIITSFCKGRTLHSFVRDPKTSLDinKTRQIAQEIIKGMGYLHAKGIVHKD 562
Cdd:cd14199   74 QEIAILKKLDHPNVVKLVEVLDDPSedHLYMVFELVKQGPVMEVPTLKPLSED--QARFYFQDLIKGIEYLHYQKIIHRD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 563 LKSKNVFY-DNGKVVITDFGLfgisgvvreerrENQLKLSHDWL-------CYLAPEIVremipgrDEDQLPFS-KAADV 633
Cdd:cd14199  152 VKPSNLLVgEDGHIKIADFGV------------SNEFEGSDALLtntvgtpAFMAPETL-------SETRKIFSgKALDV 212

                 ....*...
gi 755537521 634 YAFGTVWY 641
Cdd:cd14199  213 WAMGVTLY 220
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
446-692 1.19e-06

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: 50.77  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVhrgrwhgevaIRLLEMDGHNQDHLKLFK----KEVMNYRQT-------RHENVVLFMGACMNPPHLAII 514
Cdd:cd14191    8 ERLGSGKFGQV----------FRLVEKKTKKVWAGKFFKaysaKEKENIRQEisimnclHHPKLVQCVDAFEEKANIVMV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN---GKVVITDFGLfgisgvVRE 591
Cdd:cd14191   78 LEMVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktgTKIKLIDFGL------ARR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 592 ERRENQLKLSHDWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPFKhqpaealiwqigsGEGVRRV 671
Cdd:cd14191  152 LENAGSLKVLFGTPEFVAPEVI---------NYEPIGYATDMWSIGVICYILVSGLSPFM-------------GDNDNET 209
                        250       260
                 ....*....|....*....|.
gi 755537521 672 LASVSlgkevgeilSACWAFD 692
Cdd:cd14191  210 LANVT---------SATWDFD 221
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
537-641 1.23e-06

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: 50.72  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 537 NKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGisgvvREERRENQLKLSHDWLCYLAPEIVre 615
Cdd:cd14200  124 DQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLgDDGHVKIADFGVSN-----QFEGNDALLSSTAGTPAFMAPETL-- 196
                         90       100
                 ....*....|....*....|....*.
gi 755537521 616 mipgRDEDQLPFSKAADVYAFGTVWY 641
Cdd:cd14200  197 ----SDSGQSFSGKALDVWAMGVTLY 218
PRK14879 PRK14879
Kae1-associated kinase Bud32;
445-591 1.23e-06

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 49.91  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHGEVAI---------RLLEMDghnqdhlklfkkEVMNYRQTRHENVVLFMG--ACMNPPHL-- 511
Cdd:PRK14879   1 MKLIKRGAEAEIYLGDFLGIKAVikwripkryRHPELD------------ERIRRERTRREARIMSRArkAGVNVPAVyf 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 512 ------AIITSFCKGRTLHSFVRDPKTSLdinktRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGI 585
Cdd:PRK14879  69 vdpenfIIVMEYIEGEPLKDLINSNGMEE-----LELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLAEF 143

                 ....*.
gi 755537521 586 SGVVRE 591
Cdd:PRK14879 144 SKDLED 149
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
545-651 1.41e-06

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: 50.87  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLF-GISgvvrEERRENQLKLSH----DWlcYLAPEIvreMIP 618
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNaDCELKICDFGLArGFS----ENPGENAGFMTEyvatRW--YRAPEI---MLS 183
                         90       100       110
                 ....*....|....*....|....*....|...
gi 755537521 619 GRdedqlPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd07857  184 FQ-----SYTKAIDVWSVGCILAELLGRKPVFK 211
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
446-643 1.63e-06

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: 50.65  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd07856   16 QPVGMGAFGLVCSARdqlTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVrdpkTSLDINKtrQIAQ----EIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGIsgvvreerRENQ 597
Cdd:cd07856   96 LHRLL----TSRPLEK--QFIQyflyQILRGLKYVHSAGVIHRDLKPSNILVnENCDLKICDFGLARI--------QDPQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 598 LKLSHDWLCYLAPEIvreMIPGRDEDQlpfskAADVYAFGTVWYEL 643
Cdd:cd07856  162 MTGYVSTRYYRAPEI---MLTWQKYDV-----EVDIWSAGCIFAEM 199
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
484-698 1.67e-06

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: 50.12  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDP---KTSLDINKTRQIaqeiIKGMGYLHAKGIVH 560
Cdd:cd06630   51 REEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYgafSENVIINYTLQI----LRGLAYLHDNQIIH 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 561 KDLKSKNVFYDN-GKVV-ITDFGLFG--ISGVVREERRENQLKLShdwLCYLAPEIVRemipGRdedqlPFSKAADVYAF 636
Cdd:cd06630  127 RDLKGANLLVDStGQRLrIADFGAAArlASKGTGAGEFQGQLLGT---IAFMAPEVLR----GE-----QYGRSCDVWSV 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 637 GTVWYELQARDWPF---KHQPAEALIWQIGSGEGVRRVLASVSLGkeVGEILSACWAFDLQERPS 698
Cdd:cd06630  195 GCVIIEMATAKPPWnaeKISNHLALIFKIASATTPPPIPEHLSPG--LRDVTLRCLELQPEDRPP 257
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
494-650 1.69e-06

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: 50.01  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 494 RHENVVLFMGACMnpphlaiitsfcKGRTLHSFVRDPKTSLDINKTRQ-----------IAQEIIKGMGYLHAKGIVHKD 562
Cdd:cd13995   54 RHENIAELYGALL------------WEETVHLFMEAGEGGSVLEKLEScgpmrefeiiwVTKHVLKGLDFLHSKNIIHHD 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 563 LKSKNVFYDNGKVVITDFGL---FGISGVVREERRENQLklshdwlcYLAPEIVreMIPGRdedqlpfSKAADVYAFGTV 639
Cdd:cd13995  122 IKPSNIVFMSTKAVLVDFGLsvqMTEDVYVPKDLRGTEI--------YMSPEVI--LCRGH-------NTKADIYSLGAT 184
                        170
                 ....*....|.
gi 755537521 640 WYELQARDWPF 650
Cdd:cd13995  185 IIHMQTGSPPW 195
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
446-645 1.69e-06

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: 50.76  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKgRT 522
Cdd:cd07872   12 EKLGEGTYATVFKGRsklTENLVALKEIRLE-HEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD-KD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVREERRENQLKLs 601
Cdd:cd07872   90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLInERGELKLADFGLARAKSVPTKTYSNEVVTL- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755537521 602 hdWlcYLAPEIvremIPGRDEdqlpFSKAADVYAFGTVWYELQA 645
Cdd:cd07872  169 --W--YRPPDV----LLGSSE----YSTQIDMWGVGCIFFEMAS 200
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
446-643 2.10e-06

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: 50.39  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKgRT 522
Cdd:cd07873    8 DKLGEGTYATVYKGRsklTDNLVALKEIRLE-HEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD-KD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVREERRENQLKLs 601
Cdd:cd07873   86 LKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLInERGELKLADFGLARAKSIPTKTYSNEVVTL- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755537521 602 hdWlcYLAPEIvremIPGRDEdqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07873  165 --W--YRPPDI----LLGSTD----YSTQIDMWGVGCIFYEM 194
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
475-650 2.33e-06

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: 50.40  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 475 HNQDHLKLFKKEVMNYRQTRHENVVLFMGACMN-PPHLAIITSFCKGRTLhSFVRDPKTSLDINKTRQIAQEIIKGMGYL 553
Cdd:cd05617   54 HDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQtTSRLFLVIEYVNGGDL-MFHMQRQRKLPEEHARFYAAEICIALNFL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 554 HAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvVREERRENQLKLShdwLC----YLAPEIVRemipGRDedqlpFS 628
Cdd:cd05617  133 HERGIIYRDLKLDNVLLDaDGHIKLTDYGM------CKEGLGPGDTTST---FCgtpnYIAPEILR----GEE-----YG 194
                        170       180
                 ....*....|....*....|..
gi 755537521 629 KAADVYAFGTVWYELQARDWPF 650
Cdd:cd05617  195 FSVDWWALGVLMFEMMAGRSPF 216
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
539-658 3.66e-06

