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Conserved domains on  [gi|530379706|ref|XP_005271949|]
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casein kinase I isoform X8 [Homo sapiens]

Protein Classification

casein kinase I( domain architecture ID 10197553)

casein kinase I (CKI) family protein is a serine/threonine-protein kinase which catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, similar to CKI-gamma isoforms

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0006468|GO:0004674|GO:0005524
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
42-328 0e+00

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 652.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 281
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 282 -EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 328
Cdd:cd14126  241 eEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
328-417 1.22e-38

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


:

Pssm-ID: 463640  Cd Length: 99  Bit Score: 135.39  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  328 KQLPTPVGAVQ-QDPALSSNREAHQHRDK------MQQSKNQSADHRAAW--DSQQANPHHLRAHLAADRHGGSVQVVSS 398
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRpplpqpRRVSQQGSKGRKGAWppPTPQTNAETLGSHLPADRHGGSVQVVSS 80
                          90
                  ....*....|....*....
gi 530379706  399 TNGELNTDDPTAGRSNAPI 417
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
 
Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
42-328 0e+00

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 652.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 281
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 282 -EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 328
Cdd:cd14126  241 eEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
328-417 1.22e-38

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


Pssm-ID: 463640  Cd Length: 99  Bit Score: 135.39  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  328 KQLPTPVGAVQ-QDPALSSNREAHQHRDK------MQQSKNQSADHRAAW--DSQQANPHHLRAHLAADRHGGSVQVVSS 398
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRpplpqpRRVSQQGSKGRKGAWppPTPQTNAETLGSHLPADRHGGSVQVVSS 80
                          90
                  ....*....|....*....
gi 530379706  399 TNGELNTDDPTAGRSNAPI 417
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
43-274 6.82e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 122.25  E-value: 6.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706    43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSgDGIPQVYYFGPCGKYNAMVLELL 119
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   120 gpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPET 197
Cdd:smart00220  80 --EGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-----VKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706   198 kkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRATPIE 274
Cdd:smart00220 153 --------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
39-251 1.62e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.20  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  39 VGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQ----LHLEYRFYKQLgSGDGIPQVYYFGPCGKYNA 113
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKvLRPELAADPEarerFRREARALARL-NHPNIVRVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 192
Cdd:COG0515   84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-----RVKLIDFGIARAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 IDPETKkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:COG0515  158 GGATLT------QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG 210
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
38-308 8.93e-24

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 100.80  E-value: 8.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFG---ELRLGKNLYTNEYVAIKLEPMKSRApqLHLEYRFYKQLGSGD--------------GIP 100
Cdd:PHA02882   9 ITGKEWKIDKLIGCGGFGcvyETQCASDHCINNQAVAKIENLENET--IVMETLVYNNIYDIDkialwknihnidhlGIP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 101 QvyYFGpCG--KYNAM-----VLELLGPSLEDLFDLCdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrp 173
Cdd:PHA02882  87 K--YYG-CGsfKRCRMyyrfiLLEKLVENTKEIFKRI-KCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMV--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 174 gnKTQQVIHIIDFGLAKEYIdpETKKHIPY-REHKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:PHA02882 160 --DGNNRGYIIDYGIASHFI--IHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKG 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 252 LKADTLKERYQKIGDTKRATPIEVLCENFPE-MATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:PHA02882 236 FGHNGNLIHAAKCDFIKRLHEGKIKIKNANKfIYDFIECVTKLSYEEKPDYDALIKIF 293
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
46-200 2.42e-11

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 63.67  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   46 GKKIGCGNFGELRLGK----NLYTNEYVAIKLepMKSRAPQLHL-----EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKT--LKEGADEEERedfleEASIMKKL-DHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE-YID 194
Cdd:pfam07714  81 EYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL-----VVKISDFGLSRDiYDD 155

                  ....*.
gi 530379706  195 PETKKH 200
Cdd:pfam07714 156 DYYRKR 161
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
44-251 1.54e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.28  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  44 RVGKKIGCGNFGELRLGKNLYTNEYVAIKLepmksrapqLHLEY--------RFYK------QLgSGDGIPQVYYFGPCG 109
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKV---------LRPDLardpefvaRFRReaqsaaSL-SHPNIVSVYDVGEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 188
Cdd:NF033483  80 GIPYIVMEYVdGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR-----VKVTDFGI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 189 AKEYidPETkkhipyrehkSLT------GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 251
Cdd:NF033483 154 ARAL--SST----------TMTqtnsvlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
 
Name Accession Description Interval E-value
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
42-328 0e+00

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 652.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd14126    1 NFRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14126   81 SLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKQHVIHIIDFGLAKEYIDPETNKHI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 281
Cdd:cd14126  161 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 282 -EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGK 328
Cdd:cd14126  241 eEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDWTGK 288
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
42-308 8.44e-167

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: 469.63  E-value: 8.44e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14016   81 SLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNK--VYLIDFGLAKKYRDPRTGKHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP 281
Cdd:cd14016  159 PYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSPEELCKGLP 238
                        250       260
                 ....*....|....*....|....*...
gi 530379706 282 -EMATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:cd14016  239 kEFAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
43-317 2.24e-160

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 453.75  E-value: 2.24e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd14125    2 YRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpGNKTQQViHIIDFGLAKEYIDPETKKHIP 202
Cdd:cd14125   82 LEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGL-GKKGNLV-YIIDFGLAKKYRDPRTHQHIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 203 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP- 281
Cdd:cd14125  160 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPs 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 530379706 282 EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGY 317
Cdd:cd14125  240 EFATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
43-316 3.55e-147

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 420.36  E-value: 3.55e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd14127    2 YKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIP 202
Cdd:cd14127   82 LEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGTKNANVIHVVDFGMAKQYRDPKTKQHIP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 203 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFP- 281
Cdd:cd14127  162 YREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPIRDLCEGFPe 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 530379706 282 EMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKG 316
Cdd:cd14127  242 EFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
43-308 5.98e-120

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 351.04  E-value: 5.98e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd14128    2 YRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL--IGRPGNKtqqvIHIIDFGLAKEYIDPETKKH 200
Cdd:cd14128   82 LEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLmgIGRHCNK----LFLIDFGLAKKYRDSRTRQH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 201 IPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENF 280
Cdd:cd14128  158 IPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGF 237
                        250       260
                 ....*....|....*....|....*....
gi 530379706 281 P-EMATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:cd14128  238 PaEFAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
42-309 1.41e-68

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: 219.05  E-value: 1.41e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLF-DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLAKEYIDPETKKH 200
Cdd:cd14017   81 NLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERT-VYILDFGLARQYTNKDGEVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 201 IPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKadtlkeRYQKIGDTKRATPIEVLCENF 280
Cdd:cd14017  160 RPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKIDHEELLKGL 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 530379706 281 P-EMATYLRYVRRLDFFEKPDYDYLRKLFT 309
Cdd:cd14017  234 PkEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
38-308 8.53e-49

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 169.00  E-value: 8.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFGELRLGKNLYTN------EYVaIKLEPmKSRAPqLHLEYRFYKQLGSGD-------------- 97
Cdd:cd14015    7 VTKRQWKLGKSIGQGGFGEIYLASDDSTLsvgkdaKYV-VKIEP-HSNGP-LFVEMNFYQRVAKPEmikkwmkakklkhl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  98 GIPQVYYFG----PCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrp 173
Cdd:cd14015   84 GIPRYIGSGsheyKGEKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLG-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 174 GNKTQQVIHIIDFGLAKEYIDpeTKKHIPYRE--HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14015  162 FGKNKDQVYLVDYGLASRYCP--NGKHKEYKEdpRKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWED 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 252 LKADTLKERYQKIgdtKRATPI-EVLCENFP------EMATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:cd14015  240 NLKNPEYVQKQKE---KYMDDIpLLLKKCFPgkdvpeELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
43-313 6.26e-39

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 141.73  E-value: 6.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd14129    2 WKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14129   82 LADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKC-YMLDFGLARQFTNSCGDVRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PyREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATPIEVLCENF- 280
Cdd:cd14129  161 P-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYEHRLMLKHLp 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 530379706 281 PEMATYLRYVRRLDFFEKPDYdylrKLFTDLFD 313
Cdd:cd14129  234 PEFSVFLDHISGLDYFTKPDY----QLLVSVFD 262
CK1gamma_C pfam12605
Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically ...
328-417 1.22e-38

Casein kinase 1 gamma C terminal; This domain family is found in eukaryotes, and is typically between 54 and 99 amino acids in length. The family is found in association with pfam00069. CK1gamma is a membrane-bound member of the CK1 family. Gain-of-function and loss-of-function experiments show that CK1gamma is both necessary and sufficient to transduce LRP6 signalling in vertebrates and Drosophila cells.


Pssm-ID: 463640  Cd Length: 99  Bit Score: 135.39  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  328 KQLPTPVGAVQ-QDPALSSNREAHQHRDK------MQQSKNQSADHRAAW--DSQQANPHHLRAHLAADRHGGSVQVVSS 398
Cdd:pfam12605   1 KPMPTPVGSLQtSESAVSPSREAHIGVSRpplpqpRRVSQQGSKGRKGAWppPTPQTNAETLGSHLPADRHGGSVQVVSS 80
                          90
                  ....*....|....*....
gi 530379706  399 TNGELNTDDPTAGRSNAPI 417
Cdd:pfam12605  81 TNGELNTDDPTAGHSNAPI 99
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
43-308 1.36e-38

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 140.55  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd14130    2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNkTQQVIHIIDFGLAKEYIDpETKKHI 201
Cdd:cd14130   82 LADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPS-TYRKCYMLDFGLARQYTN-TTGEVR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADtlkeryQKIGDTKRATPIEVLCENFP 281
Cdd:cd14130  160 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK------EQVGMIKEKYEHRMLLKHMP 233
                        250       260
                 ....*....|....*....|....*...
gi 530379706 282 -EMATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:cd14130  234 sEFHLFLDHIASLDYFTKPDYQLIMSVF 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
49-242 1.57e-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: 128.16  E-value: 1.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELL-GPSLE 124
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKvipKEKLKKLLEELLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCeGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIPYR 204
Cdd:cd00180   80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT-----VKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530379706 205 ehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYF 242
Cdd:cd00180  155 -----TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
43-274 6.82e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 122.25  E-value: 6.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706    43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSgDGIPQVYYFGPCGKYNAMVLELL 119
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   120 gpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPET 197
Cdd:smart00220  80 --EGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-----VKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706   198 kkhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLKERYQKIGDTKRATPIE 274
Cdd:smart00220 153 --------LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
39-251 1.62e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.20  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  39 VGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQ----LHLEYRFYKQLgSGDGIPQVYYFGPCGKYNA 113
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKvLRPELAADPEarerFRREARALARL-NHPNIVRVYDVGEEDGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 192
Cdd:COG0515   84 LVMEYVeGESLADLLRR-RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDG-----RVKLIDFGIARAL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 IDPETKkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:COG0515  158 GGATLT------QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDG 210
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
42-251 1.86e-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: 118.46  E-value: 1.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHL----EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKvLRPELAEDEEFRErflrEARALARL-SHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDP 195
Cdd:cd14014   80 EYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR-----VKLTDFGIARA-LGD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 196 ETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14014  153 SGLTQT-----GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDG 203
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
43-308 2.56e-29

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024 [Multi-domain]  Cd Length: 301  Bit Score: 116.52  E-value: 2.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLG-----KNLYTNEYVAIKLEPmkSRAPQLHLEYRFYKQLGSGD--------------GIPQVY 103
Cdd:cd14122   12 WKLGLPIGQGGFGRLYLAdenssESVGSDAPYVVKVEP--SDNGPLFTELKFYMRAAKPDqiqkwikshklkylGVPKYW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 104 YFGPCGK----YNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQ 179
Cdd:cd14122   90 GSGLHEKngksYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLL---SYKNPD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 180 VIHIIDFGLAKEYID---PETKKHIPYREHKsltGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADT 256
Cdd:cd14122  167 QVYLVDYGLAYRYCPegvHKEYKEDPKRCHD---GTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWEDNLKDP 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 257 LKERYQKIgdTKRATPIEVLCENFP------EMATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:cd14122  244 NYVRDSKI--RYRDNISELMEKCFPgknkpgEIRKYMETVKLLGYTEKPLYPHLREIL 299
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
38-309 2.51e-26

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025 [Multi-domain]  Cd Length: 302  Bit Score: 108.01  E-value: 2.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFGELRLGKNlYTNEYV------AIKLEPMKSrAPqLHLEYRFYKQLGSGD-------------- 97
Cdd:cd14123    9 TEKKNWRLGKMIGKGGFGLIYLASP-QVNVPVeddavhVIKVEYHEN-GP-LFSELKFYQRAAKPDtiskwmkskqldyl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  98 GIPQVYYFGPC----GKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRp 173
Cdd:cd14123   86 GIPTYWGSGLTefngTSYRFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 174 gnKTQQVIHIIDFGLAKEYIdpETKKHIPYREH--KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW-- 249
Cdd:cd14123  165 --RNPNEVYLADYGLSYRYC--PNGNHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeq 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 250 --------QGLKADTLKERYQKIgdTKRATPIEVLCenfpEMATYLRYVRRLDFFEKPDYDYLRKLFT 309
Cdd:cd14123  241 nlknpvavQEAKAKLLSNLPDSV--LKWSTGGSSSM----EIAQFLSRVKDLAYDEKPDYQALKKILS 302
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
90-306 9.31e-26

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 106.47  E-value: 9.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  90 YKQLGSGD--GIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPEN 167
Cdd:cd14124   73 WKKLHSTDllGIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAEN 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 168 FLIgRPGNKTQqvIHIIDFGLAKEYIdpETKKHIPYRE-HKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRG 245
Cdd:cd14124  153 IFV-DPEDQSE--VYLAGYGFAFRYC--PGGKHVEYREgSRSPhEGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTG 227
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 246 SLPWQGLKADT-----LKERY-QKIGDT-----KRATPIEVLCEnfpematYLRYVRRLDFFEKPDYDYLRK 306
Cdd:cd14124  228 SLPWSNLLHNTedimkQKERFmDDVPGFlgpcfHQKKVSEALQK-------YLKVVMALQYEEKPDYAMLRN 292
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
38-308 8.93e-24

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 100.80  E-value: 8.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFG---ELRLGKNLYTNEYVAIKLEPMKSRApqLHLEYRFYKQLGSGD--------------GIP 100
Cdd:PHA02882   9 ITGKEWKIDKLIGCGGFGcvyETQCASDHCINNQAVAKIENLENET--IVMETLVYNNIYDIDkialwknihnidhlGIP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 101 QvyYFGpCG--KYNAM-----VLELLGPSLEDLFDLCdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrp 173
Cdd:PHA02882  87 K--YYG-CGsfKRCRMyyrfiLLEKLVENTKEIFKRI-KCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMV--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 174 gnKTQQVIHIIDFGLAKEYIdpETKKHIPY-REHKSL-TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:PHA02882 160 --DGNNRGYIIDYGIASHFI--IHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKG 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 252 LKADTLKERYQKIGDTKRATPIEVLCENFPE-MATYLRYVRRLDFFEKPDYDYLRKLF 308
Cdd:PHA02882 236 FGHNGNLIHAAKCDFIKRLHEGKIKIKNANKfIYDFIECVTKLSYEEKPDYDALIKIF 293
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
43-196 7.15e-21

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: 91.53  E-value: 7.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKlepmKSRAPQLHL-----EYRFYKQLGSGDGIPQV-----YYFGPCGKYN 112
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIK----KIKNDFRHPkaalrEIKLLKHLNDVEGHPNIvklldVFEHRGGNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEY 192
Cdd:cd05118   77 CLVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI----NLELGQLKLADFGLARSF 152

                 ....
gi 530379706 193 IDPE 196
Cdd:cd05118  153 TSPP 156
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
42-264 2.35e-20

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: 90.23  E-value: 2.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRA-PQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidKKKLKSEDeEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LL--GpsleDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKEYI 193
Cdd:cd05117   80 LCtgG----ELFDrIVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDS--PIKIIDFGLAKIFE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 194 DPEtkkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMYF-LRGSLPWQGlkaDTLKERYQKI 264
Cdd:cd05117  154 EGE--------KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLG-VILYIlLCGYPPFYG---ETEQELFEKI 213
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
42-324 5.11e-20

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: 89.58  E-value: 5.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEpmKSR------APQLHLEYRFYKQLGSgDGIPQVYY-FGPCGK-Yn 112
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKvLD--KRHiikekkVKYVTIEKEVLSRLAH-PGIVKLYYtFQDESKlY- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 aMVLELL--GPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd05581   78 -FVLEYApnGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH-----IKITDFGTAK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 191 ----------EYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKER 260
Cdd:cd05581  150 vlgpdsspesTKGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRG---SNEYLT 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 261 YQKIgdTKRATPIevlCENFPEMAtylryvrrLDFFEKpdydylrKLFTDLFDRKGYMFDYEYD 324
Cdd:cd05581  227 FQKI--VKLEYEF---PENFPPDA--------KDLIQK-------LLVLDPSKRLGVNENGGYD 270
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
42-264 9.92e-20

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: 88.34  E-value: 9.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPmKSRAPQLHLEY-----------------RFYKQLGSGDGIpqvyy 104
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIID-KSKLKEEIEEKikreieimkllnhpniiKLYEVIETENKI----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 105 fgpcgkynAMVLELLgpSLEDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIH 182
Cdd:cd14003   75 --------YLVMEYA--SGGELFDYIvnNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN-----LK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 183 IIDFGLAKEYidpetkkhIPYREHKSLTGTARYMS---INTH--LGKEQsrrdDLEALGHMfMYF-LRGSLPWQGlkaDT 256
Cdd:cd14003  140 IIDFGLSNEF--------RGGSLLKTFCGTPAYAApevLLGRkyDGPKA----DVWSLGVI-LYAmLTGYLPFDD---DN 203

                 ....*...
gi 530379706 257 LKERYQKI 264
Cdd:cd14003  204 DSKLFRKI 211
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-264 7.57e-18

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: 82.56  E-value: 7.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL--GpsleDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd05123   70 LVLDYVpgG----ELFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH-----IKLTDFGLA 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 190 KEYIDPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 264
Cdd:cd05123  141 KELSSDGDRTY-------TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVL-LYeMLTGKPPFY---AENRKEIYEKI 205
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
42-249 4.60e-17