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: 49.22  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 539 TRQIAQEIIKGMG----YLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgisgvVREERRENQLKLSHDWLCYLAP 610
Cdd:cd14172  101 TEREASEIMRDIGtaiqYLHSMNIAHRDVKPENLLYtskeKDAVLKLTDFGF------AKETTVQNALQTPCYTPYYVAP 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 611 EIVremipGRDEdqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEAL 658
Cdd:cd14172  175 EVL-----GPEK----YDKSCDMWSLGVIMYILLCGFPPFYSNTGQAI 213
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
443-651 3.95e-06

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: 49.19  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR--WHGE-VA---IRLLEMDGHN--QDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd08224    3 EIEKKIGKGQFSVVYRARclLDGRlVAlkkVQIFEMMDAKarQDCLK----EIDLLQQLNHPNIIKYLASFIENNELNIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRTLHSFVRDPKTSLDINKTRQI---AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVR 590
Cdd:cd08224   79 LELADAGDLSRLIKHFKKQKRLIPERTIwkyFVQLCSALEHMHSKRIMHRDIKPANVFITaNGVVKLGDLGL---GRFFS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 591 EERRENQLKLSHDWlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd08224  156 SKTTAAHSLVGTPY--YMSPERIREQ---------GYDFKSDIWSLGCLLYEMAALQSPFY 205
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
438-703 4.19e-06

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: 49.24  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 438 PFEQVELGEPIGQGRWGRV---HRGRWHGEVAIRLLE----MDGHNQDHLKLFKKevmnyrQTRHENVVLFMGA-----C 505
Cdd:cd06638   16 PSDTWEIIETIGKGTYGKVfkvLNKKNGSKAAVKILDpihdIDEEIEAEYNILKA------LSDHPNVVKFYGMyykkdV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIA---QEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDfg 581
Cdd:cd06638   90 KNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAyilHEALMGLQHLHVNKTIHRDVKGNNILLTTeGGVKLVD-- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 582 lFGISGVVREER-RENQLKLSHDWlcyLAPEIVremipgRDEDQL--PFSKAADVYAFGTVWYELQARDWPFKH-QPAEA 657
Cdd:cd06638  168 -FGVSAQLTSTRlRRNTSVGTPFW---MAPEVI------ACEQQLdsTYDARCDVWSLGITAIELGDGDPPLADlHPMRA 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 658 LiWQIGSGEGVRrvLASVSL-GKEVGEILSACWAFDLQERPSFSLLM 703
Cdd:cd06638  238 L-FKIPRNPPPT--LHQPELwSNEFNDFIRKCLTKDYEKRPTVSDLL 281
pknD PRK13184
serine/threonine-protein kinase PknD;
542-651 4.31e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 50.54  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 542 IAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisGVVREERRENQLKLSHDWLCYLAPEIVremIPGR 620
Cdd:PRK13184 118 IFHKICATIEYVHSKGVLHRDLKPDNILLGLfGEVVILDWGA----AIFKKLEEEDLLDIDVDERNICYSSMT---IPGK 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755537521 621 ---------DEDQL--PFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:PRK13184 191 ivgtpdymaPERLLgvPASESTDIYALGVILYQMLTLSFPYR 232
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
444-650 5.48e-06

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: 48.62  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVV----LFMgacMNPPHLAIIT 515
Cdd:cd14165    5 LGINLGEGSYAKVksaYSERLKCNVAIKIIDKKKAPDDFVeKFLPRELEILARLNHKSIIktyeIFE---TSDGKVYIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 516 SFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLfgISGVVREERr 594
Cdd:cd14165   82 ELGVQGDLLEFIKL-RGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDfNIKLTDFGF--SKRCLRDEN- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 595 eNQLKLSHDW---LCYLAPEIVrEMIPGRdedqlpfSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14165  158 -GRIVLSKTFcgsAAYAAPEVL-QGIPYD-------PRIYDIWSLGVILYIMVCGSMPY 207
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
410-582 5.67e-06

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 49.05  E-value: 5.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 410 LPSSRRPWRGPISRKASQTSVYLQEwdiPFEQVELGEPIGQGRWGRVHRGRWHG---EVAIRLLeMDGHNQDHLKLFKKE 486
Cdd:PLN00034  47 LPPPSSSSSSSSSSSASGSAPSAAK---SLSELERVNRIGSGAGGTVYKVIHRPtgrLYALKVI-YGNHEDTVRRQICRE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 487 VMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSfvrdpktsLDINKTRQ---IAQEIIKGMGYLHAKGIVHKDL 563
Cdd:PLN00034 123 IEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG--------THIADEQFladVARQILSGIAYLHRRHIVHRDI 194
                        170       180
                 ....*....|....*....|
gi 755537521 564 KSKNVFYDNGK-VVITDFGL 582
Cdd:PLN00034 195 KPSNLLINSAKnVKIADFGV 214
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
483-581 6.54e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 49.31  E-value: 6.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 483 FKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKgRTLHSFVRDP----KTSLDINKTRQIAQEIIKGMGYLHAKGI 558
Cdd:PHA03210 210 LENEILALGRLNHENILKIEEILRSEANTYMITQKYD-FDLYSFMYDEafdwKDRPLLKQTRAIMKQLLCAVEYIHDKKL 288
                         90       100
                 ....*....|....*....|....
gi 755537521 559 VHKDLKSKNVFYD-NGKVVITDFG 581
Cdd:PHA03210 289 IHRDIKLENIFLNcDGKIVLGDFG 312
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
492-706 6.61e-06

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 48.37  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 492 QTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF-- 569
Cdd:cd05076   71 QVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGNVCAKNILla 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 570 ---YDNGK---VVITDFGLfGISGVVREERRENqlklshdwLCYLAPEIVREMIpgrdedqlPFSKAADVYAFGTVWYE- 642
Cdd:cd05076  151 rlgLEEGTspfIKLSDPGV-GLGVLSREERVER--------IPWIAPECVPGGN--------SLSTAADKWGFGATLLEi 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 643 -------LQARDWPFKHQpaealIWQIGSGegvrrvLASVSlGKEVGEILSACWAFDLQERPSFSLLMDML 706
Cdd:cd05076  214 cfngeapLQSRTPSEKER-----FYQRQHR------LPEPS-CPELATLISQCLTYEPTQRPSFRTILRDL 272
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
198-241 7.13e-06

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They 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 (C1), 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. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 43.44  E-value: 7.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 198 THRFSTKSWLSQV-CNVCQKSMIFGVKCKHCRLKCHNKCTKEAPA 241
Cdd:cd20811    2 SHNFVRKTFFTLAfCDVCRKLLFQGFRCQTCGFKFHQRCSDQVPA 46
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
444-582 7.20e-06

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: 48.22  E-value: 7.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 444 LGEPIGQGRWGRVHRGR---WHGEVAIRLlEMDGHNQDHLKlfkKEVMNYRQ--------------TRHENVVLFM---G 503
Cdd:cd14016    4 LVKKIGSGSFGEVYLGIdlkTGEEVAIKI-EKKDSKHPQLE---YEAKVYKLlqggpgiprlywfgQEGDYNVMVMdllG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 acmnpPHLAIITSFCKGR-TLhsfvrdpKTSLdinktrQIAQEIIKGMGYLHAKGIVHKDLKSKN----VFYDNGKVVIT 578
Cdd:cd14016   80 -----PSLEDLFNKCGRKfSL-------KTVL------MLADQMISRLEYLHSKGYIHRDIKPENflmgLGKNSNKVYLI 141

                 ....
gi 755537521 579 DFGL 582
Cdd:cd14016  142 DFGL 145
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
523-581 8.99e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 48.69  E-value: 8.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVrDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFG 581
Cdd:PHA03207 172 LFTYV-DRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEpENAVLGDFG 230
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
448-642 9.40e-06

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: 48.03  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRgrWHG-----EVAIRLL--EMDGHNQDHLKLfkkEVMNYRQTRHENVV--------LFMGACMNPPHLA 512
Cdd:cd14038    2 LGTGGFGNVLR--WINqetgeQVAIKQCrqELSPKNRERWCL---EIQIMKRLNHPNVVaardvpegLQKLAPNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 IitSFCKGRTLHSFVRDPKTSLDINK--TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG--KVV--ITDFGLfgis 586
Cdd:cd14038   77 M--EYCQGGDLRKYLNQFENCCGLREgaILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGeqRLIhkIIDLGY---- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 587 gvvREERRENQLKLSH-DWLCYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYE 642
Cdd:cd14038  151 ---AKELDQGSLCTSFvGTLQYLAPELL---------EQQKYTVTVDYWSFGTLAFE 195
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
442-643 1.07e-05