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: 80.64  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK----LEPMKSRAPQLHLEYRFYKQLGSgdgiPQ-VYYFGPC---GKYNa 113
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKevelSGDSEEELEALEREIRILSSLKH----PNiVRYLGTErteNTLN- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEY 192
Cdd:cd06606   76 IFLEYVpGGSLASLLKKFGK-LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVD-----SDGVVKLADFGCAKRL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 193 IDPETKKhipyrEHKSLTGTARYMS---INthlGKEQSRRDDLEALG----HMFMyflrGSLPW 249
Cdd:cd06606  150 AEIATGE-----GTKSLRGTPYWMApevIR---GEGYGRAADIWSLGctviEMAT----GKPPW 201
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
42-346 1.31e-16

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: 79.93  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKlepMKSRAPQLHLeyrfyKQ----------LGSGDGIPQVYYFGPC--G 109
Cdd:cd05580    2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALK---ILKKAKIIKL-----KQvehvlnekriLSEVRHPFIVNLLGSFqdD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLELL--GpsleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIID 185
Cdd:cd05580   74 RNLYMVMEYVpgG----ELFSLLRRSgrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH-----IKITD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 186 FGLAKeYIDPETkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKERYQKI- 264
Cdd:cd05580  145 FGFAK-RVKDRT---------YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPF---FDENPMKIYEKIl 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 265 -GDTKratpievlcenFPEmatylryvrrldFFEKPDYDYLRKLFT-DLFDRKGYM-----------FDYEYDWIG---K 328
Cdd:cd05580  212 eGKIR-----------FPS------------FFDPDAKDLIKRLLVvDLTKRLGNLkngvediknhpWFAGIDWDAllqR 268
                        330
                 ....*....|....*...
gi 530379706 329 QLPTPVGAVQQDPALSSN 346
Cdd:cd05580  269 KIPAPYVPKVRGPGDTSN 286
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
42-307 3.09e-16

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: 78.49  E-value: 3.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYfgpcgkYNAMV------ 115
Cdd:cd13996    7 DFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRY------YTAWVeepply 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 --LELL-GPSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAK 190
Cdd:cd13996   81 iqMELCeGGTLRDWIDRRNSSSKNdrKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL----DNDDLQVKIGDFGLAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 191 EYIDPETKKHIP-------YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFLRgslpwqglkaDTLKERY 261
Cdd:cd13996  157 SIGNQKRELNNLnnnnngnTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILfeMLHPF----------KTAMERS 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530379706 262 QKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPD-YDYLRKL 307
Cdd:cd13996  227 TILTDLRNGILPESFKAKHPKEADLIQSLLSKNPEERPSaEQLLRSL 273
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
42-318 8.20e-16

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 77.48  E-value: 8.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKS--RAPQ---LHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEviRLKQeqhVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYMLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELLgPSLEdLFDL--CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID 194
Cdd:cd05612   81 EYV-PGGE-LFSYlrNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH-----IKLTDFGFAKKLRD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 195 petkkhipyrEHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIgdtkratpie 274
Cdd:cd05612  154 ----------RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD---DNPFGIYEKI---------- 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 530379706 275 vlcenfpeMATYLRYVRRLDFFEKpdyDYLRKLFT-DLFDRKGYM 318
Cdd:cd05612  211 --------LAGKLEFPRHLDLYAK---DLIKKLLVvDRTRRLGNM 244
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
47-264 2.18e-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: 75.98  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEP-----MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELL-G 120
Cdd:cd05611    2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKksdmiAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLnG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyiDPETKKH 200
Cdd:cd05611   82 GDCASLIKTLG-GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGH-----LKLTDFGLSR---NGLEKRH 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 201 ipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 264
Cdd:cd05611  153 -----NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH---AETPDAVFDNI 208
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
42-217 3.48e-15

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: 75.46  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK----------LEPMKSRAPQLHlEYRFYKQLGSGDGIPQVYYFGPCGKY 111
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKclyksgpnskDGNDFQKLPQLR-EIDLHRRVSRHPNIITLHDVFETEVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 112 NAMVLELLgpSLEDLFDLC--DRTFSLKTVLM--IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqVIHIIDFG 187
Cdd:cd13993   80 IYIVLEYC--PNGDLFEAIteNRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEG----TVKLCDFG 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 530379706 188 LAkeyidpeTKKHIPYrehKSLTGTARYMS 217
Cdd:cd13993  154 LA-------TTEKISM---DFGVGSEFYMA 173
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
46-249 8.32e-15

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: 74.26  E-value: 8.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRA-PQLHLEY------------RFYkqlgsgdGIP----QVYYF 105
Cdd:cd06626    5 GNKIGEGTFGKVYTAVNLDTGELMAmkeIRFQDNDPKTiKEIADEMkvlegldhpnlvRYY-------GVEvhreEVYIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 106 gpcgkynamvLELL-GPSLEDLfdlCDRTFSL-KTVLMI-AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIH 182
Cdd:cd06626   78 ----------MEYCqEGTLEEL---LRHGRILdEAVIRVyTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG-----LIK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 183 IIDFGLAKEYIDPETKkhIPYREHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06626  140 LGDFGSAVKLKNNTTT--MAPGEVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
43-206 1.48e-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: 73.67  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKlepmksrapQLHLEYRfykqlgsGDGIPQ--------------------- 101
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK---------KIRLDNE-------EEGIPStalreisllkelkhpnivkll 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 102 -VYYfgpCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqV 180
Cdd:cd07829   65 dVIH---TENKLYLVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDG-----V 136
                        170       180
                 ....*....|....*....|....*.
gi 530379706 181 IHIIDFGLAKEYidpetkkHIPYREH 206
Cdd:cd07829  137 LKLADFGLARAF-------GIPLRTY 155
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
43-191 2.30e-14

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: 73.34  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKlePMKSRAPQLH-----LEYRFYKQLGSGDGIPQVY---------YFgpc 108
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIK--KMKKKFYSWEecmnlREVKSLRKLNEHPNIVKLKevfrendelYF--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 gkynamVLELLGPSLEDLF-DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFG 187
Cdd:cd07830   76 ------VFEYMEGNLYQLMkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV-----SGPEVVKIADFG 144

                 ....
gi 530379706 188 LAKE 191
Cdd:cd07830  145 LARE 148
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
49-217 3.12e-14

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: 72.19  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKnlYTNEYVAIKLepMKSRAPQLHLEYRFYKQLgsgdgipQVY----------YFGPC--GKYNAMVL 116
Cdd:cd13999    1 IGSGSFGEVYKGK--WRGTDVAIKK--LKVEDDNDELLKEFRREV-------SILsklrhpnivqFIGAClsPPPLCIVT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID 194
Cdd:cd13999   70 EYMpGGSLYDLLHKKKIPLSWSLRLKIALD-IARgMNYLHSPPIIHRDLKSLNILLDENFT-----VKIADFGLSRIKNS 143
                        170       180
                 ....*....|....*....|...
gi 530379706 195 PETKKhipyrehKSLTGTARYMS 217
Cdd:cd13999  144 TTEKM-------TGVVGTPRWMA 159
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
42-264 3.25e-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: 72.12  E-value: 3.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKsrapQLhLEYRFYKQLG---------SGDGIPQVY-YFgpcgkY 111
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKS----QL-QKSGLEHQLRreieiqshlRHPNILRLYgYF-----E 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 112 NA----MVLELLgpSLEDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIID 185
Cdd:cd14007   71 DKkriyLILEYA--PNGELYKELKKQkrFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG-----SNGELKLAD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 186 FGLAkeyidpetkKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKI 264
Cdd:cd14007  144 FGWS---------VHAPSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLG-VLCYeLLVGKPPF---ESKSHQETYKRI 210
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
42-275 3.48e-14

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: 72.30  E-value: 3.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEpMKSRAPQLHLEYRFYKQLGSGDGI--PQV-----YYFGPCGKYnaM 114
Cdd:cd14116    6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVL-FKAQLEKAGVEHQLRREVEIQSHLrhPNIlrlygYFHDATRVY--L 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELlGPSLEDLFDL--CDRTFSLKTVLMIaIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkey 192
Cdd:cd14116   83 ILEY-APLGTVYRELqkLSKFDEQRTATYI-TELANALSYCHSKRVIHRDIKPENLLLGSAGE-----LKIADFGWS--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 193 idpetkKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATP 272
Cdd:cd14116  153 ------VHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFE---ANTYQETYKRISRVEFTFP 223

                 ...
gi 530379706 273 IEV 275
Cdd:cd14116  224 DFV 226
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
43-249 5.61e-14

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: 71.59  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAP----QLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLEL 118
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcpeNIKKEVCIQKML-SHKNVVRFYGHRREGEFQYLFLEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LgpSLEDLFD-----------LCDRTFSlktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFG 187
Cdd:cd14069   82 A--SGGELFDkiepdvgmpedVAQFYFQ---------QLMAGLKYLHSCGITHRDIKPENLLLDENDN-----LKISDFG 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 188 LAKEYIDPETKkhipyREHKSLTGTARYMSINThLGKEQSRRD--DLEALGHMFMYFLRGSLPW 249
Cdd:cd14069  146 LATVFRYKGKE-----RLLNKMCGTLPYVAPEL-LAKKKYRAEpvDVWSCGIVLFAMLAGELPW 203
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
39-191 7.10e-14

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: 71.76  E-value: 7.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  39 VGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPM----KSRAPQ----------LHLEYRFYKQLGSGDgipQVYY 104
Cdd:cd14137    2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQdkryKNRELQimrrlkhpniVKLKYFFYSSGEKKD---EVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 105 FgpcgkynaMVLELLGPSLEDL---FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVI 181
Cdd:cd14137   79 N--------LVMEYMPETLYRVirhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV----DPETGVL 146
                        170
                 ....*....|
gi 530379706 182 HIIDFGLAKE 191
Cdd:cd14137  147 KLCDFGSAKR 156
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
110-264 8.34e-14

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: 71.10  E-value: 8.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLEL-LGpslEDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDF 186
Cdd:cd05572   66 KYLYMLMEYcLG---GELWTiLRDRgLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNG-----YVKLVDF 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 187 GLAKeYIDPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKeRYQKI 264
Cdd:cd05572  138 GFAK-KLGSGRKTW-------TFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMK-IYNII 206
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
42-264 1.21e-13

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 71.93  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKIlrksDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LL-GPSLEDLfdLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID- 194
Cdd:cd05573   82 YMpGGDLMNL--LIKYdVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGH-----IKLADFGLCTKMNKs 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 195 -----------------PETKKHIPYREHK----SLTGTARYMSINTHLGKEQSRRDDLEALGhMFMY-FLRGSLPwqgL 252
Cdd:cd05573  155 gdresylndsvntlfqdNVLARRRPHKQRRvraySAVGTPDYIAPEVLRGTGYGPECDWWSLG-VILYeMLYGFPP---F 230
                        250
                 ....*....|..
gi 530379706 253 KADTLKERYQKI 264
Cdd:cd05573  231 YSDSLVETYSKI 242
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
43-217 1.44e-13

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: 70.37  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSgDGIpqVYYFGpCGKYNAMVLELL--- 119
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDS-PYI--VKYYG-SYFKNTDLWIVMeyc 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETK 198
Cdd:cd06612   81 gAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ-----AKLADFGVSGQLTDTMAK 155
                        170
                 ....*....|....*....
gi 530379706 199 KhipyrehKSLTGTARYMS 217
Cdd:cd06612  156 R-------NTVIGTPFWMA 167
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
48-246 3.61e-13

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: 69.67  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIKLEPMKSR----APQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd07832    7 RIGEGAHGIVFKAKDRETGETVALKKVALRKLeggiPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLSSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKkhiPY 203
Cdd:cd07832   87 SEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG-----VLKIADFGLARLFSEEDPR---LY 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530379706 204 REHkslTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGS 246
Cdd:cd07832  159 SHQ---VATRWYRAPELLYGSRKyDEGVDLWAVGCIFAELLNGS 199
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
42-260 7.23e-13

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: 68.32  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAP----QLHLEYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLE 117
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPsslqKLFREVRIMKILNHPN-IVKLFEVIETEKTLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LlgPSLEDLFDLCDRTFSLKTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidp 195
Cdd:cd14072   80 Y--ASGGEVFDYLVAHGRMKEKEARAKfrQIVSAVQYCHQKRIVHRDLKAENLLLDADMN-----IKIADFGFSNEF--- 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 196 etkkhIPYREHKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 260
Cdd:cd14072  150 -----TPGNKLDTFCGSPPYAAPELFQGKKYDGPEvDVWSLGVILYTLVSGSLPFDGQNLKELRER 210
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
49-274 1.08e-12

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: 67.96  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKlEPMKSRAPQLhleyRFYKQLGSGDGIP-----------------------QVYYF 105
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIK-IFNKSRLRKR----REGKNDRGKIKNAlddvrreiaimkkldhpnivrlyEVIDD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 106 GPCGK-YnaMVLELL--GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIH 182
Cdd:cd14008   76 PESDKlY--LVLEYCegGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG-----TVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 183 IIDFGLAKEYIDPETkkhipyrEHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqglKADTLKE 259
Cdd:cd14008  149 ISDFGVSEMFEDGND-------TLQKTAGTPAFLApelCDGDSKTYSGKAADIWALGVTLYCLVFGRLPF---NGDNILE 218
                        250
                 ....*....|....*
gi 530379706 260 RYQKIGDTKRATPIE 274
Cdd:cd14008  219 LYEAIQNQNDEFPIP 233
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
42-217 2.42e-12

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: 66.97  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK----LEPMKSRAPQLHL-EYRFYKQLGSGDGIPQVYYFGPCGKYNaMVL 116
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqiFEMMDAKARQDCVkEIDLLKQLNHPNVIKYLDSFIEDNELN-IVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELlgPSLEDL------FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd08228   82 EL--ADAGDLsqmikyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLGR 154
                        170       180
                 ....*....|....*....|....*..
gi 530379706 191 EYIDPETKKHipyrehkSLTGTARYMS 217
Cdd:cd08228  155 FFSSKTTAAH-------SLVGTPYYMS 174
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
42-236 2.70e-12

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: 66.51  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ----LHLEYRFYKQLGSGDGIPQVYYFGPCGKYNaMVLE 117
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKelrnLRQEIEILRKLNHPNIIEMLDSFETKKEFV-VVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LlgpSLEDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyidp 195
Cdd:cd14002   81 Y---AQGELFQILedDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGG-----VVKLCDFGFARA---- 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 530379706 196 etkkhIPYREH--KSLTGTARYMSinTHLGKEQ--SRRDDLEALG 236
Cdd:cd14002  149 -----MSCNTLvlTSIKGTPLYMA--PELVQEQpyDHTADLWSLG 186
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
43-189 3.12e-12

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 67.20  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLhlEYRFYKQLGSGD--GIPQV--------YYFGPCg 109
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIirnVEKYREAAKI--EIDVLETLAEKDpnGKSHCvqlrdwfdYRGHMC- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 kynaMVLELLGPSLED-LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL--------IGRPGNKTQQV 180
Cdd:cd14134   91 ----IVFELLGPSLYDfLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkVYNPKKKRQIR 166
                        170
                 ....*....|....*
gi 530379706 181 ------IHIIDFGLA 189
Cdd:cd14134  167 vpkstdIKLIDFGSA 181
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
41-251 5.62e-12

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: 65.88  E-value: 5.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  41 PNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL-----EPMKSRAPQLHL-----EYRFYKQLgSGDGIPQVYYFGPCGK 110
Cdd:cd14084    6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIinkrkFTIGSRREINKPrnietEIEILKKL-SHPCIIKIEDFFDAED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAMVLELLGPSleDLFDLCDRTFSLK--TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTQQVIHIIDFGL 188
Cdd:cd14084   85 DYYIVLELMEGG--ELFDRVVSNKRLKeaICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLS--SQEEECLIKITDFGL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 189 AKeyIDPETKKhipyreHKSLTGTARYMS--INTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14084  161 SK--ILGETSL------MKTLCGTPTYLApeVLRSFGTEGyTRAVDCWSLGVILFICLSGYPPFSE 218
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
43-187 5.85e-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: 65.75  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGD-----GIPQVY---YFgpcgkYN- 112
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKiIKNNKDYLDQSLDEIRLLELLNKKDkadkyHIVRLKdvfYF-----KNh 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 113 -AMVLELLGPSLEDLFDLcDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvIHIIDFG 187
Cdd:cd14133   76 lCIVFELLSQNLYEFLKQ-NKFqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ---IKIIDFG 149
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
49-277 6.30e-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: 65.80  E-value: 6.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEY-VAIKLEPMKSRAPQLHL---EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELL-GPSL 123
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLlgkEIKILKEL-KHENIVALYDFQEIANSVYLVMEYCnGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFDlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI----GRPGNKTQQVIHIIDFGLAKeYIDPETKK 199
Cdd:cd14202   89 ADYLH-TMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIADFGFAR-YLQNNMMA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 200 hipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLC 277
Cdd:cd14202  167 -------ATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSS 237
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
46-204 6.40e-12

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 65.63  E-value: 6.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706    46 GKKIGCGNFGELRLGK----NLYTNEYVAIKLepMKSRAPQLHL-----EYRFYKQLgSGDGIpqVYYFGPCGKYNA--M 114
Cdd:smart00219   4 GKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKT--LKEDASEQQIeeflrEARIMRKL-DHPNV--VKLLGVCTEEEPlyI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   115 VLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK-- 190
Cdd:smart00219  79 VMEYMeGGDLLSYLRKNRPKLSLSDLLSFALQ-IARgMEYLESKNFIHRDLAARNCLVGE-----NLVVKISDFGLSRdl 152
                          170
                   ....*....|....*..
gi 530379706   191 ---EYIDPETKKhIPYR 204
Cdd:smart00219 153 yddDYYRKRGGK-LPIR 168
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
42-253 6.86e-12

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: 65.69  E-value: 6.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSG--DGIPQVY--YFGPCgkYNAMVLE 117
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCesPYVVKCYgaFYKEG--EISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LL-GPSLEDLFDLCdRTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDP 195
Cdd:cd06623   80 YMdGGSLADLLKKV-GKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE-----VKIADFGISKV-LEN 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 196 ETKKhipyreHKSLTGTARYMS---INthlGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 253
Cdd:cd06623  153 TLDQ------CNTFVGTVTYMSperIQ---GESYSYAADIWSLGLTLLECALGKFPFLPPG 204
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
44-204 8.00e-12

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: 65.26  E-value: 8.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706    44 RVGKKIGCGNFGELRLGK----NLYTNEYVAIKLepMKSRAPQLHL-----EYRFYKQLgSGDGIpqVYYFGPCGKYNA- 113
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKT--LKEDASEQQIeeflrEARIMRKL-DHPNI--VKLLGVCTEEEPl 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   114 -MVLELL-GPSLED-LFDLCDRTFSLKTVLMIAIQlISR-MEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLA 189
Cdd:smart00221  77 mIVMEYMpGGDLLDyLRKNRPKELSLSDLLSFALQ-IARgMEYLESKNFIHRDLAARNCLVGE-----NLVVKISDFGLS 150
                          170       180
                   ....*....|....*....|
gi 530379706   190 KE-----YIDPETKKhIPYR 204
Cdd:smart00221 151 RDlydddYYKVKGGK-LPIR 169
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
40-208 1.22e-11

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: 64.58  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  40 GPnFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEP----MKSRAPQ-LHLEYRFYKqLGSGDGIPQVYYFGPCGKYNAM 114
Cdd:cd14081    1 GP-YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNkeklSKESVLMkVEREIAIMK-LIEHPNVLKLYDVYENKKYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLgpSLEDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-- 190
Cdd:cd14081   79 VLEYV--SGGELFDyLVKKgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL-----DEKNNIKIADFGMASlq 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 530379706 191 -------------EYIDPETKKHIPYREHKS 208
Cdd:cd14081  152 pegslletscgspHYACPEVIKGEKYDGRKA 182
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
42-189 1.42e-11

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: 64.33  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepMKSRA-----PQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd14078    4 YYELHETIGSGGFAKVKLATHILTGEKVAIKI--MDKKAlgddlPRVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 117 ELLgPSLEdLFDLC---DRTFSLKTVLMIAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd14078   81 EYC-PGGE-LFDYIvakDRLSEDEARVFFR-QIVSAVAYVHSQGYAHRDLKPENLLLDEDQN-----LKLIDFGLC 148
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
145-272 1.72e-11

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: 65.11  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMS---INTH 221
Cdd:cd05582  105 ELALALDHLHSLGIIYRDLKPENILLDEDGH-----IKLTDFGLSKESIDHEKKAY-------SFCGTVEYMApevVNRR 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530379706 222 lGKEQSRrdDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKIGDTKRATP 272
Cdd:cd05582  173 -GHTQSA--DWWSFGVLMFEMLTGSLPFQG---KDRKETMTMILKAKLGMP 217
pknD PRK13184
serine/threonine-protein kinase PknD;
128-275 2.16e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 66.33  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 128 DLCDRTfSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqQVIhIIDFGLAK-----EYIDPETKKHIP 202
Cdd:PRK13184 105 ELAEKT-SVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVV-ILDWGAAIfkkleEEDLLDIDVDER 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 203 YREHKSLT------GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkadtlKERYQKIGDTKR-ATPIEV 275
Cdd:PRK13184 179 NICYSSMTipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR-------RKKGRKISYRDViLSPIEV 251
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
46-200 2.42e-11

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 63.67  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   46 GKKIGCGNFGELRLGK----NLYTNEYVAIKLepMKSRAPQLHL-----EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTlkgeGENTKIKVAVKT--LKEGADEEERedfleEASIMKKL-DHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE-YID 194
Cdd:pfam07714  81 EYMpGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL-----VVKISDFGLSRDiYDD 155

                  ....*.
gi 530379706  195 PETKKH 200
Cdd:pfam07714 156 DYYRKR 161
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
39-279 2.57e-11

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: 63.87  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  39 VGPNFrvgkkIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAP-QLHLEYRFYKQ-----LGSGDGIPQVYYFGPCGKYN 112
Cdd:cd13995    7 IGSDF-----IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPsDVEIQACFRHEniaelYGALLWEETVHLFMEAGEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMV--LELLGPSledlfdlcdRTFSlktVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVihIIDFGLAK 190
Cdd:cd13995   82 SVLekLESCGPM---------REFE---IIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF----MSTKAV--LVDFGLSV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 191 EYIDpetKKHIPyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIgDTKRA 270
Cdd:cd13995  144 QMTE---DVYVP----KDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYI-IHKQA 215

                 ....*....
gi 530379706 271 TPIEVLCEN 279
Cdd:cd13995  216 PPLEDIAQD 224
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
43-265 6.59e-11

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: 62.42  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL--------EPMKSrapQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNaM 114
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIidkeqvarEGMVE---QIKREIAIMKLLRHPNIVELHEVMATKTKIF-F 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGPSleDLFDLCDRTFSLK--TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA--K 190
Cdd:cd14663   78 VMELVTGG--ELFSKIAKNGRLKedKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN-----LKISDFGLSalS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 191 EYIDPETKKHipyrehkSLTGTARYMSinthlgKEQSRRD-------DLEALGHMFMYFLRGSLPWQglkADTLKERYQK 263
Cdd:cd14663  151 EQFRQDGLLH-------TTCGTPNYVA------PEVLARRgydgakaDIWSCGVILFVLLAGYLPFD---DENLMALYRK 214

                 ..
gi 530379706 264 IG 265
Cdd:cd14663  215 IM 216
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
43-264 1.30e-10

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: 61.80  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEP----MKSRAPQ-LHLEYRFYKQLGSgdgiPQVYYFGPC---GKYNAM 114
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPksslTKPKQREkLKSEIKIHRSLKH----PNIVKFHDCfedEENVYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLgpSLEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 192
Cdd:cd14099   79 LLELC--SNGSLMELLKRrkALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN-----VKIGDFGLAAR- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 193 IDPETKKhipyreHKSLTGTARYMS--InthLGKEQ--SRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 264
Cdd:cd14099  151 LEYDGER------KKTLCGTPNYIApeV---LEKKKghSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRI 214
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
43-248 1.39e-10

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: 61.46  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHL-EYRFYKQLGSgDGIpqVYYFGP--CGKYNAMVLELL 119
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIInEILIMKECKH-PNI--VDYYDSylVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTK 198
Cdd:cd06614   79 dGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS-----VKLADFGFAAQL----TK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530379706 199 KHiPYRehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06614  150 EK-SKR--NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
44-251 1.54e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.28  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  44 RVGKKIGCGNFGELRLGKNLYTNEYVAIKLepmksrapqLHLEY--------RFYK------QLgSGDGIPQVYYFGPCG 109
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKV---------LRPDLardpefvaRFRReaqsaaSL-SHPNIVSVYDVGEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 188
Cdd:NF033483  80 GIPYIVMEYVdGRTLKDYIRE-HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR-----VKVTDFGI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 189 AKEYidPETkkhipyrehkSLT------GTARYMSinthlgKEQSR------RDDLEALGHMfMY-FLRGSLPWQG 251
Cdd:NF033483 154 ARAL--SST----------TMTqtnsvlGTVHYLS------PEQARggtvdaRSDIYSLGIV-LYeMLTGRPPFDG 210
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
49-216 1.71e-10

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: 61.08  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAP----QLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELLgpSLE 124
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKklqeNLESEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYC--AGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKeYIDPETKKHip 202
Cdd:cd14009   78 DLSQYIRKRGRLpeAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDP--VLKIADFGFAR-SLQPASMAE-- 152
                        170
                 ....*....|....
gi 530379706 203 yrehkSLTGTARYM 216
Cdd:cd14009  153 -----TLCGSPLYM 161
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
131-249 1.73e-10

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: 61.95  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 210
Cdd:cd05595   89 ERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH-----IKITDFGLCKEGITDGATM-------KTFC 156
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530379706 211 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05595  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 195
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
43-195 2.12e-10

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 61.12  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELL 119
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIidkSKLKGKEDMIESEILIIKSL-SHPNIVKLFEVYETEKEIYLILEYV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 120 GPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLAKEYIDP 195
Cdd:cd14185   81 RGG--DLFDAIIESvkFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTT-LKLADFGLAKYVTGP 155
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
42-264 2.31e-10

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 61.76  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQ---------LHLEYRFYKQLGSGDGIPQVYYFgpc 108
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKClkkrEILKMKQVQhvaqeksilMELSHPFIVNMMCSFQDENRVYF--- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 gkynamVLE-LLGPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFG 187
Cdd:PTZ00263  96 ------LLEfVVGGELFTHLRKAGR-FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH-----VKVTDFG 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 188 LAKEyidpetkkhIPYREHkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 264
Cdd:PTZ00263 164 FAKK---------VPDRTF-TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFD---DTPFRIYEKI 227
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
42-264 2.46e-10

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: 60.64  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKS-----RAPQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAmqkagMVQRVRNEVEIHCQL-KHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidp 195
Cdd:cd14186   81 EMChNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN-----IKIADFGLA------ 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 196 eTKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 264
Cdd:cd14186  150 -TQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD---TDTVKNTLNKV 214
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
48-215 4.31e-10

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: 60.32  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVA---IKLE------PMKS-RAPQLHLEYRF-----YKQLGSGDGIPQVYyfgpcgkyn 112
Cdd:cd07843   12 RIEEGTYGVVYRARDKKTGEIVAlkkLKMEkekegfPITSlREINILLKLQHpnivtVKEVVVGSNLDKIY--------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 aMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEY 192
Cdd:cd07843   83 -MVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRG-----ILKICDFGLAREY 156
                        170       180
                 ....*....|....*....|....*....
gi 530379706 193 IDPeTKKHIP------YREHKSLTGTARY 215
Cdd:cd07843  157 GSP-LKPYTQlvvtlwYRAPELLLGAKEY 184
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
48-190 4.49e-10

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: 60.41  E-value: 4.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIKlePMKSRAPQLHL------EYRFYKQLGSGDGIPQVYYFGPCGKYNaMVLELLGP 121
Cdd:cd07833    8 VVGEGAYGVVLKCRNKATGEIVAIK--KFKESEDDEDVkktalrEVKVLRQLRHENIVNLKEAFRRKGRLY-LVFEYVER 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd07833   85 TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG-----VLKLCDFGFAR 148
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
43-195 4.64e-10

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 60.03  E-value: 4.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEYRFYKQLgSGDGIPQVY--YFGPCGKYnaMVLE 117
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIidkAKCKGKEHMIENEVAILRRV-KHPNIVQLIeeYDTDTELY--LVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LLgpSLEDLFDlcDRTFSLK-----TVLMIAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLAKEY 192
Cdd:cd14095   79 LV--KGGDLFD--AITSSTKfterdASRMVT-DLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSL-KLADFGLATEV 152

                 ...
gi 530379706 193 IDP 195
Cdd:cd14095  153 KEP 155
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
42-200 4.80e-10

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: 60.15  E-value: 4.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEP-------MKSRAPQLHLEYRFYKQLGSGDGIPQVYYFgP--CGKYN 112
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglKKEREKRLEKEISRDIRTIREAALSSLLNH-PhiCRLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 A--------MVLELLgpSLEDLFDLCDRTFSLKTVLM--IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIH 182
Cdd:cd14077   81 FlrtpnhyyMLFEYV--DGGQLLDYIISHGKLKEKQArkFARQIASALDYLHRNSIVHRDLKIENILISKSGN-----IK 153
                        170
                 ....*....|....*...
gi 530379706 183 IIDFGLAKEYiDPETKKH 200
Cdd:cd14077  154 IIDFGLSNLY-DPRRLLR 170
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
43-215 7.04e-10

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: 59.89  E-value: 7.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQL---------------GSGDGIPQVY 103
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkirMENEKEGFPITAIrEIKLLQKLdhpnvvrlkeivtskGSAKYKGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 104 yfgpcgkynaMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHI 183
Cdd:cd07840   81 ----------MVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV-----LKL 145
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530379706 184 IDFGLAKEYIDPE----TKKHIP--YREHKSLTGTARY 215
Cdd:cd07840  146 ADFGLARPYTKENnadyTNRVITlwYRPPELLLGATRY 183
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
114-264 7.61e-10

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: 60.11  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDL--FDLCDRTFSLktvlmiaiqlisrmEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd05584   89 MHLEREGIFMEDTacFYLAEITLAL--------------GHLHSLGIIYRDLKPENILLDAQGH-----VKLTDFGLCKE 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 192 YIDPETKKHipyrehkSLTGTARYMS--INTHLGkeQSRRDDLEALGHMfMY-FLRGSLPWQglkADTLKERYQKI 264
Cdd:cd05584  150 SIHDGTVTH-------TFCGTIEYMApeILTRSG--HGKAVDWWSLGAL-MYdMLTGAPPFT---AENRKKTIDKI 212
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
49-262 8.10e-10

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: 59.26  E-value: 8.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKS-RAPQLHLEYRFYKQLGSGDGIPQVY--YFGPCGKYnaMVLELLGPsLED 125
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStKLKDFLREYNISLELSVHPHIIKTYdvAFETEDYY--VFAQEYAP-YGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnKTQQVIHIIDFGL---------AKEYID 194
Cdd:cd13987   78 LFSIIPPQVGLpeERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFD---KDCRRVKLCDFGLtrrvgstvkRVSGTI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 195 P-------ETKKHIPYREHKSLtgtarymsinthlgkeqsrrdDLEALGHMFMYFLRGSLPWQglKADTLKERYQ 262
Cdd:cd13987  155 PytapevcEAKKNEGFVVDPSI---------------------DVWAFGVLLFCCLTGNFPWE--KADSDDQFYE 206
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
43-193 8.92e-10

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: 59.59  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepMK----SRAPQLHL-EYRFYKQLGSGDGIPQ---VYYFGPCGKYnAM 114
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKC--MKkhfkSLEQVNNLrEIQALRRLSPHPNILRlieVLFDRKTGRL-AL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnkTQQVIHIIDFGLAK---- 190
Cdd:cd07831   78 VFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI------KDDILKLADFGSCRgiys 151

                 ....*...
gi 530379706 191 -----EYI 193
Cdd:cd07831  152 kppytEYI 159
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
47-249 9.12e-10

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: 59.98  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKS---RAPQLH-----------LEYRFYKQLGSGDGIPQVYYFgpcgkyn 112
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTilkKKEQNHimaernvllknLKHPFLVGLHYSFQTSEKLYF------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 amVLELLGPSlEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd05603   74 --VLDYVNGG-ELFFHLQrERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH-----VVLTDFGLCKE 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 192 YIDPETKKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05603  146 GMEPEETT-------STFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
45-192 9.53e-10

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: 59.03  E-value: 9.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLG--KNLYTNEY---VAIKL-----EPMKSRAPQLHLEYRFYKQLGSGDgIPQVYYFGPCGKYNAM 114
Cdd:cd14076    5 LGRTLGEGEFGKVKLGwpLPKANHRSgvqVAIKLirrdtQQENCQTSKIMREINILKGLTHPN-IVRLLDVLKTKKYIGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGPSleDLFD--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd14076   84 VLEFVSGG--ELFDyiLARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRN-----LVITDFGFANTF 156
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
145-264 1.08e-09

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: 59.15  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKH--------IPYREHKSLTGTARYM 216
Cdd:cd05579  101 EIVLALEYLHSHGIIHRDLKPDNILIDANGH-----LKLTDFGLSKVGLVRRQIKLsiqkksngAPEKEDRRIVGTPDYL 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 217 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 264
Cdd:cd05579  176 APEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHA---ETPEEIFQNI 220
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
48-236 1.10e-09

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: 59.67  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIKlePMKSRAPQLH-------LEYRFYKQLGSGDGIPqvyYFGPCGKYNA--MVLEL 118
Cdd:cd06633   28 EIGHGSFGAVYFATNSHTNEVVAIK--KMSYSGKQTNekwqdiiKEVKFLQQLKHPNTIE---YKGCYLKDHTawLVMEY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkEYIDPETk 198
Cdd:cd06633  103 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ-----VKLADFGSA-SIASPAN- 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530379706 199 khipyrehkSLTGTARYMSINTHLGKEQSRRD---DLEALG 236
Cdd:cd06633  176 ---------SFVGTPYWMAPEVILAMDEGQYDgkvDIWSLG 207
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
42-264 1.22e-09

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: 58.95  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMK-SRAPQL---HLEYRFYKQLGSGDGIPQVYYFgPCGKYNAMVL 116
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKiLDKQKvVKLKQVehtLNEKRILQAINFPFLVKLEYSF-KDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyID 194
Cdd:cd14209   81 EYVPGG--EMFSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQG-----YIKVTDFGFAKR-VK 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 195 PETkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 264
Cdd:cd14209  153 GRT---------WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKI 210
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
42-198 1.35e-09

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: 59.12  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL----EYRFYKQLGSGDGIPQVYYFGPCGKYNaM 114
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKkikLGERKEAKDGINFtalrEIKLLQELKHPNIIGLLDVFGHKSNIN-L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYID 194
Cdd:cd07841   80 VFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDG-----VLKLADFGLARSFGS 154

                 ....
gi 530379706 195 PETK 198
Cdd:cd07841  155 PNRK 158
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
42-264 1.59e-09

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: 58.46  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEpmKSRAPQLHLEYRFYKQLGSgdgiPQVYYFGPCGKYNA---MVLE 117
Cdd:cd14010    1 NYVLYDEIGRGKHSVVYKGRRKGTIEFVAIKcVD--KSKRPEVLNEVRLTHELKH----PNVLKFYEWYETSNhlwLVVE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 L-LGPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID-- 194
Cdd:cd14010   75 YcTGGDLETLLRQ-DGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGT-----LKLSDFGLARREGEil 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 195 -------PETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMF--MYFlrGSLPWQglkADTLKERYQKI 264
Cdd:cd14010  149 kelfgqfSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLyeMFT--GKPPFV---AESFTELVEKI 222
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
42-217 1.61e-09

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: 58.44  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK----LEPM--KSRAPQLHlEYRFYKQLGSGDGIpqvyyfgpcgKYNAMV 115
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKkvqiFEMMdaKARQDCLK-EIDLLQQLNHPNII----------KYLASF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LEllGPSLEDLFDLCD---------------RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqV 180
Cdd:cd08224   70 IE--NNELNIVLELADagdlsrlikhfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG-----V 142
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530379706 181 IHIIDFGLAKeYIDPETKkhipyrEHKSLTGTARYMS 217
Cdd:cd08224  143 VKLGDLGLGR-FFSSKTT------AAHSLVGTPYYMS 172
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
131-299 1.63e-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: 58.73  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSlkTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKKHI-----PYRE 205
Cdd:cd14048  114 SRELF--VCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFF-----SLDDVVKVGDFGLVTAMDQGEPEQTVltpmpAYAK 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 206 HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLrgslpwqgLKADTLKERYQKIGDTKRATPIEVLCENFPEMAT 285
Cdd:cd14048  187 HTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI--------YSFSTQMERIRTLTDVRKLKFPALFTNKYPEERD 258
                        170
                 ....*....|....
gi 530379706 286 YLRYVRRLDFFEKP 299
Cdd:cd14048  259 MVQQMLSPSPSERP 272
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
125-263 1.69e-09