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: 48.08  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEpIGQGRWGRVHRGR---WHGEVAIRLLEMDgHNQDHLKLFKKEVMNYRQTRHENVVLFmgacmnppHLAIITSFC 518
Cdd:cd07871    8 VKLDK-LGEGTYATVFKGRsklTENLVALKEIRLE-HEEGAPCTAIREVSLLKNLKHANIVTL--------HDIIHTERC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKTSLD-------INKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVR 590
Cdd:cd07871   78 LTLVFEYLDSDLKQYLDncgnlmsMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLInEKGELKLADFGLARAKSVPT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 591 EERRENQLKLshdWlcYLAPEIvremIPGRDEdqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07871  158 KTYSNEVVTL---W--YRPPDV----LLGSTE----YSTPIDMWGVGCILYEM 197
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
446-719 1.14e-05

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: 47.72  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVH------RGRwhgEVAIRLLEMD-GHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFC 518
Cdd:cd14174    8 ELLGEGAYAKVQgcvslqNGK---EYAVKIIEKNaGHSRS--RVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGLFgiSGVVREER- 593
Cdd:cd14174   83 RGGSILAHIQKRK-HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdkvSPVKICDFDLG--SGVKLNSAc 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 594 ---RENQLKLSHDWLCYLAPEIVREMIpgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQigSGEGVR- 669
Cdd:cd14174  160 tpiTTPELTTPCGSAEYMAPEVVEVFT----DEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWD--RGEVCRv 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 670 ---RVLASVSLGKEvgEILSACWA---FDLQERPSFSLLMDMLERLPKLnRRLSHP 719
Cdd:cd14174  234 cqnKLFESIQEGKY--EFPDKDWShisSEAKDLISKLLVRDAKERLSAA-QVLQHP 286
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
494-705 1.16e-05

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: 47.82  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 494 RHENVVLFMGACMN-PPHLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAK-GIVHKDLKSKNVFYD 571
Cdd:cd06620   61 HSPYIVSFYGAFLNeNNNIIICMEYMDCGSLDKILKK-KGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVN 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 572 N-GKVVITDfglFGISGVVREERRENQLKLShdwlCYLAPeivrEMIPGRDedqlpFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd06620  140 SkGQIKLCD---FGVSGELINSIADTFVGTS----TYMSP----ERIQGGK-----YSVKSDVWSLGLSIIELALGEFPF 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 651 KHQPAEA-----------LIWQIgSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDM 705
Cdd:cd06620  204 AGSNDDDdgyngpmgildLLQRI-VNEPPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
448-643 1.45e-05

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: 47.49  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH--GE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVlfmgacmnpphlaiitsfckgrTLH 524
Cdd:cd07864   15 IGEGTYGQVYKAKDKdtGElVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVV----------------------NLK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 SFVRDPKTSLDINK-------------------------------TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN- 572
Cdd:cd07864   73 EIVTDKQDALDFKKdkgafylvfeymdhdlmgllesglvhfsedhIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNk 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 573 GKVVITDFGLFGISGvvREERRENQLKLSHDWlcYLAPEIV--REMipgrdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07864  153 GQIKLADFGLARLYN--SEESRPYTNKVITLW--YRPPELLlgEER----------YGPAIDVWSCGCILGEL 211
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
439-651 1.46e-05

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: 47.56  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVEL---GEPIGQGRWG--RVHRGRWHG-EVAIRLL--EMDGHNQdhlklfkKEVMNYRQTR-HENVVLFMGACMNPP 509
Cdd:cd14180    2 FQCYELdleEPALGEGSFSvcRKCRHRQSGqEYAVKIIsrRMEANTQ-------REVAALRLCQsHPNIVALHEVLHDQY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 510 HLAIITSFCKGRTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgi 585
Cdd:cd14180   75 HTYLVMELLRGGELLDRIKK-KARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadesDGAVLKVIDFGF--- 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 586 sGVVREERREnQLKLSHDWLCYLAPEIVREMipGRDEdqlpfskAADVYAFGTVWYELQARDWPFK 651
Cdd:cd14180  151 -ARLRPQGSR-PLQTPCFTLQYAAPELFSNQ--GYDE-------SCDLWSLGVILYTMLSGQVPFQ 205
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
448-582 1.54e-05

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 46.43  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  448 IGQGRWGRVHRGRWHGEVAI---------RLLEMDghnqdhlklfkkEVMNYRQTRHE------------NV-VLFMgac 505
Cdd:TIGR03724   2 IAKGAEAIIYLGDFLGRKAVikervpksyRHPELD------------ERLRKERTRREarllsrarkagvNTpVIYD--- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  506 MNPPHLAIITSFCKGRTLHSFVRDPKTsldinktrqiaqEIIKGMGY----LHAKGIVHKDLKSKNVFYDNGKVVITDFG 581
Cdd:TIGR03724  67 VDPDNKTIVMEYIEGKPLKDVIEENGD------------ELAREIGRlvgkLHKAGIVHGDLTTSNIIVRDDKVYLIDFG 134

                  .
gi 755537521  582 L 582
Cdd:TIGR03724 135 L 135
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
536-581 1.55e-05

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: 47.57  E-value: 1.55e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 536 INKTRQIAQEIIKGMGYLHAK-GIVHKDLKSKNV--FYDNGKVVITDFG 581
Cdd:cd14136  118 LPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVllCISKIEVKIADLG 166
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
543-653 1.76e-05

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: 47.05  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFGisgvvreERRENQLKLSHDWLCYLAPEIVREMIpgrd 621
Cdd:cd05606  104 AAEVILGLEHMHNRFIVYRDLKPANILLDeHGHVRISDLGLAC-------DFSKKKPHASVGTHGYMAPEVLQKGV---- 172
                         90       100       110
                 ....*....|....*....|....*....|..
gi 755537521 622 edqlPFSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd05606  173 ----AYDSSADWFSLGCMLYKLLKGHSPFRQH 200
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
520-650 1.81e-05

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: 47.24  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGLfgiSGVVR--EER 593
Cdd:cd14197   94 GEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSesplGDIKIVDFGL---SRILKnsEEL 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 594 RENQLKLShdwlcYLAPEIVremipgrdeDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14197  171 REIMGTPE-----YVAPEIL---------SYEPISTATDMWSIGVLAYVMLTGISPF 213
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
440-643 1.85e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 47.12  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITS 516
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARdrvTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 517 FCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFGL---FGISgvVRe 591
Cdd:PLN00009  82 YLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrrTNALKLADFGLaraFGIP--VR- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755537521 592 errenqlKLSHD--WLCYLAPEIvreMIPGRDedqlpFSKAADVYAFGTVWYEL 643
Cdd:PLN00009 159 -------TFTHEvvTLWYRAPEI---LLGSRH-----YSTPVDIWSVGCIFAEM 197
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
448-659 1.88e-05

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: 47.31  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRG---RWHGEVAIRLLEMDGHNQDHLKL-FKKEVMN----YRQTRHENVV-LFMGACMNPPHLAIITSFC 518
Cdd:cd13990    8 LGKGGFSEVYKAfdlVEQRYVACKIHQLNKDWSEEKKQnYIKHALReyeiHKSLDHPRIVkLYDVFEIDTDSFCTVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 519 KGRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYL--HAKGIVHKDLKSKNVFYDNGKVV----ITDFGLfgiSGVVREE 592
Cdd:cd13990   88 DGNDLDFYLKQHK-SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSgeikITDFGL---SKIMDDE 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 593 RRENQ-LKLSHD-----WlcYLAPEIvreMIPGRDEDQLpfSKAADVYAFGTVWYELQARDWPFKHQPAEALI 659
Cdd:cd13990  164 SYNSDgMELTSQgagtyW--YLPPEC---FVVGKTPPKI--SSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAI 229
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
546-646 2.11e-05

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: 47.13  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 546 IIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgiSGVVREERRENQLK--LSHDWlcYLAPEIVreMIPGRde 622
Cdd:cd07834  112 ILRGLKYLHSAGVIHRDLKPSNILVnSNCDLKICDFGL---ARGVDPDEDKGFLTeyVVTRW--YRAPELL--LSSKK-- 182
                         90       100
                 ....*....|....*....|....
gi 755537521 623 dqlpFSKAADVYAFGTVWYELQAR 646
Cdd:cd07834  183 ----YTKAIDIWSVGCIFAELLTR 202
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
530-643 2.14e-05