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: 58.47  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKhIP 202
Cdd:cd13994   84 DLFTLIekADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG-----VLKLTDFGTAEVFGMPAEKE-SP 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 203 YRehKSLTGTARYMSINTHLGKEQS-RRDDLEALGHMFMYFLRGSLPWQglKADTLKERYQK 263
Cdd:cd13994  158 MS--AGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWR--SAKKSDSAYKA 215
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
42-192 1.78e-09

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: 58.71  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRApqLHLEYRFYKQLGSGDGIPQVY--YFGPCGKYNAMVLE- 117
Cdd:cd14132   19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKvLKPVKKKK--IKREIKILQNLRGGPNIVKLLdvVKDPQSKTPSLIFEy 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 -------LLGPSLEDlFDLCDRTFslktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAK 190
Cdd:cd14132   97 vnntdfkTLYPTLTD-YDIRYYMY----------ELLKALDYCHSKGIMHRDVKPHNIMI----DHEKRKLRLIDWGLAE 161

                 ..
gi 530379706 191 EY 192
Cdd:cd14132  162 FY 163
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
114-217 1.93e-09

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: 58.13  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLgPSLEdLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd14093   86 LVFELC-RKGE-LFDYLTEvvTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN-----VKISDFGFATR 158
                         90       100
                 ....*....|....*....|....*.
gi 530379706 192 yIDPETKkhipYREhksLTGTARYMS 217
Cdd:cd14093  159 -LDEGEK----LRE---LCGTPGYLA 176
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
131-251 2.30e-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: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyidpeTKKHiPYREHKSLT 210
Cdd:cd05578   94 KVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGH-----VHITDFNIA-------TKLT-DGTLATSTS 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530379706 211 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd05578  161 GTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEI 201
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
47-215 2.38e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 58.29  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHL-EYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNETIAlkkIRLEQEDEGVPSTAIrEISLLKEMQHGN-IVRLQDVVHSEKRLYLVFEYLDLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqVIHIIDFGLAKEY-IDPETKKH 200
Cdd:PLN00009  87 LKKHMDSSpDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTN----ALKLADFGLARAFgIPVRTFTH 162
                        170
                 ....*....|....*....
gi 530379706 201 ----IPYREHKSLTGTARY 215
Cdd:PLN00009 163 evvtLWYRAPEILLGSRHY 181
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
42-236 3.10e-09

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: 57.73  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL-----EPmksRAPQLHLEYRFYKQLGSGDGIPQVY----YFGPCGKYN 112
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRmyfndEE---QLRVAIKEIEIMKRLCGHPNIVQYYdsaiLSSEGRKEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKN--LIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd13985   78 LLLMEYCPGSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR-----FKLCDFGSA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530379706 190 -KEYIDPETKKHIPYRE-----HKSLTGTARYMsINTHLGKEQSRRDDLEALG 236
Cdd:cd13985  153 tTEHYPLERAEEVNIIEeeiqkNTTPMYRAPEM-IDLYSKKPIGEKADIWALG 204
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
43-268 3.26e-09

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: 57.73  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLE-YRFYKQLGSGDGIPQVYyfgPCGKYNAMVLELL-G 120
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEiLLRYGQHPNIITLKDVY---DDGKHVYLVTELMrG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKEyidpetkk 199
Cdd:cd14175   80 GELLDKI-LRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNP--ESLRICDFGFAKQ-------- 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 200 hipYREHKSLTGTARYMS--INTHLGKEQSRRD--DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 268
Cdd:cd14175  149 ---LRAENGLLMTPCYTAnfVAPEVLKRQGYDEgcDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGK 218
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
43-187 3.53e-09

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: 57.94  E-value: 3.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSR-APQLHLEYRFYKQLGSGDgipqvyyfgPCGKYN--------- 112
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRfHQQALVEVKILKHLNDND---------PDDKHNivrykdsfi 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 -----AMVLELLGPSLEDLfdLCDRTF---SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQqvIHII 184
Cdd:cd14210   86 frghlCIVFELLSINLYEL--LKSNNFqglSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKSS--IKVI 160

                 ...
gi 530379706 185 DFG 187
Cdd:cd14210  161 DFG 163
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
42-216 3.82e-09

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: 57.01  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGEL-----RLGKNLYtneyvAIKLEPMKSRAPQlhlEYRFYKQ-------LGSGDGIPQVYYFGPCG 109
Cdd:cd13997    1 HFHELEQIGSGSFSEVfkvrsKVDGCLY-----AVKKSKKPFRGPK---ERARALReveahaaLGQHPNIVRYYSSWEEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLELL-GPSLEDLFDLCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDF 186
Cdd:cd13997   73 GHLYIQMELCeNGSLQDALEELSPISKLSEaeVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG-----TCKIGDF 147
                        170       180       190
                 ....*....|....*....|....*....|
gi 530379706 187 GLAKeyidpETKKHIPYREhksltGTARYM 216
Cdd:cd13997  148 GLAT-----RLETSGDVEE-----GDSRYL 167
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
48-239 4.12e-09

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: 57.71  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHLEYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLELLGPSLE 124
Cdd:cd07873    9 KLGEGTYATVYKGRSKLTDNLVAlkeIRLEHEEGAPCTAIREVSLLKDLKHAN-IVTLHDIIHTEKSLTLVFEYLDKDLK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYR 204
Cdd:cd07873   88 QYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLAR-------AKSIPTK 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530379706 205 EHKSLTGTARYMSINTHLGK-EQSRRDDLEALGHMF 239
Cdd:cd07873  156 TYSNEVVTLWYRPPDILLGStDYSTQIDMWGVGCIF 191
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
114-198 4.79e-09

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: 56.85  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSleDLFD-LCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqqvIHIIDFGLA 189
Cdd:cd14103   67 LVMEYVAGG--ELFErVVDDDFELteRDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQ----IKIIDFGLA 140

                 ....*....
gi 530379706 190 KEYiDPETK 198
Cdd:cd14103  141 RKY-DPDKK 148
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
42-257 5.24e-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: 57.63  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL--------------EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFgp 107
Cdd:cd05619    6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKAlkkdvvlmdddvecTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFF-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 108 cgkynamVLELL-GPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDF 186
Cdd:cd05619   84 -------VMEYLnGGDLMFHIQSCHK-FDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-----IKIADF 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 187 GLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05619  151 GMCKENMLGDAKT-------STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEEL 214
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
47-259 5.25e-09

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: 57.26  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIK--------------LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFgpcgkyn 112
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKalkkdvvlidddveCTMVEKRVLALAWENPFLTHLYCTFQTKEHLFF------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 amVLELL-GPSLedLFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd05620   74 --VMEFLnGGDL--MFHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-----IKIADFGMCK 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 191 EYIDPETKKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 259
Cdd:cd05620  145 ENVFGDNRA-------STFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFE 206
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
143-264 6.38e-09

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: 56.81  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHL 222
Cdd:cd05608  111 TAQIISGLEHLHQRRIIYRDLKPENVLLDDDGN-----VRISDLGLAVELKDGQTKT-------KGYAGTPGFMAPELLL 178
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530379706 223 GKEQSRRDDLEALGHMFMYFL--RGSLPWQGLKADTlKERYQKI 264
Cdd:cd05608  179 GEEYDYSVDYFTLGVTLYEMIaaRGPFRARGEKVEN-KELKQRI 221
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
48-192 6.52e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 56.67  E-value: 6.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd07839    7 KIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEGVPSSALrEICLLKELKHKN-IVRLYDVLHSDKKLTLVFEYCDQDL 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd07839   86 KKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE-----LKLADFGLARAF 149
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
43-189 6.90e-09

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 57.26  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepMKSRAP---QLHLEYRFYKQLGSgdgipqvyYFGPCGKYN------- 112
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKV--LKNKPAyfrQAMLEIAILTLLNT--------KYDPEDKHHivrlldh 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 -------AMVLELLGPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQvIHII 184
Cdd:cd14212   71 fmhhghlCIVFELLGVNLYELLKQNQfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN--LDSPE-IKLI 147

                 ....*
gi 530379706 185 DFGLA 189
Cdd:cd14212  148 DFGSA 152
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
126-259 8.18e-09

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: 56.38  E-value: 8.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidPETKKhipyre 205
Cdd:cd05577   84 IYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH-----VRISDLGLAVEF--KGGKK------ 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 206 HKSLTGTARYMSINTHLGKEQ-SRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 259
Cdd:cd05577  151 IKGRVGTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKE 205
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
125-206 8.44e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.40  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQqvIHIIDFGLAK------------ 190
Cdd:PHA03390  95 DLFDLLkkEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDR--AKDR--IYLCDYGLCKiigtpscydgtl 170
                         90
                 ....*....|....*.
gi 530379706 191 EYIDPETKKHIPYREH 206
Cdd:PHA03390 171 DYFSPEKIKGHNYDVS 186
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
46-217 1.22e-08

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: 55.87  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVAIK-----LEPMKSR--APQLHLEYRFYKQLGSgdgiPQ-VYYFGPCGKYNAM--V 115
Cdd:cd06632    5 GQLLGSGSFGSVYEGFNGDTGDFFAVKevslvDDDKKSResVKQLEQEIALLSKLRH----PNiVQYYGTEREEDNLyiF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LELL-GPSLEDLFDlcdRTFSLKTVLmIAI---QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAke 191
Cdd:cd06632   81 LEYVpGGSIHKLLQ---RYGAFEEPV-IRLytrQILSGLAYLHSRNTVHRDIKGANILVDTNG-----VVKLADFGMA-- 149
                        170       180
                 ....*....|....*....|....*..
gi 530379706 192 yidpetkKHIPYREH-KSLTGTARYMS 217
Cdd:cd06632  150 -------KHVEAFSFaKSFKGSPYWMA 169
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
41-188 1.33e-08

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: 55.74  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  41 PNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQ---------LHLEY-----RFYKQLGSGDGIPqvy 103
Cdd:cd14079    2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKIlnrQKIKSLDMEekirreiqiLKLFRhphiiRLYEVIETPTDIF--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 104 yfgpcgkynaMVLELLGPslEDLFDLCDRTFSLKTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvI 181
Cdd:cd14079   79 ----------MVMEYVSG--GELFDYIVQKGRLSEDEARRFfqQIISGVEYCHRHMVVHRDLKPENLLLDSNMN-----V 141

                 ....*..
gi 530379706 182 HIIDFGL 188
Cdd:cd14079  142 KIADFGL 148
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
47-263 1.35e-08

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: 55.62  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKnLYTNEY----VAIKLepMKSRAP-----QLHLEYRFYKQLGsgdgipqvyyfgpcgkyNAMVLE 117
Cdd:cd00192    1 KKLGEGAFGEVYKGK-LKGGDGktvdVAVKT--LKEDASeserkDFLKEARVMKKLG-----------------HPNVVR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LLGPSLED-----LFDLCDR--------------------TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGR 172
Cdd:cd00192   61 LLGVCTEEeplylVMEYMEGgdlldflrksrpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 173 PGnktqqVIHIIDFGLAkeyidpetKKHIPYREHKSLTGTA---RYM---SINTHLGKEQSrrdDLEALGhMFMY--FLR 244
Cdd:cd00192  141 DL-----VVKISDFGLS--------RDIYDDDYYRKKTGGKlpiRWMapeSLKDGIFTSKS---DVWSFG-VLLWeiFTL 203
                        250
                 ....*....|....*....
gi 530379706 245 GSLPWQGLKADTLKERYQK 263
Cdd:cd00192  204 GATPYPGLSNEEVLEYLRK 222
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
43-224 1.42e-08

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: 55.39  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHL----EYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLEL 118
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKrkleEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LGPSLEDLFDLCDRTfSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyIDPETK 198
Cdd:cd14050   83 CDTSLQQYCEETHSL-PESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDG-----VCKLGDFGLVVE-LDKEDI 155
                        170       180
                 ....*....|....*....|....*....
gi 530379706 199 KHIpyrehksLTGTARYMS---INTHLGK 224
Cdd:cd14050  156 HDA-------QEGDPRYMApelLQGSFTK 177
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
42-217 1.64e-08

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: 55.81  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK------LEPMKSRAPQLHlEYRFYKQLGSGDGIPQVYYFGPCGKYNaMV 115
Cdd:cd08229   25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKkvqifdLMDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELN-IV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LELLGPSleDL------FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLA 189
Cdd:cd08229  103 LELADAG--DLsrmikhFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG-----VVKLGDLGLG 175
                        170       180
                 ....*....|....*....|....*...
gi 530379706 190 KEYIDPETKKHipyrehkSLTGTARYMS 217
Cdd:cd08229  176 RFFSSKTTAAH-------SLVGTPYYMS 196
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
43-270 1.65e-08

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: 55.79  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRF-YKQLGSGDGIPQVYyfgPCGKYNAMVLELL-G 120
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLrYGQHPNIITLKDVY---DDGKFVYLVMELMrG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKEyidpetkk 199
Cdd:cd14178   82 GELLDRI-LRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNP--ESIRICDFGFAKQ-------- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 200 hipYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRA 270
Cdd:cd14178  151 ---LRAENGLLMTPCYTA--NFVAPEVLKRQgydaacDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYA 222
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
114-215 1.66e-08

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: 55.79  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 193
Cdd:cd07871   80 LVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE-----LKLADFGLARAKS 154
                         90       100
                 ....*....|....*....|....*...
gi 530379706 194 DPeTKKH------IPYREHKSLTGTARY 215
Cdd:cd07871  155 VP-TKTYsnevvtLWYRPPDVLLGSTEY 181
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
130-236 1.70e-08

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: 55.12  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 130 CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYidpeTKKHIPYrehkSL 209
Cdd:cd08220   94 KGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL----NKKRTVVKIGDFGISKIL----SSKSKAY----TV 161
                         90       100
                 ....*....|....*....|....*..
gi 530379706 210 TGTARYMSINTHLGKEQSRRDDLEALG 236
Cdd:cd08220  162 VGTPCYISPELCEGKPYNQKSDIWALG 188
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
131-198 1.76e-08

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: 55.79  E-value: 1.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqviHII--DFGLAKEYIDPETK 198
Cdd:cd05575   90 ERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQG-------HVVltDFGLCKEGIEPSDT 152
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
47-315 2.06e-08

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: 55.74  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMK---SRAPQLHLEYR---FYKQLGSGDGIPQVYYFGPCGKYnAMVLELLG 120
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAErnvLLKNVKHPFLVGLHYSFQTTDKL-YFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSlEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI---DPE 196
Cdd:cd05604   81 GG-ELFFHLQrERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH-----IVLTDFGLCKEGIsnsDTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 197 TkkhipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKR---ATPI 273
Cdd:cd05604  155 T----------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRpgiSLTA 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 530379706 274 EVLCENFPEMATYLRYVRRLDFFEKPDYDYLRKL-FTDLFDRK 315
Cdd:cd05604  225 WSILEELLEKDRQLRLGAKEDFLEIKNHPFFESInWTDLVQKK 267
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
49-220 2.07e-08

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: 55.53  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK-----LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELL---- 119
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqeLSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPNDLPLLamey 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 --GPSLEDLFDLCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIH-IIDFGLAKE--- 191
Cdd:cd13989   81 csGGDLRKVLNQPENCCGLKEseVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGR---VIYkLIDLGYAKEldq 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530379706 192 ------------YIDPETKKHIPYrehkslTGTARYMSINT 220
Cdd:cd13989  158 gslctsfvgtlqYLAPELFESKKY------TCTVDYWSFGT 192
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
42-217 2.26e-08

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: 55.40  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHL----EYRFYKQLGSGDGIP---QVYYFGPCGKYNA- 113
Cdd:cd07866    9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPItalrEIKILKKLKHPNVVPlidMAVERPDKSKRKRg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 ---MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd07866   89 svyMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG-----ILKIADFGLAR 163
                        170       180
                 ....*....|....*....|....*..
gi 530379706 191 EYIDPetkkhIPYREHKSLTGTARYMS 217
Cdd:cd07866  164 PYDGP-----PPNPKGGGGGGTRKYTN 185
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
49-238 2.44e-08

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: 54.80  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLgSGDGIpqVYYFGPC---GKYNAMVLELLGPSLED 125
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEVKLMRRL-SHPNI--LRFIGVCvkdNKLNFITEYVNGGTLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIhIIDFGLAKEYIDPETKKhiPYR- 204
Cdd:cd14065   78 LLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLV-REANRGRNAV-VADFGLAREMPDEKTKK--PDRk 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 530379706 205 EHKSLTGTARYMSINTHLGKEQSRRDDLEALGHM 238
Cdd:cd14065  154 KRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
46-306 2.44e-08

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: 54.85  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-----------LHLEYRFYKQLgSGDGIPQvyYFGPC--GKYN 112
Cdd:cd06628    5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmldaLQREIALLREL-QHENIVQ--YLGSSsdANHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELL-GPSLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd06628   82 NIFLEYVpGGSVATLLNNYG-AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG-----IKISDFGISKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 192 Y----IDPETKKHIPyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDT 267
Cdd:cd06628  156 LeansLSTKNNGARP-----SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP--DCTQMQAIF-KIGEN 227
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 530379706 268 KRATPIEVLCEnfpEMATYLRYVRRLDFFEKPDYDYLRK 306
Cdd:cd06628  228 ASPTIPSNISS---EARDFLEKTFEIDHNKRPTADELLK 263
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
131-193 2.48e-08

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: 55.44  E-value: 2.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 193
Cdd:cd05571   89 ERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGH-----IKITDFGLCKEEI 146
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
133-274 2.49e-08

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: 55.01  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 133 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQV----IHIIDFGLAKeYIDPETKKhipyrehKS 208
Cdd:cd14201  101 TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVsgirIKIADFGFAR-YLQSNMMA-------AT 172
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 209 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIE 274
Cdd:cd14201  173 LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRE 238
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
145-272 3.02e-08

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: 54.55  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGK 224
Cdd:cd14189  109 QIISGLKYLHLKGILHRDLKLGNFFI----NENME-LKVGDFGLAARLEPPEQRK-------KTICGTPNYLAPEVLLRQ 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQGLKadtLKERYQKIGDTKRATP 272
Cdd:cd14189  177 GHGPESDVWSLGCVMYTLLCGNPPFETLD---LKETYRCIKQVKYTLP 221
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
140-308 3.08e-08

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: 54.80  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 140 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpETKKHIPYREHKsltGTARYMSIN 219
Cdd:cd14047  120 LEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGK-----VKIGDFGLVT-----SLKNDGKRTKSK---GTLSYMSPE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 220 THLGKEQSRRDDLEALGHMFMYFLRgslpwqglKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKP 299
Cdd:cd14047  187 QISSQDYGKEVDIYALGLILFELLH--------VCDSAFEKSKFWTDLRNGILPDIFDKRYKIEKTIIKKMLSKKPEDRP 258

                 ....*....
gi 530379706 300 DYDYLRKLF 308
Cdd:cd14047  259 NASEILRTL 267
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
143-264 3.25e-08

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 55.42  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE------------TKKHIPYREHK--- 207
Cdd:cd05600  123 AISSLHQLGYIH------RDLKPENFLIDSSGH-----IKLTDFGLASGTLSPKkiesmkirleevKNTAFLELTAKerr 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 208 ---------------SLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 264
Cdd:cd05600  192 niyramrkedqnyanSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG---STPNETWANL 260
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
114-195 3.55e-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: 54.19  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAkEY 192
Cdd:cd14119   73 MVMEYCVGGLQEMLDSApDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL-----TTDGTLKISDFGVA-EA 146

                 ...
gi 530379706 193 IDP 195
Cdd:cd14119  147 LDL 149
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
114-217 4.55e-08

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: 53.81  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLgpSLEDLFDLCDRTFSLkTVLMIAI---QLISRMEYVHSKNLIYRDVKPENFLI-GRPGNKtqqvIHIIDFGLA 189
Cdd:cd14006   66 LILELC--SGGELLDRLAERGSL-SEEEVRTymrQLLEGLQYLHNHHILHLDLKPENILLaDRPSPQ----IKIIDFGLA 138
                         90       100
                 ....*....|....*....|....*...
gi 530379706 190 KEYIDPETKKHIpyrehkslTGTARYMS 217
Cdd:cd14006  139 RKLNPGEELKEI--------FGTPEFVA 158
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
49-250 4.72e-08

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: 54.08  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQL-HLEYRFYKQLGSGDGIPQVYYFGPCGKYnAMVLELlgPSLEDLF 127
Cdd:cd14087    9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVcESELNVLRRVRHTNIIQLIEVFETKERV-YMVMEL--ATGGELF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 128 D--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAkeyidpETKKHIPYRE 205
Cdd:cd14087   86 DriIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSK--IMITDFGLA------STRKKGPNCL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 530379706 206 HKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14087  158 MKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD 202
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
128-316 4.82e-08

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: 54.60  E-value: 4.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 128 DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPETKKhipyreh 206
Cdd:cd05103  170 DLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPDYVR------- 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 207 kslTGTAR----YMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRAtpievlcenfP 281
Cdd:cd05103  238 ---KGDARlplkWMAPETIFDRVYTIQSDVWSFGvLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRA----------P 304
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530379706 282 EMATYLRYVRRLDFFE-KPDYdylRKLFTDLFDRKG 316
Cdd:cd05103  305 DYTTPEMYQTMLDCWHgEPSQ---RPTFSELVEHLG 337
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
129-217 5.02e-08

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: 53.94  E-value: 5.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 129 LCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqviHII--DFGLAKEYIDPETkkhipYRE 205
Cdd:cd05583   90 LYQREhFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEG-------HVVltDFGLSKEFLPGEN-----DRA 157
                         90
                 ....*....|..
gi 530379706 206 HkSLTGTARYMS 217
Cdd:cd05583  158 Y-SFCGTIEYMA 168
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
43-189 5.27e-08

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: 53.79  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSgdgiPQV--YYFGPCGKYN-AMVL 116
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKvidLEEAEDEIEDIQQEIQFLSQCDS----PYItkYYGSFLKGSKlWIIM 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 117 ELL-GPSLEDLFDLCdrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd06609   79 EYCgGGSVLDLLKPG--PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGD-----VKLADFGVS 145
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
47-245 5.53e-08

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: 54.23  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHLEYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd07872   12 EKLGEGTYATVFKGRSKLTENLVAlkeIRLEHEEGAPCTAIREVSLLKDLKHAN-IVTLHDIVHTDKSLTLVFEYLDKDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPY 203
Cdd:cd07872   91 KQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE-----LKLADFGLAR-------AKSVPT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530379706 204 REHKSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRG 245
Cdd:cd07872  159 KTYSNEVVTLWYRPPDVLLGsSEYSTQIDMWGVGCIFFEMASG 201
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
42-249 5.63e-08

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: 53.90  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAP----QLHLEYRFYKQLgSGDGIpqVYYFGpCGKYNAM 114
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKqveIDPINTEASkevkALECEIQLLKNL-QHERI--VQYYG-CLQDEKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 V---LELL-GPSLED-------LFDLCDRTFSLktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHI 183
Cdd:cd06625   77 LsifMEYMpGGSVKDeikaygaLTENVTRKYTR--------QILEGLAYLHSNMIVHRDIKGANILRDSNGN-----VKL 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 184 IDFGLAKEYIDPETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06625  144 GDFGASKRLQTICSSTGM-----KSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW 204
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
142-260 5.98e-08

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: 53.63  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIHIIDFGLAKeYIDPETKKhipyrehKSLTGTARYMSINTH 221
Cdd:cd14098  106 LTKQILEAMAYTHSMGITHRDLKPENILITQDDPV---IVKISDFGLAK-VIHTGTFL-------VTFCGTMAYLAPEIL 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530379706 222 LGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKER 260
Cdd:cd14098  175 MSKEQNLQGgysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKR 219
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
49-308 6.75e-08

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: 54.28  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK--LEPMKS--RAPQLHLEYRFYKQLGSGDGIPQVYYFGPCG---KYNA--MVLELL 119
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKklSRPFQSliHARRTYRELRLLKHMKHENVIGLLDVFTPATsieNFNEvyLVTNLM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDlCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKK 199
Cdd:cd07878  103 GADLNNIVK-CQK-LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCE-----LRILDFGLARQ-ADDEMTG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 200 HIPYREHKSLTGTARYMSINTHLgkeqsrrdDLEALGHMFMYFLRGSLPWQGLK-ADTLKERYQKIGdtkraTPI-EVLC 277
Cdd:cd07878  175 YVATRWYRAPEIMLNWMHYNQTV--------DIWSVGCIMAELLKGKALFPGNDyIDQLKRIMEVVG-----TPSpEVLK 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 530379706 278 ENFPEMATylRYVRRLDFFEKPDydyLRKLF 308
Cdd:cd07878  242 KISSEHAR--KYIQSLPHMPQQD---LKKIF 267
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
128-263 7.10e-08

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: 53.53  E-value: 7.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 128 DLCD-----RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNK----TQQVIHIIDFGLAKeYIDPETK 198
Cdd:cd14120   78 DLADylqakGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRkpspNDIRLKIADFGFAR-FLQDGMM 156
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 199 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 263
Cdd:cd14120  157 A-------ATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEK 214
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
52-250 7.36e-08

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: 53.29  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  52 GNFGELRLGKNLYTNEYVAIKLEPM----KSRAPQlhlEYRFYKQLGSgDGIPQVY--YFGPcgKYNAMVLELLGpSLED 125
Cdd:cd14111   14 GRFGVIRRCRENATGKNFPAKIVPYqaeeKQGVLQ---EYEILKSLHH-ERIMALHeaYITP--RYLVLIAEFCS-GKEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrPGNktqqVIHIIDFGLAKEYiDPETKKHIPYR 204
Cdd:cd14111   87 LHSLIDRfRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT-NLN----AIKIVDFGSAQSF-NPLSLRQLGRR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 205 ehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14111  161 -----TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE 201
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
39-200 7.79e-08

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 53.91  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  39 VGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQL----HLEYRFYKQLGSGDGIPQVYYFGPCGKYNAM 114
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTakrtLRELKILRHFKHDNIIAIRDILRPKVPYADF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 -----VLELLGPSLEDLFDlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd07855   83 kdvyvVLDLMESDLHHIIH-SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE-----LKIGDFGMA 156
                        170
                 ....*....|.
gi 530379706 190 KEyIDPETKKH 200
Cdd:cd07855  157 RG-LCTSPEEH 166
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
134-257 7.88e-08

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: 53.93  E-value: 7.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIdpetkkhipYREHKSLT--G 211
Cdd:cd05592   93 FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH-----IKIADFGMCKENI---------YGENKASTfcG 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 212 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05592  159 TPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDEL 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
48-199 8.29e-08

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: 53.53  E-value: 8.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQLGSGDGIP--QVYYfGPCGKYNA------MV 115
Cdd:cd07865   19 KIGQGTFGEVFKARHRKTGQIVALKkvlMENEKEGFPITALrEIKILQLLKHENVVNliEICR-TKATPYNRykgsiyLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDP 195
Cdd:cd07865   98 FEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDG-----VLKLADFGLARAFSLA 172

                 ....
gi 530379706 196 ETKK 199
Cdd:cd07865  173 KNSQ 176
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
43-170 8.32e-08

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: 53.73  E-value: 8.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepMKSRApqlHL------EYRFYKQLGSGD-------GIPQVY-YF--- 105
Cdd:cd14136   12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKV--VKSAQ---HYteaaldEIKLLKCVREADpkdpgreHVVQLLdDFkht 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 106 GPCGKYNAMVLELLGPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLI 170
Cdd:cd14136   87 GPNGTHVCMVFEVLGPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLL 153
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
49-236 8.54e-08

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: 53.25  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCgkynamvleLLGPSLED 125
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKvlnLDTDDDDVSDIQKEVALLSQLKLGQPKNIIKYYGSY---------LKGPSLWI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTfSLKTvLMIA-------IQLISR-----MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 193
Cdd:cd06917   80 IMDYCEGG-SIRT-LMRAgpiaeryIAVIMRevlvaLKFIHKDGIIHRDIKAANILVTNTGN-----VKLCDFGVAASLN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530379706 194 DPETKKhipyrehKSLTGTARYMSINTHL-GKEQSRRDDLEALG 236
Cdd:cd06917  153 QNSSKR-------STFVGTPYWMAPEVITeGKYYDTKADIWSLG 189
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
102-236 8.58e-08

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: 53.29  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 102 VYYFGPCGKYNAM--VLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQ 178
Cdd:cd14156   51 VRYLGICVKDEKLhpILEYVsGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGRE 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 179 QVihIIDFGLAKEYI-----DPETKkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALG 236
Cdd:cd14156  131 AV--VTDFGLAREVGempanDPERK--------LSLVGSAFWMAPEMLRGEPYDRKVDVFSFG 183
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
114-245 9.01e-08

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: 53.04  E-value: 9.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDlCDRTFSL---KTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGL 188
Cdd:cd13982   72 IALELCAASLQDLVE-SPRESKLflrPGLEPVRLlrQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRAMISDFGL 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 189 AKEYidpETKKHiPYREHKSLTGT----ARYMsINTHLGKEQSRRDDLEALGHMFMYFLRG 245
Cdd:cd13982  151 CKKL---DVGRS-SFSRRSGVAGTsgwiAPEM-LSGSTKRRQTRAVDIFSLGCVFYYVLSG 206
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
131-249 9.29e-08

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: 53.87  E-value: 9.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLT 210
Cdd:cd05602  102 ERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH-----IVLTDFGLCKENIEPNGTT-------STFC 169
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530379706 211 GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05602  170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
47-250 9.32e-08

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: 53.07  E-value: 9.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQlgsgdgiPQVYYFGPC---GKYNAMVLELl 119
Cdd:cd14665    6 KDIGSGNFGVARLMRDKQTKELVAVKYiergEKIDENVQREIINHRSLRH-------PNIVRFKEViltPTHLAIVMEY- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 gPSLEDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI-GRPGNKtqqvIHIIDFGLakeyidpe 196
Cdd:cd14665   78 -AAGGELFErICNAgRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdGSPAPR----LKICDFGY-------- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 197 TKKHIPYREHKSLTGTARYMSINTHLGKE-QSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14665  145 SKSSVLHSQPKSTVGTPAYIAPEVLLKKEyDGKIADVWSCGVTLYVMLVGAYPFE 199
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
49-217 9.50e-08

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: 53.18  E-value: 9.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMK-SRAPQ-LHLEYRFYKQLgSGDGIpqVYYFGPC--GKYNAMVLELL-GPSL 123
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPERdSREVQpLHEEIALHSRL-SHKNI--VQYLGSVseDGFFKIFMEQVpGGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLfdLCDRTFSLK----TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEY--IDPET 197
Cdd:cd06624   93 SAL--LRSKWGPLKdnenTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLV----NTYSGVVKISDFGTSKRLagINPCT 166
                        170       180
                 ....*....|....*....|
gi 530379706 198 kkhipyrehKSLTGTARYMS 217
Cdd:cd06624  167 ---------ETFTGTLQYMA 177
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
42-217 9.60e-08

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: 52.85  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQLGSgdgiPQV--YY--FGPCGKYNa 113
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeidLSNMSEKEREEALnEVKLLSKLKH----PNIvkYYesFEENGKLC- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLgpsleDLFDLCDR---------TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHII 184
Cdd:cd08215   76 IVMEYA-----DGGDLAQKikkqkkkgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG-----VVKLG 145
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530379706 185 DFGLAKEYIDPETKKhipyrehKSLTGTARYMS 217
Cdd:cd08215  146 DFGISKVLESTTDLA-------KTVVGTPYYLS 171
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
43-248 1.02e-07

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: 53.15  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSgdgiPQVY-YFGPCGKYNAM--VL 116
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKiidLEEAEDEIEDIQQEITVLSQCDS----PYVTkYYGSYLKDTKLwiIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFD--LCDRTfSLKTVLMiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 193
Cdd:cd06641   82 EYLgGGSALDLLEpgPLDET-QIATILR---EILKGLDYLHSEKKIHRDIKAANVLLSEHGE-----VKLADFGVAGQLT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 194 DPETKKHipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06641  153 DTQIKRN-------*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-203 1.25e-07

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: 53.07  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMK--SRAPQLHLEYRFYKQLGSGD--GIPQVYyfgPCGKYNAMVLELLgpSLE 124
Cdd:cd14166   11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSplSRDSSLENEIAVLKRIKHENivTLEDIY---ESTTHYYLVMQLV--SGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKE----------- 191
Cdd:cd14166   86 ELFDrILERgVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSK--IMITDFGLSKMeqngimstacg 163
                        170
                 ....*....|....*
gi 530379706 192 ---YIDPETKKHIPY 203
Cdd:cd14166  164 tpgYVAPEVLAQKPY 178
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
145-275 1.64e-07

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: 52.29  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqVIHIIDFGLAKeYIDPETKKHipyrehkSLTGTARYMSINTHLGK 224
Cdd:cd14121  103 QLASALQFLREHNISHMDLKPQNLLLSSRYNP---VLKLADFGFAQ-HLKPNDEAH-------SLRGSPLYMAPEMILKK 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530379706 225 EQSRRDDLEALGhMFMY-FLRGSLPWqglKADTLKERYQKIgdtKRATPIEV 275
Cdd:cd14121  172 KYDARVDLWSVG-VILYeCLFGRAPF---ASRSFEELEEKI---RSSKPIEI 216
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
43-268 1.70e-07

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: 53.10  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRF-YKQLGSGDGIPQVYyfgPCGKYNAMVLELL-G 120
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLrYGQHPNIITLKDVY---DDGKYVYVVTELMkG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqQVIHIIDFGLAKEyidpetkk 199
Cdd:cd14176   98 GELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNP--ESIRICDFGFAKQ-------- 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 200 hipYREHKSLTGTARYMSinTHLGKEQSRRD------DLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 268
Cdd:cd14176  167 ---LRAENGLLMTPCYTA--NFVAPEVLERQgydaacDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGK 236
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
42-215 1.75e-07

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 52.51  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHL-EYRFYKQLGSGDgIPQVYYFGPCGKYNAMVLE 117
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKARNKLTGEVVAlkkIRLDTETEGVPSTAIrEISLLKELNHPN-IVKLLDVIHTENKLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LLGPSLEDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDP- 195
Cdd:cd07860   80 FLHQDLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA-----IKLADFGLARAFGVPv 154
                        170       180
                 ....*....|....*....|....
gi 530379706 196 ETKKH----IPYREHKSLTGTARY 215
Cdd:cd07860  155 RTYTHevvtLWYRAPEILLGCKYY 178
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
43-265 1.99e-07

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: 52.17  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPmKSRAPQLHLEYRFYKQLG-----SGDGIPQVY-YFGPCGKYNAMVL 116
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD-RRRASPDFVQKFLPRELSilrrvNHPNIVQMFeCIEVANGRLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 EllgPSLEDLFDLCDRTFSLKTVLM--IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqvIHIIDFGLAKEYID 194
Cdd:cd14164   81 E---AAATDLLQKIQEVHHIPKDLArdMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK----IKIADFGFARFVED 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 195 PETKKHipyrehkSLTGTARYMSINTHLG-KEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLkeRYQKIG 265
Cdd:cd14164  154 YPELST-------TFCGSRAYTPPEVILGtPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRG 216
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
114-264 2.09e-07

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 52.33  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLE-DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAke 191
Cdd:cd05630   77 LVLTLMnGGDLKfHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGH-----IRISDLGLA-- 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 192 yidpetkKHIPYREH-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKI 264
Cdd:cd05630  150 -------VHVPEGQTiKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERL 216
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
131-259 2.11e-07

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: 52.78  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKkhipyrehKSL 209
Cdd:cd05593  109 ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-----IKITDFGLCKEGItDAATM--------KTF 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530379706 210 TGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKE 259
Cdd:cd05593  176 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 225
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
35-282 2.15e-07

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 52.69  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  35 GVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGK 110
Cdd:cd05621   46 ELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAMVLELL-GPSLEDL---FDLCDRTFSLKTVlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDF 186
Cdd:cd05621  126 YLYMVMEYMpGGDLVNLmsnYDVPEKWAKFYTA-----EVVLALDAIHSMGLIHRDVKPDNMLLDKYGH-----LKLADF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 187 GLAKEyIDPETKKHIpyrehKSLTGTARYMSinTHLGKEQ------SRRDDLEALGHMFMYFLRGSLPWQglkADTLKER 260
Cdd:cd05621  196 GTCMK-MDETGMVHC-----DTAVGTPDYIS--PEVLKSQggdgyyGRECDWWSVGVFLFEMLVGDTPFY---ADSLVGT 264
                        250       260
                 ....*....|....*....|..
gi 530379706 261 YQKIGDTKRATpievlceNFPE 282
Cdd:cd05621  265 YSKIMDHKNSL-------NFPD 279
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
46-273 2.15e-07