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: 46.90  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 530 PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL---FGISgvVReerrenqlKLSHD-- 603
Cdd:cd07835   92 PLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDtEGALKLADFGLaraFGVP--VR--------TYTHEvv 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755537521 604 WLCYLAPEIvreMIPGRDedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07835  162 TLWYRAPEI---LLGSKH-----YSTPVDIWSVGCIFAEM 193
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
445-663 2.24e-05

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: 47.02  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGR---WHGEVAIRLLEMDGHNQdHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGR 521
Cdd:cd14090    7 GELLGEGAYASVQTCInlyTGKEYAVKIIEKHPGHS-RSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 522 TLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVV---ITDFGLfgISGVVREERRENQ 597
Cdd:cd14090   86 PLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCEsMDKVSpvkICDFDL--GSGIKLSSTSMTP 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755537521 598 LKlSHDWLC------YLAPEIVREMIpgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIG 663
Cdd:cd14090  163 VT-TPELLTpvgsaeYMAPEVVDAFV----GEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDCGWDRG 229
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
448-582 2.30e-05

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: 46.83  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGR--WHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVV----LFMGACMNppHLAIITSFCKg 520
Cdd:cd07843   13 IEEGTYGVVYRARdkKTGEiVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVtvkeVVVGSNLD--KIYMVMEYVE- 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755537521 521 RTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGL 582
Cdd:cd07843   90 HDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNrGILKICDFGL 152
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
446-650 2.31e-05

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: 46.94  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGR---WHGEVAIRLLEMD-GHNQDhlKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII-TSFCKG 520
Cdd:cd14173    8 EVLGEGAYARVQTCInliTNKEYAVKIIEKRpGHSRS--RVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVfEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN----GKVVITDFGLFgiSGVvreerren 596
Cdd:cd14173   86 SILSHIHR--RRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHpnqvSPVKICDFDLG--SGI-------- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 597 qlKLSHDwlC----------------YLAPEIVREMipgrDEDQLPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14173  154 --KLNSD--CspistpelltpcgsaeYMAPEVVEAF----NEEASIYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
540-650 2.43e-05

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: 47.33  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 540 RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgvVREERRENQlklSHDWLC----YLAPEIVR 614
Cdd:cd05618  124 RFYSAEISLALNYLHERGIIYRDLKLDNVLLDSeGHIKLTDYGM------CKEGLRPGD---TTSTFCgtpnYIAPEILR 194
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755537521 615 emipGRDedqlpFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd05618  195 ----GED-----YGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
448-613 2.54e-05

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: 46.45  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHR------GR-WHGE-VAIRllemdgHNQDHLKLfKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd14103    1 LGRGKFGTVYRcvekatGKeLAAKfIKCR------KAKDREDV-RNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN---VFYDNGKVVITDFGLfgisgvVREERREN 596
Cdd:cd14103   74 GGELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENilcVSRTGNQIKIIDFGL------ARKYDPDK 147
                        170
                 ....*....|....*..
gi 755537521 597 QLKLSHDWLCYLAPEIV 613
Cdd:cd14103  148 KLKVLFGTPEFVAPEVV 164
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
441-658 2.69e-05

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: 47.05  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 441 QVELGEPIGQGRWGRV------HRGRwhgEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVvlfMGA--CMNPPHLA 512
Cdd:cd07853    1 DVEPDRPIGYGAFGVVwsvtdpRDGK---RVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNV---LSAldILQPPHID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 513 ------IITSFCKGrTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgi 585
Cdd:cd07853   75 pfeeiyVVTELMQS-DLHKIIVSPQ-PLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLkICDFGL--- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 586 sgvVREERRENQLKLSHDWLC--YLAPEIvreMIPGRDedqlpFSKAADVYAFGTVWYELQARDWPFKHQ-PAEAL 658
Cdd:cd07853  150 ---ARVEEPDESKHMTQEVVTqyYRAPEI---LMGSRH-----YTSAVDIWSVGCIFAELLGRRILFQAQsPIQQL 214
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
534-651 3.26e-05

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: 46.58  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 534 LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgvvREERRENQL-KLSHDWLCYLAPE 611
Cdd:cd05605   99 FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDhGHVRISDLGL-------AVEIPEGETiRGRVGTVGYMAPE 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755537521 612 IVremipgrDEDQLPFSkaADVYAFGTVWYELQARDWPFK 651
Cdd:cd05605  172 VV-------KNERYTFS--PDWWGLGCLIYEMIEGQAPFR 202
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
447-582 3.28e-05

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: 46.59  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 447 PIGQGRWGRV--HRGRWHGE-VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLfMGACMNPPHLAI-----ITSFC 518
Cdd:cd07858   12 PIGRGAYGIVcsAKNSETNEkVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIA-IKDIMPPPHREAfndvyIVYEL 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 519 KGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 582
Cdd:cd07858   91 MDTDLHQIIRSSQT-LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNaNCDLKICDFGL 154
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
435-582 3.89e-05

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: 46.38  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 435 WDIPF---EQVELGEPIGQGRWGRV---HRGRWHGEVAIRLLEmdghNQDHLKlFKKEVM---NYRQtrHENVVLFMGAC 505
Cdd:cd14132   10 LNVEWgsqDDYEIIRKIGRGKYSEVfegINIGNNEKVVIKVLK----PVKKKK-IKREIKilqNLRG--GPNIVKLLDVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 506 MNP--PHLAIITSFCKG---RTLHSfvrdpktSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVIT 578
Cdd:cd14132   83 KDPqsKTPSLIFEYVNNtdfKTLYP-------TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDheKRKLRLI 155

                 ....
gi 755537521 579 DFGL 582
Cdd:cd14132  156 DWGL 159
C1_DGKepsilon_typeIII_rpt1 cd20801
first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, ...
199-239 4.06e-05

first protein kinase C conserved region 1 (C1 domain) found in type III diacylglycerol kinase, DAG kinase epsilon, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase epsilon, also called diglyceride kinase epsilon (DGK-epsilon), is the only isoform classified as type III; it possesses a hydrophobic domain in addition to C1 and catalytic domains that are present in all DGKs, and shows selectivity for acyl chains. It is highly selective for arachidonate-containing species of DAG. It may terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition. DAG kinase epsilon contains two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410351  Cd Length: 54  Bit Score: 41.53  E-value: 4.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755537521 199 HRFSTKSWLSQV--CNVCQKSMIFGVKCKHCRLKCHNKCTKEA 239
Cdd:cd20801    4 HHWVSTDLFSKPtyCSVCETLILSGAFCDCCGLCVDEGCLRKA 46
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
541-703 4.75e-05

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: 45.83  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 541 QIAQEIIKGMGYLHAK-GIVHKDLKSKNVFYD-NGKVVITDFGlfgISGVVREERRENQlklSHDWLCYLAPEivREMIP 618
Cdd:cd06618  118 KMTVSIVKALHYLKEKhGVIHRDVKPSNILLDeSGNVKLCDFG---ISGRLVDSKAKTR---SAGCAAYMAPE--RIDPP 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 619 GRDEdqlpFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPS 698
Cdd:cd06618  190 DNPK----YDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPSLPPNEGFSPDFCSFVDLCLTKDHRYRPK 265

                 ....*
gi 755537521 699 FSLLM 703
Cdd:cd06618  266 YRELL 270
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
525-582 4.84e-05

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 46.81  E-value: 4.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 525 SFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGL 582
Cdd:PRK09605 416 EYIGGKDLKDVLEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGL 473
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
448-643 4.93e-05

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: 45.76  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRwHGE----VAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTL 523
Cdd:cd07848    9 VGEGAYGVVLKCR-HKEtkeiVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 524 HSFVRDPKTSLDiNKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV-ITDFGLfgiSGVVREERRENQLK-LS 601
Cdd:cd07848   88 ELLEEMPNGVPP-EKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLkLCDFGF---ARNLSEGSNANYTEyVA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755537521 602 HDWlcYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd07848  164 TRW--YRSPELLLGA---------PYGKAVDMWSVGCILGEL 194
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
443-582 5.17e-05

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: 45.71  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 443 ELGEPIGQGRWGRVHRGR---WHGEVAIRLlEMDGHNQDHLKLFKKEVMNYRQTRHenVVLFMGACMNPPHLAIITSFCk 519
Cdd:cd14017    3 KVVKKIGGGGFGEIYKVRdvvDGEEVAMKV-ESKSQPKQVLKMEVAVLKKLQGKPH--FCRLIGCGRTERYNYIVMTLL- 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 520 GRTLHSFVRD-PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-----FYDNGKVVITDFGL 582
Cdd:cd14017   79 GPNLAELRRSqPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigrgPSDERTVYILDFGL 147
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
473-714 5.47e-05

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: 45.82  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 473 DGHNQDHLKLFKKEVMNYRQTRHENVV-LFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMG 551
Cdd:cd14040   47 DEKKENYHKHACREYRIHKELDHPRIVkLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIVMQIVNALR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 552 YLH--AKGIVHKDLKSKNVFYDNG----KVVITDFGL--------FGISGVVREERRENQLklshdWlcYLAPEIvreMI 617
Cdd:cd14040  126 YLNeiKPPIIHYDLKPGNILLVDGtacgEIKITDFGLskimdddsYGVDGMDLTSQGAGTY-----W--YLPPEC---FV 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 618 PGRDEDQLpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVS--LGKEVGEILSACWAFDLQE 695
Cdd:cd14040  196 VGKEPPKI--SNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKpvVSNEAKAFIRRCLAYRKED 273
                        250
                 ....*....|....*....
gi 755537521 696 RPSFSLLMDMLERLPKLNR 714
Cdd:cd14040  274 RFDVHQLASDPYLLPHMRR 292
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
473-661 5.49e-05

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: 45.82  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 473 DGHNQDHLKLFKKEVMNYRQTRHENVV-LFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTsLDINKTRQIAQEIIKGMG 551
Cdd:cd14041   47 DEKKENYHKHACREYRIHKELDHPRIVkLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIIMQIVNALK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 552 YLHA--KGIVHKDLKSKNVFYDNG----KVVITDFGLFGIS-----GVVREERRENQLKLSHdWlcYLAPEIvreMIPGR 620
Cdd:cd14041  126 YLNEikPPIIHYDLKPGNILLVNGtacgEIKITDFGLSKIMdddsyNSVDGMELTSQGAGTY-W--YLPPEC---FVVGK 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755537521 621 DEDQLpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQ 661
Cdd:cd14041  200 EPPKI--SNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQ 238
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
445-582 6.20e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168 [Multi-domain]  Cd Length: 204  Bit Score: 44.58  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHRGRWHGEVAI---------RLLEMDghnqdhlklfkkEVMNYRQTRHENVVLF----MGAC------ 505
Cdd:COG3642    1 MDLIKQGAEAIIYLTDFLGLPAVvkeripkryRHPELD------------EKLRRERTRREARILAkareAGVPvpivyd 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 506 MNPPHLAIITSFCKGRTLHSFVRDPKTSLdinkTRQIAQEIikgmGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGL 582
Cdd:COG3642   69 VDPDNGLIVMEYIEGELLKDALEEARPDL----LREVGRLV----GKLHKAGIVHGDLTTSNIILSGGRIYFIDFGL 137
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
511-650 6.28e-05

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: 45.80  E-value: 6.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 511 LAIITSFCKGRTLHSFVRDPKtslDINKTRQIAQEIIKGMG----YLHAKGIVHKDLKSKNVFYD----NGKVVITDFGL 582
Cdd:cd14170   74 LLIVMECLDGGELFSRIQDRG---DQAFTEREASEIMKSIGeaiqYLHSINIAHRDVKPENLLYTskrpNAILKLTDFGF 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 583 fgisgvVREERRENQLKLSHDWLCYLAPEIVremipGRDEdqlpFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14170  151 ------AKETTSHNSLTTPCYTPYYVAPEVL-----GPEK----YDKSCDMWSLGVIMYILLCGYPPF 203
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
545-661 6.36e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 46.16  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVF-YDNGKVVITDFGLfgisgvVREERRENQLKLSHDWlC----YLAPEIVremipg 619
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFlMPTGIIKLGDFGF------SKQYSDSVSLDVASSF-CgtpyYLAPELW------ 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755537521 620 rdeDQLPFSKAADVYAFGTVWYELQARDWPFKhQPAEALIWQ 661
Cdd:PTZ00267 244 ---ERKRYSKKADMWSLGVILYELLTLHRPFK-GPSQREIMQ 281
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
440-569 6.54e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 45.30  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELgEPIGQGRWGRVHR--GRWHGEV-AIR--LLEMDGHNQDHLKLfkKEVMNYRQT-RHENVVLFMGACMNPPHLAI 513
Cdd:cd14139    1 EFLEL-EKIGVGEFGSVYKciKRLDGCVyAIKrsMRPFAGSSNEQLAL--HEVYAHAVLgHHPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 514 ITSFCKGRTLHSFVRDPKTS---LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF 569
Cdd:cd14139   78 QNEYCNGGSLQDAISENTKSgnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIF 136
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
446-587 6.88e-05

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: 45.85  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVlfmgacmnpphlAIITSFCKGRT 522
Cdd:cd07874   23 KPIGSGAQGIVcaaYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNII------------SLLNVFTPQKS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSF--------------VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLFGISG 587
Cdd:cd07874   91 LEEFqdvylvmelmdanlCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNiVVKSDCTLKILDFGLARTAG 170
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
521-704 6.94e-05

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: 45.33  E-value: 6.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFGlfgiSGVVREERRENQL 598
Cdd:cd14102   90 KDLFDFITE-KGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlrTGELKLIDFG----SGALLKDTVYTDF 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 599 KLSHdwlCYLAPEIVR-EMIPGRdedqlpfskAADVYAFGTVWYELQARDWPFKhQPAEALiwqigsgEGvrRVLASVSL 677
Cdd:cd14102  165 DGTR---VYSPPEWIRyHRYHGR---------SATVWSLGVLLYDMVCGDIPFE-QDEEIL-------RG--RLYFRRRV 222
                        170       180
                 ....*....|....*....|....*..
gi 755537521 678 GKEVGEILSACWAFDLQERPSFSLLMD 704
Cdd:cd14102  223 SPECQQLIKWCLSLRPSDRPTLEQIFD 249
PHA02988 PHA02988
hypothetical protein; Provisional
455-652 6.95e-05

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 45.50  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 455 RVHRGRWHGE-VAIRLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVV----LFMGACMNPPHLAIITSFCKGRTLHSFVR 528
Cdd:PHA02988  35 SIYKGIFNNKeVIIRTFKKFHKGHKVLiDITENEIKNLRRIDSNNILkiygFIIDIVDDLPRLSLILEYCTRGYLREVLD 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 529 DPKtSLDINKTRQIAQEIIKGMGYLHAK-GIVHKDLKSkNVFY--DNGKVVITDFGLFGISGVVREERRenqlklshDWL 605
Cdd:PHA02988 115 KEK-DLSFKTKLDMAIDCCKGLYNLYKYtNKPYKNLTS-VSFLvtENYKLKIICHGLEKILSSPPFKNV--------NFM 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 606 CYLAPEIVREMIPGRDEDQlpfskaaDVYAFGTVWYELQARDWPFKH 652
Cdd:PHA02988 185 VYFSYKMLNDIFSEYTIKD-------DIYSLGVVLWEIFTGKIPFEN 224
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
540-704 7.04e-05

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: 45.35  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 540 RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFGlfgiSGVVREERRENQLKLSHdwlCYLAPEIVR-EM 616
Cdd:cd14100  109 RSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlnTGELKLIDFG----SGALLKDTVYTDFDGTR---VYSPPEWIRfHR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 617 IPGRdedqlpfskAADVYAFGTVWYELQARDWPFKHQPaealiwQIGSGEgvrrVLASVSLGKEVGEILSACWAFDLQER 696
Cdd:cd14100  182 YHGR---------SAAVWSLGILLYDMVCGDIPFEHDE------EIIRGQ----VFFRQRVSSECQHLIKWCLALRPSDR 242

                 ....*...
gi 755537521 697 PSFSLLMD 704
Cdd:cd14100  243 PSFEDIQN 250
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
199-243 7.20e-05

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 41.13  E-value: 7.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 199 HRFSTKSW-LSQVCNVCQkSMIF----GVKCKHCRLKCHNKC-TKEAPACR 243
Cdd:cd20818    4 HKFATVQFnIPTYCEVCN-SFIWlmekGLVCQVCKFTCHKKCySKITAPCK 53
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
541-707 7.25e-05