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: 52.00  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEyrfyKQLGSGDGIPQ-------------VYYFG------ 106
Cdd:cd06629    6 GELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADS----RQKTVVDALKSeidtlkdldhpniVQYLGfeeted 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 107 ---------PCGKYnAMVLELLGPSLEDLFDLCDRtfslktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKT 177
Cdd:cd06629   82 yfsifleyvPGGSI-GSCLRKYGKFEEDLVRFFTR------------QILDGLAYLHSKGILHRDLKADNILV-----DL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 178 QQVIHIIDFGLAKEyidpetKKHIpYREHK--SLTGTARYMS---INThLGKEQSRRDDLEALGHMFMYFLRGSLPWqgl 252
Cdd:cd06629  144 EGICKISDFGISKK------SDDI-YGNNGatSMQGSVFWMApevIHS-QGQGYSAKVDIWSLGCVVLEMLAGRRPW--- 212
                        250       260
                 ....*....|....*....|....
gi 530379706 253 kadTLKERYQ---KIGDTKRATPI 273
Cdd:cd06629  213 ---SDDEAIAamfKLGNKRSAPPV 233
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
43-249 2.20e-07

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: 52.26  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKsrapQLHLEYRFYK-------QLGSGDgipQVYYFGPCGK-YNAM 114
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKK----KLLKQYGFPRrppprgsKAAQGE---QAKPLAPLERvYQEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 -------------VLELLGPSLED----LFDL----------CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPEN 167
Cdd:cd14200   75 ailkkldhvnivkLIEVLDDPAEDnlymVFDLlrkgpvmevpSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 168 FLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrEHKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLR 244
Cdd:cd14200  155 LLLGDDGH-----VKIADFGVSNQFEGNDA-------LLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVY 222

                 ....*
gi 530379706 245 GSLPW 249
Cdd:cd14200  223 GKCPF 227
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
47-202 2.21e-07

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: 51.68  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHlEYRFYKQLgsgDGIPQVYYFGPCG-KYNAM-VLELL- 119
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKTcretLPPDLKRKFLQ-EARILKQY---DHPNIVKLIGVCVqKQPIMiVMELVp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE-----YID 194
Cdd:cd05041   77 GGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENN-----VLKISDFGMSREeedgeYTV 151

                 ....*...
gi 530379706 195 PETKKHIP 202
Cdd:cd05041  152 SDGLKQIP 159
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
43-249 2.25e-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: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepmksraPQLHLEYRFYKQLGSGDGIPQ-------VYYFGPCGKYNA-- 113
Cdd:cd06605    3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKV-------IRLEIDEALQKQILRELDVLHkcnspyiVGFYGAFYSEGDis 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLCDRTfSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd06605   76 ICMEYMdGGSLDKILKEVGRI-PERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ-----VKLCDFGVSGQ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 192 YIDPETkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06605  150 LVDSLA---------KTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPY 198
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
43-192 2.42e-07

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: 51.89  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKlepmKSRAPqlhleyrfykqlGSGDGIP-----------QVYYFG-P--- 107
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALK----KVRVP------------LSEEGIPlstireiallkQLESFEhPnvv 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 108 -----CGKYN-------AMVLELLGPSLEDLFDLC-DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpg 174
Cdd:cd07838   65 rlldvCHGPRtdrelklTLVFEHVDQDLATYLDKCpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS-- 142
                        170
                 ....*....|....*...
gi 530379706 175 nktQQVIHIIDFGLAKEY 192
Cdd:cd07838  143 ---DGQVKLADFGLARIY 157
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
43-192 2.62e-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: 51.89  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL--------------------------EPMKSRAP--QLHLEYRFYKQLG 94
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVlskkklmrqagfprrppprgaraapeGCTQPRGPieRVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  95 SGDGIPQVYYFG-PCGKYNAMVLELL--GPSLEDLfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIG 171
Cdd:cd14199   84 HPNVVKLVEVLDdPSEDHLYMVFELVkqGPVMEVP---TLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG 160
                        170       180
                 ....*....|....*....|.
gi 530379706 172 RPGNktqqvIHIIDFGLAKEY 192
Cdd:cd14199  161 EDGH-----IKIADFGVSNEF 176
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
48-190 2.87e-07

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: 52.04  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSRAPQ--LHLEYRFYKQLGSGDGIPQVYYFGPCGKYNaMVLELLGPSL 123
Cdd:cd07846    8 LVGEGSYGMVMKCRHKETGQIVAIKkfLESEDDKMVKkiAMREIKMLKQLRHENLVNLIEVFRRKKRWY-LVFEFVDHTV 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd07846   87 LDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSG-----VVKLCDFGFAR 148
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
42-254 3.26e-07

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: 51.56  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-------LHLEYRFYKQLgSGDGIPQvyYFG----PCGK 110
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQEtskevnaLECEIQLLKNL-RHDRIVQ--YYGclrdPEEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAMVLELL-GPSLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd06653   80 KLSIFVEYMpGGSVKDQLKAYG-ALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGN-----VKLGDFGAS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 190 KeyidpetKKHIPYREH---KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 254
Cdd:cd06653  154 K-------RIQTICMSGtgiKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEA 214
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
47-190 3.32e-07

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: 51.13  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEyVAIK-LEPmKSRAPQLHL-EYRFYKQLgSGDGIPQVYyfGPCGK----YnaMVLELL- 119
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNGTTK-VAVKtLKP-GTMSPEAFLqEAQIMKKL-RHDKLVQLY--AVCSDeepiY--IVTELMs 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 190
Cdd:cd05034   74 kGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGE-----NNVCKVADFGLAR 140
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
131-249 3.47e-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: 51.95  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHS-KNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKkhipyrehKS 208
Cdd:cd05594  119 ERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-----IKITDFGLCKEGIkDGATM--------KT 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530379706 209 LTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05594  186 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 226
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
48-190 3.60e-07

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: 51.52  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHL-EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd07835    6 KIGEGTYGVVYKARDKLTGEIVAlkkIRLETEDEGVPSTAIrEISLLKEL-NHPNIVRLLDVVHSENKLYLVFEFLDLDL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 124 EDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd07835   85 KKYMDSSPLTgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA-----LKLADFGLAR 147
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
109-190 3.62e-07

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: 51.16  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 GKYN-AMVLELLgpSLEDLFD-LCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHII 184
Cdd:cd14191   70 EKANiVMVLEMV--SGGELFErIIDEDFELteRECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC---VNKTGTKIKLI 144

                 ....*.
gi 530379706 185 DFGLAK 190
Cdd:cd14191  145 DFGLAR 150
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
41-199 3.65e-07

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 51.07  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  41 PNFRVGKKIGCGNF-----GELRLGKNL--YTNEYVAIKlEPMKSRAPQLHL-EYRFYKQLGSGDGIPQVYYfgpCGKYN 112
Cdd:cd14019    1 NKYRIIEKIGEGTFssvykAEDKLHDLYdrNKGRLVALK-HIYPTSSPSRILnELECLERLGGSNNVSGLIT---AFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLgPSLE-----DLFdlcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFG 187
Cdd:cd14019   77 DQVVAVL-PYIEhddfrDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY----NRETGKGVLVDFG 147
                        170
                 ....*....|..
gi 530379706 188 LAKEYIDPETKK 199
Cdd:cd14019  148 LAQREEDRPEQR 159
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
42-254 3.66e-07

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: 51.20  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-------LHLEYRFYKQLgSGDGIPQVYYF--GPCGKYN 112
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPEtskevnaLECEIQLLKNL-LHERIVQYYGClrDPQERTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELL-GPSLED-------LFDLCDRTFSLktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHII 184
Cdd:cd06652   82 SIFMEYMpGGSIKDqlksygaLTENVTRKYTR--------QILEGVHYLHSNMIVHRDIKGANILRDSVGN-----VKLG 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 185 DFGLAKEYidpeTKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 254
Cdd:cd06652  149 DFGASKRL----QTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEA 214
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
102-191 4.30e-07

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: 51.08  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 102 VYYFGPCGKYNAMVLEL--LGpSLEDLFDLCDRTF-SLKTVLM--IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNK 176
Cdd:cd14000   73 VYLLGIGIHPLMLVLELapLG-SLDHLLQQDSRSFaSLGRTLQqrIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPN 151
                         90
                 ....*....|....*
gi 530379706 177 TQQVIHIIDFGLAKE 191
Cdd:cd14000  152 SAIIIKIADYGISRQ 166
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-203 4.50e-07

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: 50.83  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEYRFYKQLgSGDGIPQVY--YFGPCGKYnaMVLELLgpSL 123
Cdd:cd14083   11 LGTGAFSEVVLAEDKATGKLVAIKCidkKALKGKEDSLENEIAVLRKI-KHPNIVQLLdiYESKSHLY--LVMELV--TG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFD--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK----------- 190
Cdd:cd14083   86 GELFDriVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSK--IMISDFGLSKmedsgvmstac 163
                        170
                 ....*....|....*.
gi 530379706 191 ---EYIDPETKKHIPY 203
Cdd:cd14083  164 gtpGYVAPEVLAQKPY 179
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
43-196 4.51e-07

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 51.54  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLepMKSRAPQLHLEYRFYKQ------LGSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKV--LKKSETLAQEEVSFFEEerdimaKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLCDRTFSLKTV------LMIAIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd05601   81 EYHpGGDLLSLLSRYDDIFEESMArfylaeLVLAIHSLHSMGYVH------RDIKPENILIDRTGH-----IKLADFGSA 149
                        170       180
                 ....*....|....*....|....
gi 530379706 190 -----------------KEYIDPE 196
Cdd:cd05601  150 aklssdktvtskmpvgtPDYIAPE 173
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
42-189 4.54e-07

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: 50.97  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKS------------RAPQLHleyrfykQLGSGDGIPQVYYFGPCG 109
Cdd:cd14070    3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKakkdsyvtknlrREGRIQ-------QMIRHPNITQLLDILETE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNAMVLEL-LGPSLEDlfDLCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFG 187
Cdd:cd14070   76 NSYYLVMELcPGGNLMH--RIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN-----IKLIDFG 148

                 ..
gi 530379706 188 LA 189
Cdd:cd14070  149 LS 150
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
47-190 4.58e-07

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: 50.81  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEY---VAIKL---EPMKSRAPQLHLEYRFYKQLgsgDGIPQVYYFGPC-GKYNAMVLEL- 118
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSGKeveVAVKTlkqEHEKAGKKEFLREASVMAQL---DHPCIVRLIGVCkGEPLMLVMELa 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 119 -LGPSLEDLFDlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 190
Cdd:cd05060   78 pLGPLLKYLKK--RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL-----VNRHQAKISDFGMSR 143
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
47-208 4.88e-07

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: 51.42  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSR--APQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPS 122
Cdd:cd07856   16 QPVGMGAFGLVCSARDQLTGQNVAVKkiMKPFSTPvlAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYIDPETKKHIP 202
Cdd:cd07856   96 LHRL--LTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCD-----LKICDFGLAR-IQDPQMTGYVS 167

                 ....*.
gi 530379706 203 YREHKS 208
Cdd:cd07856  168 TRYYRA 173
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
46-196 5.09e-07

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: 50.91  E-value: 5.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKnlYTNEY-VAIKL--EPMKSRAPQLHlEYRFYKQLgSGDGIPQVYyfGPCGKYNAM--VLELLG 120
Cdd:cd05059    9 LKELGSGQFGVVHLGK--WRGKIdVAIKMikEGSMSEDDFIE-EAKVMMKL-SHPKLVQLY--GVCTKQRPIfiVTEYMA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 121 -PSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPE 196
Cdd:cd05059   83 nGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG-----EQNVVKVSDFGLARYVLDDE 154
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
38-270 5.52e-07

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 51.54  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNA 113
Cdd:cd05622   70 MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLY 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDL---FDLCDRTFSLKTVlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL- 188
Cdd:cd05622  150 MVMEYMpGGDLVNLmsnYDVPEKWARFYTA-----EVVLALDAIHSMGFIHRDVKPDNMLLDKSGH-----LKLADFGTc 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 189 ----------------AKEYIDPETKkhipyrehKSLTGTARYmsinthlgkeqSRRDDLEALGHMFMYFLRGSLPWQgl 252
Cdd:cd05622  220 mkmnkegmvrcdtavgTPDYISPEVL--------KSQGGDGYY-----------GRECDWWSVGVFLYEMLVGDTPFY-- 278
                        250
                 ....*....|....*...
gi 530379706 253 kADTLKERYQKIGDTKRA 270
Cdd:cd05622  279 -ADSLVGTYSKIMNHKNS 295
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
143-314 6.60e-07

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: 50.81  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNL---IYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYidpetkkhipYREHK-SLTGTARY 215
Cdd:cd14145  110 AVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKvenGDLSNKILKITDFGLAREW----------HRTTKmSAAGTYAW 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 216 MSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLCenfPEmatylRYVRRLDF 295
Cdd:cd14145  180 MAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGI--DGLAVAY-GVAMNKLSLPIPSTC---PE-----PFARLMED 248
                        170
                 ....*....|....*....
gi 530379706 296 FEKPDyDYLRKLFTDLFDR 314
Cdd:cd14145  249 CWNPD-PHSRPPFTNILDQ 266
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
42-190 6.72e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 51.57  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSRAPQL-------HLEYRFYKQlgsgdgipqvYYFGPCGKYN 112
Cdd:PTZ00036  67 SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKkvLQDPQYKNRELlimknlnHINIIFLKD----------YYYTECFKKN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 A------MVLELLGPSLEDLFDLCDR---TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTqqvIHI 183
Cdd:PTZ00036 137 EkniflnVVMEFIPQTVHKYMKHYARnnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI-DPNTHT---LKL 212

                 ....*..
gi 530379706 184 IDFGLAK 190
Cdd:PTZ00036 213 CDFGSAK 219
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
134-249 7.47e-07

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: 51.07  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehkSLTGTA 213
Cdd:cd05614  102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH-----VVLTDFGLSKEFLTEEKERTY------SFCGTI 170
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530379706 214 RYMSINTHLGKE-QSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05614  171 EYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPF 207
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
142-248 7.51e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 50.98  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAK---EYIDPetkkhipyreHKSLTGTARYMS- 217
Cdd:PLN00034 173 VARQILSGIAYLHRRHIVHRDIKPSNLLI----NSAKNV-KIADFGVSRilaQTMDP----------CNSSVGTIAYMSp 237
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530379706 218 --INTHL--GKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:PLN00034 238 erINTDLnhGAYDGYAGDIWSLGVSILEFYLGRFP 272
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
137-248 7.60e-07

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: 50.50  E-value: 7.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 137 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYM 216
Cdd:cd06621  105 KVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ-----VKLCDFGVSGELVNSLA---------GTFTGTSYYM 170
                         90       100       110
                 ....*....|....*....|....*....|..
gi 530379706 217 SINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06621  171 APERIQGGPYSITSDVWSLGLTLLEVAQNRFP 202
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
143-257 7.62e-07

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: 50.19  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPETKkhipyrehKSLTGTARYMSINTHL 222
Cdd:cd14059   87 SKQIASGMNYLHLHKIIHRDLKSPNVLVT-----YNDVLKISDFGTSKELSEKSTK--------MSFAGTVAWMAPEVIR 153
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530379706 223 GKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 257
Cdd:cd14059  154 NEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAI 188
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
139-264 7.72e-07

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: 50.73  E-value: 7.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 139 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYREHKSLTGTARYMSI 218
Cdd:cd07870  100 VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE-----LKLADFGLAR-------AKSIPSQTYSSEVVTLWYRPP 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530379706 219 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLkADTLkERYQKI 264
Cdd:cd07870  168 DVLLGAtDYSSALDIWGAGCIFIEMLQGQPAFPGV-SDVF-EQLEKI 212
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
134-249 7.82e-07

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: 50.38  E-value: 7.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehkSLTGTA 213
Cdd:cd05613  102 FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGH-----VVLTDFGLSKEFLLDENERAY------SFCGTI 170
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530379706 214 RYMSINTHLGKE--QSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05613  171 EYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLTGASPF 208
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
47-252 8.12e-07

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: 50.44  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSgdgiPQVY-YFGPCGKYNAM--VLELLG 120
Cdd:cd06642   10 ERIGKGSFGEVYKGIDNRTKEVVAIKiidLEEAEDEIEDIQQEITVLSQCDS----PYITrYYGSYLKGTKLwiIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 P-SLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKK 199
Cdd:cd06642   86 GgSALDL--LKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD-----VKLADFGVAGQLTDTQIKR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530379706 200 HipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGL 252
Cdd:cd06642  159 N-------TFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL 204
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
42-264 8.33e-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: 50.25  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEpMKSRAPQLHLEYRFYKQLG-----SGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd14117    7 DFDIGRPLGKGKFGNVYLAREKQSKFIVALKVL-FKSQIEKEGVEHQLRREIEiqshlRHPNILRLYNYFHDRKRIYLIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL--GPSLEDLFDLCdrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkeyid 194
Cdd:cd14117   86 EYAprGELYKELQKHG--RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE-----LKIADFGWS----- 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 195 petkKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKI 264
Cdd:cd14117  154 ----VHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE---SASHTETYRRI 216
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
43-204 8.88e-07

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: 50.08  E-value: 8.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHL--EYRFYKQLgSGDGIPQVY-YFGPCGKynaMVL 116
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSikkDKIEDEQDMVRIrrEIEIMSSL-NHPHIIRIYeVFENKDK---IVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELLGPSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID 194
Cdd:cd14073   79 VMEYASGGELYDYISERRRLpeREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN-----AKIADFGLSNLYSK 153
                        170       180
                 ....*....|....*....|....*
gi 530379706 195 ---------------PETKKHIPYR 204
Cdd:cd14073  154 dkllqtfcgsplyasPEIVNGTPYQ 178
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
47-189 9.70e-07

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: 50.14  E-value: 9.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKlePMKSRAPQLH-------LEYRFYKQLGSGDGIPqvyYFGpC---GKYNAMVL 116
Cdd:cd06607    7 REIGHGSFGAVYYARNKRTSEVVAIK--KMSYSGKQSTekwqdiiKEVKFLRQLRHPNTIE---YKG-CylrEHTAWLVM 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 117 ELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLA 189
Cdd:cd06607   81 EYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPG-----TVKLADFGSA 148
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
47-203 1.05e-06

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 50.15  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRApqlHLEYRFYKQLGSGDGIPQVY--YFG----PCGKYNA----MVL 116
Cdd:cd14171   12 QKLGTGISGPVRVCVKKSTGERFALKILLDRPKA---RTEVRLHMMCSGHPNIVQIYdvYANsvqfPGESSPRarllIVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELLGPSleDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQVIHIIDFGLAKEYI- 193
Cdd:cd14171   89 ELMEGG--ELFDRIsqHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKD--NSEDAPIKLCDFGFAKVDQg 164
                        170
                 ....*....|
gi 530379706 194 DPETKKHIPY 203
Cdd:cd14171  165 DLMTPQFTPY 174
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
141-196 1.17e-06