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: 45.47  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 541 QIAQEIIKGMGYLH-AKGIVHKDLKSKNVFY--DNGKVVITDFGlfgisgvVREERRENQLKLSHDWLCYL------APE 611
Cdd:cd14001  114 KVALSIARALEYLHnEKKILHGDIKSGNVLIkgDFESVKLCDFG-------VSLPLTENLEVDSDPKAQYVgtepwkAKE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 612 IVremipgrdEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE-------------GVRRVLASVSLG 678
Cdd:cd14001  187 AL--------EEGGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIEDDDEDESFDedeedeeayygtlGTRPALNLGELD 258
                        170       180       190
                 ....*....|....*....|....*....|..
gi 755537521 679 KE---VGEILSACWAFDLQERPSFSLLMDMLE 707
Cdd:cd14001  259 DSyqkVIELFYACTQEDPKDRPSAAHIVEALE 290
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
523-643 8.05e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 45.76  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGISGVVREERrenqlklS 601
Cdd:PHA03212 169 LYCYLAA-KRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHpGDVCLGDFGAACFPVDINANK-------Y 240
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755537521 602 HDWLCYLA---PEIVremipGRDedqlPFSKAADVYAFGTVWYEL 643
Cdd:PHA03212 241 YGWAGTIAtnaPELL-----ARD----PYGPAVDIWSAGIVLFEM 276
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
198-240 8.13e-05

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, 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. C-Raf, also known as proto-oncogene 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 mid-gestation 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. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), 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. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410420  Cd Length: 52  Bit Score: 40.71  E-value: 8.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 755537521 198 THRFSTKSWLS-QVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAP 240
Cdd:cd20870    3 THNFVRKTFLKlAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVP 46
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
448-650 8.91e-05

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: 45.02  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWH---GEVAIRLLE----MDGH-NQDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd08228   10 IGRGQFSEVYRATCLldrKPVALKKVQifemMDAKaRQDCVK----EIDLLKQLNHPNVIKYLDSFIEDNELNIVLELAD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQ---EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvrEERRE 595
Cdd:cd08228   86 AGDLSQMIKYFKKQKRLIPERTVWKyfvQLCSAVEHMHSRRVMHRDIKPANVFITaTGVVKLGDLGL--------GRFFS 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 596 NQLKLSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd08228  158 SKTTAAHSLVgtpYYMSPERIHEN---------GYNFKSDIWSLGCLLYEMAALQSPF 206
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
199-242 9.00e-05

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 40.45  E-value: 9.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 199 HRFSTKSW-LSQVCNVCQKSM-IFGVKCKHCRLKCHNKC-TKEAPAC 242
Cdd:cd20826    3 HSFKEKSFrKPRTCDVCKQIIwNEGSSCRVCKYACHRKCePKVTAAC 49
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
494-643 9.65e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 45.09  E-value: 9.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 494 RHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTS---LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY 570
Cdd:cd14051   58 KHPHVVRYYSAWAEDDHMIIQNEYCNGGSLADAISENEKAgerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 571 DNGKVVItdfglfgISGVVREERRENQLK------------LSH------------DwlC-YLAPEIVREmipgrDEDQL 625
Cdd:cd14051  138 SRTPNPV-------SSEEEEEDFEGEEDNpesnevtykigdLGHvtsisnpqveegD--CrFLANEILQE-----NYSHL 203
                        170
                 ....*....|....*...
gi 755537521 626 PfskAADVYAFGTVWYEL 643
Cdd:cd14051  204 P---KADIFALALTVYEA 218
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
446-582 9.83e-05

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: 45.07  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRGRW--HGEVA----IRLLEMDGHNQDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd07869   11 EKLGEGSYATVYKGKSkvNGKLValkvIRLQEEEGTPFTAIR----EASLLKGLKHANIVLLHDIIHTKETLTLVFEYVH 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 520 GRTLHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL 582
Cdd:cd07869   87 TDLCQYMDKHPG-GLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIsDTGELKLADFGL 149
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
465-643 1.02e-04

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: 45.16  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 465 VAIRLLEM-DGHNQDHLKlfkKEVMNYRQTRHENVV-----LFMGACMNPPHLAIITSFCKGRTLHSFVRD------PKT 532
Cdd:cd07854   33 VAVKKIVLtDPQSVKHAL---REIKIIRRLDHDNIVkvyevLGPSGSDLTEDVGSLTELNSVYIVQEYMETdlanvlEQG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 533 SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV--ITDFGLFGISGVVREERRENQLKLSHDWlcYLAP 610
Cdd:cd07854  110 PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlkIGDFGLARIVDPHYSHKGYLSEGLVTKW--YRSP 187
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755537521 611 EIVreMIPGRdedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07854  188 RLL--LSPNN------YTKAIDMWAAGCIFAEM 212
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
543-659 1.05e-04

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: 45.03  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlfgisgvvreerreNQLKLSHDWLC----------YLAPE 611
Cdd:cd05597  108 LAEMVLAIDSIHQLGYVHRDIKPDNVLLDrNGHIRLADFG--------------SCLKLREDGTVqssvavgtpdYISPE 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 612 IVREMIPGRDEdqlpFSKAADVYAFGTVWYELQARDWPFKhqpAEALI 659
Cdd:cd05597  174 ILQAMEDGKGR----YGPECDWWSLGVCMYEMLYGETPFY---AESLV 214
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
199-241 1.22e-04

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 40.33  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 199 HRFSTKSWLSQV-CNVCQKSMIF----GVKCKHCRLKCHNKCTKEAPA 241
Cdd:cd20809    1 HKFIVRTFSTPTkCNHCTSLMVGlvrqGLVCEVCGYACHVSCADKAPQ 48
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
440-651 1.62e-04

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: 44.25  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 440 EQVELGEPIGQGRWGRVHR-------GRWhgeVAIRLLEMDGHNQDHLKLFKKEVMNYRQTR---HENVVLFMGACM--- 506
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKardlkngGRF---VALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTvsr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 507 --NPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLF 583
Cdd:cd07862   78 tdRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVtSSGQIKLADFGLA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 584 GISGVvreerrenQLKLSH--DWLCYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd07862  158 RIYSF--------QMALTSvvVTLWYRAPEVLL---------QSSYATPVDLWSVGCIFAEMFRRKPLFR 210
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
439-643 2.15e-04

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: 44.07  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 439 FEQVELgepIGQGRWGRV-----HRGrwHGEVAIRLL--EMDGHNQ--------DHLKLfKKEVMNYRQTRHENVVLFMG 503
Cdd:cd14210   15 YEVLSV---LGKGSFGQVvkcldHKT--GQLVAIKIIrnKKRFHQQalvevkilKHLND-NDPDDKHNIVRYKDSFIFRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 504 acmnppHLAIITSFCkGRTLHSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNV-FYDNGKVVIT--D 579
Cdd:cd14210   89 ------HLCIVFELL-SINLYELLKSNNfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENIlLKQPSKSSIKviD 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 580 FGlfgiSGVVreerrENQLKLShdwlcYL------APEIVREMipgrdedqlPFSKAADVYAFGTVWYEL 643
Cdd:cd14210  162 FG----SSCF-----EGEKVYT-----YIqsrfyrAPEVILGL---------PYDTAIDMWSLGCILAEL 208
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
431-643 2.33e-04

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 43.70  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 431 YLQE----WdipFEQVELGEpigqgrwgrVHRGRWHGEVAIRLLEMDGH--NQDHlklFKKEVMNYRQTRHENVVLFMGA 504
Cdd:cd05086    1 YIQEigngW---FGKVLLGE---------IYTGTSVARVVVKELKASANpkEQDD---FLQQGEPYYILQHPNILQCVGQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPPHLAIITSFCKGRTLHSFVRDPKTSL----DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITD 579
Cdd:cd05086   66 CVEAIPYLLVFEFCDLGDLKTYLANQQEKLrgdsQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDlTVKVGD 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 580 FGLfgisGVVReeRRENQLKLSHDWLC---YLAPEIVREMipgrdEDQL---PFSKAADVYAFGTVWYEL 643
Cdd:cd05086  146 YGI----GFSR--YKEDYIETDDKKYAplrWTAPELVTSF-----QDGLlaaEQTKYSNIWSLGVTLWEL 204
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
535-581 3.03e-04

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 43.58  E-value: 3.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 535 DINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD--NGKVVITDFG 581
Cdd:cd14013  118 ENVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSegDGQFKIIDLG 166
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
446-582 3.17e-04

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: 43.41  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRVHRG--RWHGE-VAIRLLEMDGHNQDHLKLFKkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRT 522
Cdd:cd07870    6 EKLGEGSYATVYKGisRINGQlVALKVISMKTEEGVPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537521 523 LHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGL 582
Cdd:cd07870   85 AQYMIQHPG-GLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYlGELKLADFGL 144
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
498-653 3.20e-04

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: 43.50  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 498 VVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINkTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVV 576
Cdd:cd14223   65 IVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEAE-MRFYAAEIILGLEHMHSRFVVYRDLKPANILLDeFGHVR 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 577 ITDFGLfgisGVVREERRENQLKLSHDwlcYLAPEIVREMIpgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQ 653
Cdd:cd14223  144 ISDLGL----ACDFSKKKPHASVGTHG---YMAPEVLQKGV--------AYDSSADWFSLGCMLFKLLRGHSPFRQH 205
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
523-666 3.39e-04

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 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: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 43.10  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREErrENQLKLSH 602
Cdd:cd14022   71 MHSFVRTCKKLREEEAARLFYQ-IASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGH--DDSLSDKH 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 603 DWLCYLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14022  148 GCPAYVSPEIL-------NTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ 204
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
523-581 3.40e-04

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: 43.41  E-value: 3.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537521 523 LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFG 581
Cdd:cd07831   86 LYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDILKLADFG 144
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
484-643 3.58e-04

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: 43.05  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 484 KKEV-MNYRQTRHENVV----LFMGACMNPPHLAIITSFCKGRTLHSFVRDpktSLDINKTRQIAQEIIKGMG----YLH 554
Cdd:cd14089   41 RREVeLHWRASGCPHIVriidVYENTYQGRKCLLVVMECMEGGELFSRIQE---RADSAFTEREAAEIMRQIGsavaHLH 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 555 AKGIVHKDLKSKNVFY----DNGKVVITDFGlFGisgvvreerRENQLKLSHDWLC----YLAPEIVremipGRDEdqlp 626
Cdd:cd14089  118 SMNIAHRDLKPENLLYsskgPNAILKLTDFG-FA---------KETTTKKSLQTPCytpyYVAPEVL-----GPEK---- 178
                        170
                 ....*....|....*..
gi 755537521 627 FSKAADVYAFGTVWYEL 643
Cdd:cd14089  179 YDKSCDMWSLGVIMYIL 195
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
441-698 3.60e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.96  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  441 QVELGEPIGQGRWGRV----HRgRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPH--LAII 514
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVflvkHK-RTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKANqkLYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  515 TSFCKGRTLHSFVRDPKT---SLDINKTRQIAQEIIKGMGYLH-------AKGIVHKDLKSKNVFYDN-----GKVV--- 576
Cdd:PTZ00266   93 MEFCDAGDLSRNIQKCYKmfgKIEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTgirhiGKITaqa 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521  577 -------ITDFGLFGISGVVREErrenqlKLSHDWL---CYLAPEIVREMIPGRDEDqlpfskaADVYAFGTVWYELQAR 646
Cdd:PTZ00266  173 nnlngrpIAKIGDFGLSKNIGIE------SMAHSCVgtpYYWSPELLLHETKSYDDK-------SDMWALGCIIYELCSG 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755537521  647 DWPF-KHQPAEALIWQIGSGEGvrrvLASVSLGKEVGEILSACWAFDLQERPS 698
Cdd:PTZ00266  240 KTPFhKANNFSQLISELKRGPD----LPIKGKSKELNILIKNLLNLSAKERPS 288
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
535-582 3.62e-04

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: 43.32  E-value: 3.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 535 DINKtRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGL 582
Cdd:cd07852  106 DIHK-QYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDcRVKLADFGL 153
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
530-581 3.63e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 43.91  E-value: 3.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 530 PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFG 581
Cdd:PLN03224 302 PQDKRDINVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTvDGQVKIIDFG 354
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
476-643 3.94e-04

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: 43.04  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 476 NQDHLKLFKKEVMNYRQ-TRHENVVLFMGACMNPP-----HLAIITSFCKGRTLhsfvrdpktsLDINKTR--------- 540
Cdd:cd14037   40 DEHDLNVCKREIEIMKRlSGHKNIVGYIDSSANRSgngvyEVLLLMEYCKGGGV----------IDLMNQRlqtgltese 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 541 --QIAQEIIKGMGYLHA--KGIVHKDLKSKNVFY-DNGKVVITDFGlfGISGVVREERRE---NQLK---LSHDWLCYLA 609
Cdd:cd14037  110 ilKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLIsDSGNYKLCDFG--SATTKILPPQTKqgvTYVEediKKYTTLQYRA 187
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755537521 610 PEIVrEMIPGrdedqLPFSKAADVYAFGTVWYEL 643
Cdd:cd14037  188 PEMI-DLYRG-----KPITEKSDIWALGCLLYKL 215
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
448-642 4.33e-04

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 42.95  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGEV-AIRLLEMDGHNQ--DHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLh 524
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSyAVKLFKQEKKMQwkKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 525 sFVRDPKTSLDINKTRQIAQEIIKGMG----YLHAK---GIVHKDLKSKNVFYD-NGKVVITDFGLFGI-SGVVREERRE 595
Cdd:cd14160   80 -FDRLQCHGVTKPLSWHERINILIGIAkaihYLHNSqpcTVICGNISSANILLDdQMQPKLTDFALAHFrPHLEDQSCTI 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 596 NQLKLSHDWLCYLAPEIVREmipGRdedqlpFSKAADVYAFGTVWYE 642
Cdd:cd14160  159 NMTTALHKHLWYMPEEYIRQ---GK------LSVKTDVYSFGIVIME 196
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
523-666 4.37e-04

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 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: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 42.73  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREErrENQLKLSH 602
Cdd:cd14023   71 MHSYVRSCK-RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGE--DDALSDKH 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537521 603 DWLCYLAPEIVremipgrDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd14023  148 GCPAYVSPEIL-------NTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ 204
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
448-571 4.57e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 42.90  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRWHGEVAI--RLLEMDGHNQDHL-KLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLH 524
Cdd:cd14157    1 ISEGTFADIYKGYRHGKQYVikRLKETECESPKSTeRFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQ 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755537521 525 SFVRDPKTSLDINKTRQ--IAQEIIKGMGYLHAKGIVHKDLKSKNVFYD 571
Cdd:cd14157   81 DRLQQQGGSHPLPWEQRlsISLGLLKAVQHLHNFGILHGNIKSSNVLLD 129
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
523-666 4.69e-04

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB 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: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 42.42  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLK-SKNVFYDNGKvviTDFGLFGISGVVREERRENQLKLS 601
Cdd:cd13976   71 LHSYVRSRK-RLREPEAARLFRQIASAVAHCHRNGIVLRDLKlRKFVFADEER---TKLRLESLEDAVILEGEDDSLSDK 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755537521 602 HDWLCYLAPEIVRemiPGRDEDqlpfSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGE 666
Cdd:cd13976  147 HGCPAYVSPEILN---SGATYS----GKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQ 204
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
199-240 5.11e-04

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; 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. 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. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 38.57  E-value: 5.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755537521 199 HRFSTKSWLSQV-CNVCqKSMIFG-----VKCKHCRLKCHNKCTKEAP 240
Cdd:cd20837    1 HRFKVYNYMSPTfCDHC-GSLLWGlfrqgLKCEECGMNVHHKCQKKVA 47
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
199-236 5.46e-04

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 38.80  E-value: 5.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755537521 199 HRFS---TKSWLSQVCNVCqKSMIFGV-----KCKHCRLKCHNKCT 236
Cdd:cd20819    6 HHFVlqkSKSSSKQYCDKC-CGIIWGLlqtwyRCTDCGYRCHSKCL 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
194-243 6.30e-04

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 38.58  E-value: 6.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537521 194 GLSVTHRFSTKSWLS-QVCNVCQKSMIF----GVKCKHCRLKCHNKCTKEAP-ACR 243
Cdd:cd20828    1 GFTQPHNFEPHSFVTpTNCDYCLQILWGivkkGMKCSECGYNCHEKCQPQVPkQCS 56
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
199-242 6.48e-04

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 38.19  E-value: 6.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755537521  199 HRFSTKSWLSQV-CNVCQKSMIF----GVKCKHCRLKCHNKCTKEAPAC 242
Cdd:pfam00130   1 HHFVHRNFKQPTfCDHCGEFLWGlgkqGLKCSWCKLNVHKRCHEKVPPE 49
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
446-587 6.55e-04

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: 42.72  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 446 EPIGQGRWGRV---HRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVlfmgacmnpphlAIITSFCKGRT 522
Cdd:cd07875   30 KPIGSGAQGIVcaaYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNII------------GLLNVFTPQKS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 523 LHSF--------------VRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKN-VFYDNGKVVITDFGLFGISG 587
Cdd:cd07875   98 LEEFqdvyivmelmdanlCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNiVVKSDCTLKILDFGLARTAG 177
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
543-582 6.77e-04