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: 50.16  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 141 MIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKeYIDPE 196
Cdd:cd07854  118 LFMYQLLRGLKYIHSANVLHRDLKPANVFI----NTEDLVLKIGDFGLAR-IVDPH 168
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
114-209 1.18e-06

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: 49.65  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLEL--LGPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnktqQVIHIIDFGLAKE 191
Cdd:cd05040   74 MVTELapLGSLLDRLRKDQGH-FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASK-----DKVKIGDFGLMRA 147
                         90
                 ....*....|....*...
gi 530379706 192 YidPETKKHIPYREHKSL 209
Cdd:cd05040  148 L--PQNEDHYVMQEHRKV 163
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
43-187 1.19e-06

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 49.85  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMK-----SRAPQLH---LEYRFYKQLGSGDGIPQV-----YYFGPCG 109
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNrvqqwSKLPGVNpvpNEVALLQSVGGGPGHRGVirlldWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYnaMVLELLGPSlEDLFDLCDRTFSLKTVL--MIAIQLISRMEYVHSKNLIYRDVKPENFLIG-RPGNktqqvIHIIDF 186
Cdd:cd14101   82 FL--LVLERPQHC-QDLFDYITERGALDESLarRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGD-----IKLIDF 153

                 .
gi 530379706 187 G 187
Cdd:cd14101  154 G 154
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
48-190 1.20e-06

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 50.06  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLH----LEYRFYKQLgsgdgipqvyyfgpcgKYNAMV--LELLGP 121
Cdd:cd07847    8 KIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKkialREIRMLKQL----------------KHPNLVnlIEVFRR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 S--LEDLFDLCDRTF-----------SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGL 188
Cdd:cd07847   72 KrkLHLVFEYCDHTVlneleknprgvPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITK-----QGQIKLCDFGF 146

                 ..
gi 530379706 189 AK 190
Cdd:cd07847  147 AR 148
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
42-187 1.25e-06

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 50.45  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd05596   27 DFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLlskfEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMD 106
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 118 LL-GPSLEDLFDLCD------RTFSLKTVLmiAIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFG 187
Cdd:cd05596  107 YMpGGDLVNLMSNYDvpekwaRFYTAEVVL--ALDAIHSMGFVH------RDVKPDNMLLDASGH-----LKLADFG 170
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
142-198 1.25e-06

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 49.73  E-value: 1.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 142 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFG--------------------LAKEYIDPETK 198
Cdd:cd06617  108 IAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ-----VKLCDFGisgylvdsvaktidagckpyMAPERINPELN 180
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
114-250 1.26e-06

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: 50.04  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKe 191
Cdd:cd14179   79 LVMELLKGG--ELLERIKKKqhFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE--IKIIDFGFAR- 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 192 yIDPETKKHIpyrehKSLTGTARYMS--INTHLGKEQSRrdDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14179  154 -LKPPDNQPL-----KTPCFTLHYAApeLLNYNGYDESC--DLWSLGVILYTMLSGQVPFQ 206
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
47-249 1.37e-06

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: 49.75  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAP---QL----------HLEY--RFYKQ-LGSGDGIPQVYYFGPCGK 110
Cdd:cd06620   11 KDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSvrkQIlrelqilhecHSPYivSFYGAfLNENNNIIICMEYMDCGS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAmVLELLGPsledlfdlcdrtFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd06620   91 LDK-ILKKKGP------------FPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQ-----IKLCDFGVS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 190 KEYIDPETKkhipyrehkSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06620  153 GELINSIAD---------TFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
35-189 1.38e-06

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 49.25  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  35 GVLMVGPNFRVGKKIGCGNFGELRLGKnlYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPcgkyNAM 114
Cdd:COG2112   34 SIYSGGTLIGGLRLLGKGYRGVVFLGK--LGGKKVALKIRRTDSPRPSLKKEAEILKKANGAGVGPKLYDYGR----DFL 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 115 VLELL-GPSLEDlfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDV-KPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:COG2112  108 VMEYIeGEPLKD----WLENLDKEELRKVIRELLEAAYLLDRIGIDHGELsRPGKHVIVDKGR-----PYIIDFESA 175
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
145-317 1.48e-06

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: 49.55  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLA-KEYIDPETKkhipyrehKSLTGTARYMSINTHLG 223
Cdd:cd14187  115 QIILGCQYLHRNRVIHRDLKLGNLFL----NDDMEV-KIGDFGLAtKVEYDGERK--------KTLCGTPNYIAPEVLSK 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 224 KEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATPIEVlcenFPEMATYLRYVRRLDFFEKPDYDy 303
Cdd:cd14187  182 KGHSFEVDIWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIPKHI----NPVAASLIQKMLQTDPTARPTIN- 253
                        170
                 ....*....|....
gi 530379706 304 lrKLFTDLFDRKGY 317
Cdd:cd14187  254 --ELLNDEFFTSGY 265
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
113-266 1.61e-06

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: 49.33  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLGPSLEDLfdlcDRTFSLKTVLMIaiqlisrmEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK-- 190
Cdd:cd05609   88 ATLLKNIGPLPVDM----ARMYFAETVLAL--------EYLHSYGIVHRDLKPDNLLITSMGH-----IKLTDFGLSKig 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 191 ----------EYIDPETKKHIpyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKER 260
Cdd:cd05609  151 lmslttnlyeGHIEKDTREFL----DKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEEL 223

                 ....*..
gi 530379706 261 Y-QKIGD 266
Cdd:cd05609  224 FgQVISD 230
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
43-203 1.64e-06

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: 49.50  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEP---MKSRAPQLHLEYRFYKQLGSGDGIP-QVYYFGPCGKYNAMVLEL 118
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPkkaLRGKEAMVENEIAVLRRINHENIVSlEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LGpsleDLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK------ 190
Cdd:cd14169   85 GG----ELFDrIIERgSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSK--IMISDFGLSKieaqgm 158
                        170       180
                 ....*....|....*....|.
gi 530379706 191 --------EYIDPETKKHIPY 203
Cdd:cd14169  159 lstacgtpGYVAPELLEQKPY 179
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
46-194 1.66e-06

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: 49.16  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVAIK-----LEP-MKSRAPQlhlEYRFYKQLGSgdgiPQ-VYYFGPCGKYNAM--VL 116
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADNTPVAVKscretLPPdLKAKFLQ---EARILKQYSH----PNiVRLIGVCTQKQPIyiVM 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYID 194
Cdd:cd05084   74 ELVqGGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTE-----KNVLKISDFGMSREEED 147
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
38-264 1.78e-06

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: 49.41  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  38 MVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHL-------EYRFYKQLGSgdgiPQVYYFGPCG 109
Cdd:cd14105    2 NVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKfIKKRRSKASRRGVsredierEVSILRQVLH----PNIITLHDVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 KYNA---MVLELLgpSLEDLFDLCDRTFSLKTVLMIAI--QLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIHII 184
Cdd:cd14105   78 ENKTdvvLILELV--AGGELFDFLAEKESLSEEEATEFlkQILDGVNYLHTKNIAHFDLKPENIML-LDKNVPIPRIKLI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 185 DFGLAKEyIDPETkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQGlkaDTLKER 260
Cdd:cd14105  155 DFGLAHK-IEDGN-------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLG---DTKQET 219

                 ....
gi 530379706 261 YQKI 264
Cdd:cd14105  220 LANI 223
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
25-316 1.80e-06

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: 49.62  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  25 NTRGTGSSSSGVLMVgpnfrVGKKIGCGNFGE-LRLGKNLY-TNEYVAIKLEPMKSRApQLHLEYRFYKQLGSgdgIPQV 102
Cdd:cd14207   75 NLLGACTKSGGPLMV-----IVEYCKYGNLSNyLKSKRDFFvTNKDTSLQEELIKEKK-EAEPTGGKKKRLES---VTSS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 103 YYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIH 182
Cdd:cd14207  146 ESFASSGFQEDKSLSDVEEEEEDSGDFYKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSE-----NNVVK 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 183 IIDFGLAKE-YIDPETKKhipyrehkslTGTAR----YMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKAD- 255
Cdd:cd14207  221 ICDFGLARDiYKNPDYVR----------KGDARlplkWMAPESIFDKIYSTKSDVWSYGvLLWEIFSLGASPYPGVQIDe 290
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 256 ----TLKEryqkiGDTKRAtpievlcenfPEMATYLRYVRRLDFFEKPDYDylRKLFTDLFDRKG 316
Cdd:cd14207  291 dfcsKLKE-----GIRMRA----------PEFATSEIYQIMLDCWQGDPNE--RPRFSELVERLG 338
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
45-191 1.80e-06

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: 49.27  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGknLYTNEYVAIKLEPMKSRAPQLHL-EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELLGP-S 122
Cdd:cd05039   10 LGELIGKGEFGDVMLG--DYRGQKVAVKCLKDDSTAAQAFLaEASVMTTL-RHPNLVQLLGVVLEGNGLYIVTEYMAKgS 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 123 LEDLFDLCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 191
Cdd:cd05039   87 LVDYLRSRGRAvITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDN-----VAKVSDFGLAKE 151
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
43-189 2.46e-06

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: 48.87  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL-EPMKSRAPQlHL---EYRFYKQLGSGDGIPQVYYFG-PCGKYnaMVLE 117
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIiDKAKCCGKE-HLienEVSILRRVKHPNIIMLIEEMDtPAELY--LVME 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 118 LLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQvIHIIDFGLA 189
Cdd:cd14184   80 LVKGG--DLFDAITSStkYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKS-LKLGDFGLA 150
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
47-205 2.51e-06

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: 49.13  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRL----GKNLYTNEYVAIKlePMKSRAPQLHLE--YRFYKQLGSGDGIPQVYYFGPC----GKYNAMVL 116
Cdd:cd05080   10 RDLGEGHFGKVSLycydPTNDGTGEMVAVK--ALKADCGPQHRSgwKQEIDILKTLYHENIVKYKGCCseqgGKSLQLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELLgpSLEDLFD-LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYidP 195
Cdd:cd05080   88 EYV--PLGSLRDyLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN-----DRLVKIGDFGLAKAV--P 158
                        170
                 ....*....|
gi 530379706 196 ETKKHIPYRE 205
Cdd:cd05080  159 EGHEYYRVRE 168
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
114-261 2.54e-06

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: 48.95  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 192
Cdd:cd06654   94 VVMEYLaGGSLTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGS-----VKLTDFGFCAQ- 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 IDPETKKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 261
Cdd:cd06654  166 ITPEQSK------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY--LNENPLRALY 226
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
145-300 2.61e-06

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: 49.04  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPEN-FLIGrpgnkTQQVIHIIDFGLA-----KEYIDPETKKHIPYREHKSLTGTARYMSI 218
Cdd:cd14049  128 QLLEGVTYIHSMGIVHRDLKPRNiFLHG-----SDIHVRIGDFGLAcpdilQDGNDSTTMSRLNGLTHTSGVGTCLYAAP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 219 NTHLGKEQSRRDDLEALGHMFMYFLRgslPWqglkaDTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEK 298
Cdd:cd14049  203 EQLEGSHYDFKSDMYSIGVILLELFQ---PF-----GTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSER 274

                 ..
gi 530379706 299 PD 300
Cdd:cd14049  275 PS 276
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
114-190 2.62e-06

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: 49.22  E-value: 2.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 114 MVLELL--GPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAK 190
Cdd:cd14092   76 LVMELLrgGELLERIRKK--KRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDA--EIKIVDFGFAR 150
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
126-271 2.69e-06

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: 48.75  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyidpetkkhipYRE 205
Cdd:cd05607   93 IYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGN-----CRLSDLGLAVE-----------VKE 156
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 206 HKSLT---GTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKEryqkigDTKRAT 271
Cdd:cd05607  157 GKPITqraGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKE------ELKRRT 219
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
49-219 2.85e-06

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: 49.27  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKL--EPMKS--RAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNA-----MVLELL 119
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKlsRPFQSiiHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEfndvyLVTHLM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDlCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeYIDPETKK 199
Cdd:cd07877  105 GADLNNIVK-CQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE-----LKILDFGLAR-HTDDEMTG 176
                        170       180
                 ....*....|....*....|
gi 530379706 200 HIPYREHKSLTGTARYMSIN 219
Cdd:cd07877  177 YVATRWYRAPEIMLNWMHYN 196
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
126-263 2.94e-06

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: 48.81  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyidpetkkhIPYRE 205
Cdd:cd05632   93 IYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGH-----IRISDLGLAVK---------IPEGE 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 206 H-KSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 263
Cdd:cd05632  159 SiRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDR 217
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
145-203 2.96e-06

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: 48.45  E-value: 2.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE--------------------YIDPETKKHIPY 203
Cdd:cd14162  108 QLVAGVEYCHSKGVVHRDLKCENLLLDKNNN-----LKITDFGFARGvmktkdgkpklsetycgsyaYASPEILRGIPY 181
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
48-195 3.00e-06

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: 48.90  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIKlepmKSRAPQlhleyrfykqlgSGDGIP-----QVYYFGPCGKYNamVLELL--- 119
Cdd:cd07845   14 RIGEGTYGIVYRARDTTSGEIVALK----KVRMDN------------ERDGIPisslrEITLLLNLRHPN--IVELKevv 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 -GPSLEDLF---DLCD-----------RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHII 184
Cdd:cd07845   76 vGKHLDSIFlvmEYCEqdlaslldnmpTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG-----CLKIA 150
                        170
                 ....*....|.
gi 530379706 185 DFGLAKEYIDP 195
Cdd:cd07845  151 DFGLARTYGLP 161
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
47-215 3.05e-06

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 48.57  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRAPQLHL-EYRFYKQLGSGDGI---------PQVYyfgpcgkyna 113
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAmkkIRLESEEEGVPSTAIrEISLLKELQHPNIVcledvlmqeNRLY---------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDLC--DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 191
Cdd:cd07861   76 LVFEFLSMDLKKYLDSLpkGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKG-----VIKLADFGLARA 150
                        170       180
                 ....*....|....*....|....*....
gi 530379706 192 Y-IDPETKKH----IPYREHKSLTGTARY 215
Cdd:cd07861  151 FgIPVRVYTHevvtLWYRAPEVLLGSPRY 179
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
145-296 3.15e-06

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: 48.47  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGK 224
Cdd:cd14188  109 QIVSGLKYLHEQEILHRDLKLGNFFI----NENME-LKVGDFGLAARLEPLEHRR-------RTICGTPNYLSPEVLNKQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKRATP----------IEVLCENFPEMATYLRYVRRLD 294
Cdd:cd14188  177 GHGCESDIWALGCVMYTMLLGRPPFE---TTNLKETYRCIREARYSLPssllapakhlIASMLSKNPEDRPSLDEIIRHD 253

                 ..
gi 530379706 295 FF 296
Cdd:cd14188  254 FF 255
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
47-208 3.62e-06

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: 48.75  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSR--APQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMV-LELLGP 121
Cdd:cd07879   21 KQVGSGAYGSVCSAIDKRTGEKVAIKklSRPFQSEifAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQdFYLVMP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLE-DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQvIHIIDFGLAKeYIDPETKKH 200
Cdd:cd07879  101 YMQtDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAV----NEDCE-LKILDFGLAR-HADAEMTGY 174

                 ....*...
gi 530379706 201 IPYREHKS 208
Cdd:cd07879  175 VVTRWYRA 182
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
49-251 3.68e-06

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: 48.48  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLED 125
Cdd:cd14173   10 LGEGAYARVQTCINLITNKEYAVKIiekRPGHSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSILS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYIDPETKKHIPYRE 205
Cdd:cd14173   90 HIHR-RRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSP--VKICDFDLGSGIKLNSDCSPISTPE 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530379706 206 HKSLTGTARYMS--INTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14173  167 LLTPCGSAEYMApeVVEAFNEEASiydKRCDLWSLGVILYIMLSGYPPFVG 217
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
125-249 3.81e-06

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: 48.43  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeYIDPETKkhip 202
Cdd:cd14181  102 ELFDyLTEKvTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL-----DDQLHIKLSDFGFSC-HLEPGEK---- 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 203 YREhksLTGTARYMSI--------NTH--LGKEQsrrdDLEALGHMFMYFLRGSLPW 249
Cdd:cd14181  172 LRE---LCGTPGYLAPeilkcsmdETHpgYGKEV----DLWACGVILFTLLAGSPPF 221
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
42-272 4.10e-06

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: 48.46  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEyrfykqlgsgdgipqvyyfgpCGKYNAMVLELLG- 120
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVE---------------------CTMVEKRVLALSGk 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 -PSLEDL---FDLCDRT-FSLKTV----LMIAIQLISRME----------------YVHSKNLIYRDVKPENFLIGRPGN 175
Cdd:cd05616   60 pPFLTQLhscFQTMDRLyFVMEYVnggdLMYHIQQVGRFKephavfyaaeiaiglfFLQSKGIIYRDLKLDNVMLDSEGH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 176 ktqqvIHIIDFGLAKEYI-DPETKkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 254
Cdd:cd05616  140 -----IKIADFGMCKENIwDGVTT--------KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDE 206
                        250
                 ....*....|....*...
gi 530379706 255 DTLkerYQKIGDTKRATP 272
Cdd:cd05616  207 DEL---FQSIMEHNVAYP 221
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
47-248 4.67e-06

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: 48.12  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAM--VLELLGP-SL 123
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLwiIMEYLGGgSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDL-----FDlcdrTFSLKTVLMiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETK 198
Cdd:cd06640   90 LDLlragpFD----EFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLLSEQGD-----VKLADFGVAGQLTDTQIK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530379706 199 KhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06640  158 R-------NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
42-196 4.77e-06

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: 48.34  E-value: 4.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPM--KSRAPQLHLEyRFYKQLGSGDGIPQVYYFGPCGKYNAMVL 116
Cdd:cd05610    5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVvkkADMinKNMVHQVQAE-RDALALSKSPFIVHLYYSLQSANNVYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 E-LLG---PSLEDLFDLCDRTFSLKTVLMIAIQLisrmEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd05610   84 EyLIGgdvKSLLHIYGYFDEEMAVKYISEVALAL----DYLHRHGIIHRDLKPDNMLISNEGH-----IKLTDFGLSKVT 154

                 ....
gi 530379706 193 IDPE 196
Cdd:cd05610  155 LNRE 158
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
43-203 4.94e-06