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: 42.67  E-value: 6.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 582
Cdd:cd05589  107 AACVVLGLQFLHEHKIVYRDLKLDNLLLDtEGYVKIADFGL 147
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
448-709 7.00e-04

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: 42.33  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 448 IGQGRWGRVHRGRW---HGEVAIRLLE----MDGH-NQDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd08229   32 IGRGQFSEVYRATClldGVPVALKKVQifdlMDAKaRADCIK----EIDLLKQLNHPNVIKYYASFIEDNELNIVLELAD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GRTLHSFVRDPKTSLDINKTRQIAQ---EIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgisgvvrEERRE 595
Cdd:cd08229  108 AGDLSRMIKHFKKQKRLIPEKTVWKyfvQLCSALEHMHSRRVMHRDIKPANVFITaTGVVKLGDLGL--------GRFFS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 596 NQLKLSHDWL---CYLAPEIVREMipgrdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAE--ALIWQIGSGEgvRR 670
Cdd:cd08229  180 SKTTAAHSLVgtpYYMSPERIHEN---------GYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCD--YP 248
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755537521 671 VLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERL 709
Cdd:cd08229  249 PLPSDHYSEELRQLVNMCINPDPEKRPDITYVYDVAKRM 287
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
545-582 7.10e-04

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: 42.56  E-value: 7.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755537521 545 EIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGL 582
Cdd:cd05610  112 EVALALDYLHRHGIIHRDLKPDNMLISNeGHIKLTDFGL 150
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
481-656 7.31e-04

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: 42.27  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 481 KLFKKEVMNYRQTRHENVVLfmgACMNPPHL-AIITSF-------------CKGRTLHSFVRdpKTSLDINKTRQIAQEI 546
Cdd:cd14113   38 KFVNKKLMKRDQVTHELGVL---QSLQHPQLvGLLDTFetptsyilvlemaDQGRLLDYVVR--WGNLTEEKIRFYLREI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 547 IKGMGYLHAKGIVHKDLKSKNVFYDNG----KVVITDFGlfgisgvvrEERRENQLKLSHDWLC---YLAPEIvremIPG 619
Cdd:cd14113  113 LEALQYLHNCRIAHLDLKPENILVDQSlskpTIKLADFG---------DAVQLNTTYYIHQLLGspeFAAPEI----ILG 179
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755537521 620 RdedqlPFSKAADVYAFGTVWYELQARDWPFKHQPAE 656
Cdd:cd14113  180 N-----PVSLTSDLWSIGVLTYVLLSGVSPFLDESVE 211
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
505-646 7.56e-04

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: 42.54  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 505 CMNPP---HLAIITSFCKGRTLHSFVRDPKTSLDINKTrqIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGK----VVI 577
Cdd:cd13977  101 CFDPRsacYLWFVMEFCDGGDMNEYLLSRRPDRQTNTS--FMLQLSSALAFLHRNQIVHRDLKPDNILISHKRgepiLKV 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 578 TDFGLFGI---SGVVREERRE-NQLKLSHdwLC----YLAPEIVREMipgrdedqlpFSKAADVYAFGTVWYELQAR 646
Cdd:cd13977  179 ADFGLSKVcsgSGLNPEEPANvNKHFLSS--ACgsdfYMAPEVWEGH----------YTAKADIFALGIIIWAMVER 243
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
445-643 7.66e-04

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: 42.36  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 445 GEPIGQGRWGRVHR-----GRWHGEVAIRLLEMDGHNQDHLKlfkkEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCK 519
Cdd:cd07867    7 GCKVGRGTYGHVYKakrkdGKDEKEYALKQIEGTGISMSACR----EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 520 GR-------TLHSFVRDPKTSLDINKT--RQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-----DNGKVVITDFGLFGI 585
Cdd:cd07867   83 AEhdlwhiiKFHRASKANKKPMQLPRSmvKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegpERGRVKIADMGFARL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755537521 586 SGVVREERRENQLKLSHDWlcYLAPEIvreMIPGRDedqlpFSKAADVYAFGTVWYEL 643
Cdd:cd07867  163 FNSPLKPLADLDPVVVTFW--YRAPEL---LLGARH-----YTKAIDIWAIGCIFAEL 210
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
210-240 7.85e-04

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); 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 are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 38.04  E-value: 7.85e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755537521 210 VCNVCQKSM--IF--GVKCKHCRLKCHNKCTKEAP 240
Cdd:cd20796   14 VCQHCKKLLkgLFrqGLQCKDCKFNCHKKCAEKVP 48
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
442-640 9.12e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 41.81  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 442 VELGEPIGQGRWGRVHRGRWHG-------EVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAII 514
Cdd:cd14208    1 LTFMESLGKGSFTKIYRGLRTDeeddercETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGKDSIMVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 515 TSFCKGRT-LHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKnvfydngKVVITDFGLFGISGVVREER 593
Cdd:cd14208   81 EFVCHGALdLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAK-------KVLLSREGDKGSPPFIKLSD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755537521 594 RENQLK-LSHDWLC----YLAPEIVRemipgrdeDQLPFSKAADVYAFG-TVW 640
Cdd:cd14208  154 PGVSIKvLDEELLAeripWVAPECLS--------DPQNLALEADKWGFGaTLW 198
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
211-246 9.52e-04

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 38.12  E-value: 9.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755537521 211 CNVCQkSMIFGVK-----CKHCRLKCHNKCTKEAPA-CRITF 246
Cdd:cd20799   19 CNVCE-NMLVGLRkqglcCTFCKYTVHERCVSRAPAsCIRTY 59
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
199-241 9.74e-04

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, 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 (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 37.61  E-value: 9.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755537521 199 HRFSTK-SWLSQVCNVCQKSMIFG---VKCKHCRLKCHNKCTKEAPA 241
Cdd:cd20814    5 HRFTTGlNMRATKCAVCLDGVPFGrqaSKCSECGIVCHPKCSSSLPN 51
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
498-582 1.04e-03

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: 41.79  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 498 VVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDinktrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVV 576
Cdd:cd06619   61 IIGFYGAFFVENRISICTEFMDGGSLDVYRKIPEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTrGQVK 135

                 ....*.
gi 755537521 577 ITDFGL 582
Cdd:cd06619  136 LCDFGV 141
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
543-651 1.05e-03

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: 41.88  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 543 AQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLfgisgVVREERRENqLKLSHDWLCYLAPEIVREMipgrd 621
Cdd:cd05632  110 AAEILCGLEDLHRENTVYRDLKPENILLDDyGHIRISDLGL-----AVKIPEGES-IRGRVGTVGYMAPEVLNNQ----- 178
                         90       100       110
                 ....*....|....*....|....*....|
gi 755537521 622 edqlPFSKAADVYAFGTVWYELQARDWPFK 651
Cdd:cd05632  179 ----RYTLSPDYWGLGCLIYEMIEGQSPFR 204
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
521-650 1.08e-03

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: 41.94  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 521 RTLHSFVRDPKTS-LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-----KVVITDFGLFG-ISGVVREER 593
Cdd:cd14229   85 QNLYDFLKQNKFSpLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPvrqpyRVKVIDFGSAShVSKTVCSTY 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755537521 594 RENQLklshdwlcYLAPEIVRemipgrdedQLPFSKAADVYAFGTVWYELqARDWPF 650
Cdd:cd14229  165 LQSRY--------YRAPEIIL---------GLPFCEAIDMWSLGCVIAEL-FLGWPL 203
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
199-243 1.11e-03

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 37.68  E-value: 1.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537521 199 HRFSTKSWLSQV-CNVCQKSM----IFGVKCKHCRLKCHNKC-TKEAPACR 243
Cdd:cd20824    2 HNFKPHSFSIPTkCDYCGEKIwglsKKGLSCKDCGFNCHIKCeLKVPPECP 52
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
535-650 1.13e-03

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: 41.34  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537521 535 DINKTRQIA---QEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLfgisgvvreERRENQLKLSHdwLCYLAPE 611
Cdd:cd14109   94 DYYTERQVAvfvRQLLLALKHMHDLGIAHLDLRPEDILLQDDKLKLADFGQ---------SRRLLRGKLTT--LIYGSPE 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755537521 612 IVR-EMIPGRdedqlPFSKAADVYAFGTVWYELQARDWPF 650
Cdd:cd14109  163 FVSpEIVNSY-----PVTLATDMWSVGVLTYVLLGGISPF 197
 
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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