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: 47.97  E-value: 4.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHL-EYRFYKQLgsgDGIPQVYYFGPCGKYNA--MVLELL 119
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARrELALLAEL---DHKSIVRFHDAFEKRRVviIVTELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPslEDLFDLCDRTFSLKT-VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTQQViHIIDFGLAKEyIDPETK 198
Cdd:cd14108   81 HE--ELLERITKRPTVCESeVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMA--DQKTDQV-RICDFGNAQE-LTPNEP 154

                 ....*
gi 530379706 199 KHIPY 203
Cdd:cd14108  155 QYCKY 159
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
49-216 4.98e-06

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: 47.83  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLepMKSRAPQLHL------EYRFYKQLGSGDGIPQVYYF---GPCGkynaMVLELL 119
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKC--LHSSPNCIEErkallkEAEKMERARHSYVLPLLGVCverRSLG----LVMEYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVH--SKNLIYRDVKPENFLIgrpgNKTQQVIhIIDFGLAKEYIdpE 196
Cdd:cd13978   75 eNGSLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL----DNHFHVK-ISDFGLSKLGM--K 147
                        170       180
                 ....*....|....*....|
gi 530379706 197 TKKHIPYREHKSLTGTARYM 216
Cdd:cd13978  148 SISANRRRGTENLGGTPIYM 167
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
48-220 5.00e-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: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIK-----LEPmKSRApQLHLEYRFYKQLG-----SGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd14038    1 RLGTGGFGNVLRWINQETGEQVAIKqcrqeLSP-KNRE-RWCLEIQIMKRLNhpnvvAARDVPEGLQKLAPNDLPLLAME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LL-GPSLEDLFDLCDRTFSLK--TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNktQQVIH-IIDFGLAKE-- 191
Cdd:cd14038   79 YCqGGDLRKYLNQFENCCGLRegAILTLLSDISSALRYLHENRIIHRDLKPENIVL-QQGE--QRLIHkIIDLGYAKEld 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530379706 192 -------------YIDPEtkkhipYREHKSLTGTARYMSINT 220
Cdd:cd14038  156 qgslctsfvgtlqYLAPE------LLEQQKYTVTVDYWSFGT 191
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
43-195 5.10e-06

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: 47.96  E-value: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRA-PQLHLEYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLELLgp 121
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTrARAFQERDILARL-SHRRLTCLLDQFETRKTLILILELC-- 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 122 SLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnkTQQVIHIIDFGLAKEyIDP 195
Cdd:cd14107   81 SSEELLDRLFLKGVVteAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSP---TREDIKICDFGFAQE-ITP 152
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
43-263 5.24e-06

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: 47.93  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRAPQLHLEYRFYKQLGSGDGI--PQVYYfgpCGKYNAMVL 116
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKinreKAGSSAVKLLEREVDILKHVNHAHIIhlEEVFE---TPKRMYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRP--GNKTQQVIHIIDFGLAKEyi 193
Cdd:cd14097   80 ELCeDGELKELLLR-KGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiiDNNDKLNIKVTDFGLSVQ-- 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 194 dpetKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQK 263
Cdd:cd14097  157 ----KYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRK 222
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
114-250 5.31e-06

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: 47.74  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL--GPSLEDLfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd14118   93 MVFELVdkGAVMEVP---TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH-----VKIADFGVSNE 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 192 Y--IDPETkkhipyrehKSLTGTARYMSINTHLGKEQS---RRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14118  165 FegDDALL---------SSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFE 219
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
45-255 5.62e-06

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: 47.73  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGKnlYTNEyVAIKLEPMkSRAPQLHLEyrFYKQLGSG------DGIpqVYYFGPCGKYN--AMVL 116
Cdd:cd14063    4 IKEVIGKGRFGRVHRGR--WHGD-VAIKLLNI-DYLNEEQLE--AFKEEVAAykntrhDNL--VLFMGACMDPPhlAIVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 117 ELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKtqqvIHIIDFGLAK--EYI 193
Cdd:cd14063   76 SLCkGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENGR----VVITDFGLFSlsGLL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 194 DPETKKH---IPYrehksltGTARYMS--INTHLGKEQSRRDDLE--------ALGHMFMYFLRGSLPWQGLKAD 255
Cdd:cd14063  150 QPGRREDtlvIPN-------GWLCYLApeIIRALSPDLDFEESLPftkasdvyAFGTVWYELLAGRWPFKEQPAE 217
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
42-189 5.67e-06

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 48.31  E-value: 5.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSRAPQL-HLeyRFYKQLGSGDGIP---QVYYFGPCGKYNAMV 115
Cdd:cd05629    2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKtlLKSEMFKKDQLaHV--KAERDVLAESDSPwvvSLYYSFQDAQYLYLI 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 116 LELLgPSlEDLFDLCDR--TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd05629   80 MEFL-PG-GDLMTMLIKydTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH-----IKLSDFGLS 148
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
43-264 5.91e-06

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: 47.81  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLyTNEYVAIKL--EPMKSRAPQLHLEYRFYKQLGSGDGIpQVYYFGPCGKYNAMVLELL- 119
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKIlkSDDLLKQQDFQKEVQALKRLRHKHLI-SLFAVCSVGEPVYIITELMe 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLA---KEYIDP 195
Cdd:cd05148   86 kGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGE-----DLVCKVADFGLArliKEDVYL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 196 ETKKHIPYRehksltGTARYMSINTHLgkeqSRRDDLEALGhMFMY--FLRGSLPWQGLkadTLKERYQKI 264
Cdd:cd05148  161 SSDKKIPYK------WTAPEAASHGTF----STKSDVWSFG-ILLYemFTYGQVPYPGM---NNHEVYDQI 217
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
145-264 6.08e-06

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 47.95  E-value: 6.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHLGK 224
Cdd:cd05585  102 ELLCALECLHKFNVIYRDLKPENILLDYTGH-----IALCDFGLCKLNMKDDDKTN-------TFCGTPEYLAPELLLGH 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 264
Cdd:cd05585  170 GYTKAVDWWTLGVLLYEMLTGLPPFYD---ENTNEMYRKI 206
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
52-236 6.38e-06

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: 47.71  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  52 GNFGELRLGKnlYTNEYVAIKLEPMKSRAPQLHlEYRFYKQLG-SGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLfDLC 130
Cdd:cd14053    6 GRFGAVWKAQ--YLNRLVAVKIFPLQEKQSWLT-EREIYSLPGmKHENILQFIGAEKHGESLEAEYWLITEFHERG-SLC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 D----RTFSLKTVLMIAIQLISRMEYVHS----------KNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDpe 196
Cdd:cd14053   82 DylkgNVISWNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLL-----KSDLTACIADFGLALKFEP-- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 530379706 197 tkkHIPYREHKSLTGTARYMSINTHLGKEQSRRD-----DLEALG 236
Cdd:cd14053  155 ---GKSCGDTHGQVGTRRYMAPEVLEGAINFTRDaflriDMYAMG 196
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
42-260 6.46e-06

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: 47.82  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTN-EYVAIKLEP----------MKSRApQLHLEYRFYKQLgSGDGIPQVYYFGPCGK 110
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVPLRNTgKPVAIKVVRkadlssdnlkGSSRA-NILKEVQIMKRL-SHPNIVKLLDFQESDE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAMVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI-------------GRPGN 175
Cdd:cd14096   80 YYYIVLELADGG--EIFHQIVRLtyFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrKADDD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 176 KTQQ---------------VIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFM 240
Cdd:cd14096  158 ETKVdegefipgvggggigIVKLADFGLSKQVWDSNT---------KTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLY 228
                        250       260
                 ....*....|....*....|
gi 530379706 241 YFLRGSLPWQGLKADTLKER 260
Cdd:cd14096  229 TLLCGFPPFYDESIETLTEK 248
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
114-236 8.27e-06

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: 47.00  E-value: 8.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLeDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKe 191
Cdd:cd14004   85 LVMEKHGSGM-DLFDFIERKPNMdeKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT-----IKLIDFGSAA- 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530379706 192 YIDPEtkkhiPYrehKSLTGTARYMSI-----NTHLGKEQsrrdDLEALG 236
Cdd:cd14004  158 YIKSG-----PF---DTFVGTIDYAAPevlrgNPYGGKEQ----DIWALG 195
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
139-253 8.38e-06

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: 47.38  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 139 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpetKKHIPYREHKSLTGTARYMSI 218
Cdd:cd07869  105 VKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE-----LKLADFGLAR-------AKSVPSHTYSNEVVTLWYRPP 172
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530379706 219 NTHLGK-EQSRRDDLEALGHMFMYFLRGSLPWQGLK 253
Cdd:cd07869  173 DVLLGStEYSTCLDMWGVGCIFVEMIQGVAAFPGMK 208
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
49-190 8.39e-06

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: 47.67  E-value: 8.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK--LEPMKS--RAPQLHLEYRFYKQL---------------GSGDGIPQVYyfgpcg 109
Cdd:cd07851   23 VGSGAYGQVCSAFDTKTGRKVAIKklSRPFQSaiHAKRTYRELRLLKHMkhenviglldvftpaSSLEDFQDVY------ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 110 kynaMVLELLGPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLA 189
Cdd:cd07851   97 ----LVTHLMGADLNNI--VKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV----NEDCEL-KILDFGLA 165

                 .
gi 530379706 190 K 190
Cdd:cd07851  166 R 166
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
43-191 8.77e-06

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: 47.30  E-value: 8.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVY--YF--GPCGKYNAM--V 115
Cdd:cd06608    8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKiMDIIEDEEEEIKLEINILRKFSNHPNIATFYgaFIkkDPPGGDDQLwlV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LELL-GPSLEDL---FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd06608   88 MEYCgGGSVTDLvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE-----VKLVDFGVSAQ 162
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
124-316 9.53e-06

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: 47.10  E-value: 9.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPETKKhip 202
Cdd:cd05054  125 EDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPDYVR--- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 203 yrehkslTGTAR----YMSINTHLGKEQSRRDDLEALGhMFMY--FLRGSLPWQGLKADtlKERYQKIGDTKRATPievl 276
Cdd:cd05054  197 -------KGDARlplkWMAPESIFDKVYTTQSDVWSFG-VLLWeiFSLGASPYPGVQMD--EEFCRRLKEGTRMRA---- 262
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530379706 277 cenfPEMATYLRYVRRLDFFEKPDYDylRKLFTDLFDRKG 316
Cdd:cd05054  263 ----PEYTTPEIYQIMLDCWHGEPKE--RPTFSELVEKLG 296
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
143-283 9.57e-06

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: 46.95  E-value: 9.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNL---IYRDVKPENFLIGRPG---NKTQQVIHIIDFGLAKEYidpetkkhipyreHK----SLTGT 212
Cdd:cd14147  107 AVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIendDMEHKTLKITDFGLAREW-------------HKttqmSAAGT 173
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 213 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC-ENFPEM 283
Cdd:cd14147  174 YAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGI--DCLAVAY-GVAVNKLTLPIPSTCpEPFAQL 242
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-249 9.75e-06

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: 47.18  E-value: 9.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHIpyrehksltGTARYMSINTH 221
Cdd:cd06619  100 IAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQ-----VKLCDFGVSTQLVNSIAKTYV---------GTNAYMAPERI 165
                         90       100
                 ....*....|....*....|....*...
gi 530379706 222 LGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06619  166 SGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
114-261 1.02e-05

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: 47.02  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEy 192
Cdd:cd06656   93 VVMEYLaGGSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-----VKLTDFGFCAQ- 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 IDPETKKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWqgLKADTLKERY 261
Cdd:cd06656  165 ITPEQSK------RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALY 225
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
145-249 1.05e-05

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: 47.02  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKeyIDPETKkhipYRehKSLTGTARYMSINTHLGK 224
Cdd:cd14082  111 QILVALRYLHSKNIVHCDLKPENVLLASAEPFPQ--VKLCDFGFAR--IIGEKS----FR--RSVVGTPAYLAPEVLRNK 180
                         90       100
                 ....*....|....*....|....*
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd14082  181 GYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
47-189 1.11e-05

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: 46.94  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-----LHLEYRFYKQLGSgdgiPQVYYFGPC--GKYNA-MVLEL 118
Cdd:cd06634   21 REIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNekwqdIIKEVKFLQKLRH----PNTIEYRGCylREHTAwLVMEY 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 119 LGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLA 189
Cdd:cd06634   97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPG-----LVKLGDFGSA 162
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
47-236 1.14e-05

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: 46.97  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-----LHLEYRFYKQLGSGDGIPqvyYFGPCGKYNA--MVLELL 119
Cdd:cd06635   31 REIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNekwqdIIKEVKFLQRIKHPNSIE---YKGCYLREHTawLVMEYC 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAkEYIDPETkk 199
Cdd:cd06635  108 LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ-----VKLADFGSA-SIASPAN-- 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530379706 200 hipyrehkSLTGTARYMSINTHLGKEQSRRD---DLEALG 236
Cdd:cd06635  180 --------SFVGTPYWMAPEVILAMDEGQYDgkvDVWSLG 211
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
42-312 1.15e-05

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: 46.99  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEyVAIKLEPMKSRAPQLHL-EYRFYKQLGSGDGIPQVYYFGPCGKYnaMVLELLG 120
Cdd:cd05069   13 SLRLDVKLGQGCFGEVWMGTWNGTTK-VAIKTLKPGTMMPEAFLqEAQIMKKLRHDKLVPLYAVVSEEPIY--IVTEFMG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 P-SLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYIDPEtk 198
Cdd:cd05069   90 KgSLLDFLKEGDgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD-----NLVCKIADFGLARLIEDNE-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 199 khipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLkadTLKERYQKIGDTKRATPIEVLC 277
Cdd:cd05069  163 ----YTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGM---VNREVLEQVERGYRMPCPQGCP 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 530379706 278 ENFPEMatyLRYVRRLDFFEKPDYDYLRKLFTDLF 312
Cdd:cd05069  236 ESLHEL---MKLCWKKDPDERPTFEYIQSFLEDYF 267
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
49-311 1.18e-05

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: 46.52  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRlgKNLYTNEYVAIKL------EPMKSRAPQLHLEYRFYKQLGSGDGIPqvyYFGPCGK--YNAMVLELL- 119
Cdd:cd14148    2 IGVGGFGKVY--KGLWRGEEVAVKAarqdpdEDIAVTAENVRQEARLFWMLQHPNIIA---LRGVCLNppHLCLVMEYAr 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKN---LIYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYi 193
Cdd:cd14148   77 GGALNRA--LAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPienDDLSGKTLKITDFGLAREW- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 194 dPETKKhipyrehKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADTLKERYqKIGDTKRATPI 273
Cdd:cd14148  154 -HKTTK-------MSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR--EIDALAVAY-GVAMNKLTLPI 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 530379706 274 EVLCenfPE-MATYLRYVRRLDFFEKPDYDYLRKLFTDL 311
Cdd:cd14148  223 PSTC---PEpFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
132-189 1.20e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.58  E-value: 1.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 132 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:PHA03211 255 RPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPED-----ICLGDFGAA 307
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
49-215 1.24e-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: 47.10  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQLGSG----------DGIPQVYYFGPCGKYnAM 114
Cdd:cd07864   15 IGEGTYGQVYKAKDKDTGELVALKkvrLDNEKEGFPITAIrEIKILRQLNHRsvvnlkeivtDKQDALDFKKDKGAF-YL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA----K 190
Cdd:cd07864   94 VFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ-----IKLADFGLArlynS 168
                        170       180
                 ....*....|....*....|....*..
gi 530379706 191 EYIDPETKKHIP--YREHKSLTGTARY 215
Cdd:cd07864  169 EESRPYTNKVITlwYRPPELLLGEERY 195
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
125-189 1.24e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 1.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 125 DLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvihIIDFGLA 189
Cdd:PHA03207 171 DLFTYVDRSgpLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAV-----LGDFGAA 232
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
145-249 1.25e-05

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 46.74  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqviHIIDFGLAkEYIDPE-------TKKHIPyrehksltGTARYMS 217
Cdd:cd13991  106 QALEGLEYLHSRKILHGDVKADNVLLSSDGSDA----FLCDFGHA-ECLDPDglgkslfTGDYIP--------GTETHMA 172
                         90       100       110
                 ....*....|....*....|....*....|..
gi 530379706 218 INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd13991  173 PEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
43-191 1.25e-05

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: 46.59  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-------------LHLEY--RFYKQ-LGSGDGIPQVYYfg 106
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNnsrilrevmllsrLNHQHvvRYYQAwIERANLYIQMEY-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 107 pCGKYnamvlellgpSLED-----LFDLCDRTFSLKTvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvI 181
Cdd:cd14046   86 -CEKS----------TLRDlidsgLFQDTDRLWRLFR------QILEGLAYIHSQGIIHRDLKPVNIFLDSNGN-----V 143
                        170
                 ....*....|
gi 530379706 182 HIIDFGLAKE 191
Cdd:cd14046  144 KIGDFGLATS 153
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
44-248 1.28e-05

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: 46.71  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  44 RVGKKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVY-------YFGPCGKYNAM 114
Cdd:cd13975    3 KLGRELGRGQYGVVYACDSWGGHFPCALKsvVPPDDKHWNDLALEFHYTRSLPKHERIVSLHgsvidysYGGGSSIAVLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELLGpslEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKeyid 194
Cdd:cd13975   83 IMERLH---RDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDK-----KNRAKITDLGFCK---- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 195 PETKKhipyreHKSLTGTARYMSINTHLGKEQSRRdDLEALGHMFMYFLRGS--LP 248
Cdd:cd13975  151 PEAMM------SGSIVGTPIHMAPELFSGKYDNSV-DVYAFGILFWYLCAGHvkLP 199
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
46-191 1.36e-05

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: 46.54  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGkNLYTNEYVAIKlePMKSRAPQlHLEYRFYKQ---LGSGDGIPQVYYFGPCGKYNA--MVLELLg 120
Cdd:cd05085    1 GELLGKGNFGEVYKG-TLKDKTPVAVK--TCKEDLPQ-ELKIKFLSEariLKQYDHPNIVKLIGVCTQRQPiyIVMELV- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 121 PSLEDLFDLCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE 191
Cdd:cd05085   76 PGGDFLSFLRKKKDELKTkqLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGE-----NNALKISDFGMSRQ 143
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
45-252 1.36e-05

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: 46.59  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGKnlyTNEYVAIKLEPMKSRAPQlHLEyRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELL----- 119
Cdd:cd14151   12 VGQRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTPQ-QLQ-AFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVtqwce 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyidpETKK 199
Cdd:cd14151   87 GSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFL-----HEDLTVKIGDFGLAT-----VKSR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 200 HIPYREHKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGL 252
Cdd:cd14151  157 WSGSHQFEQLSGSILWMApevIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI 212
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
114-253 1.39e-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: 46.79  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL--GPSLEDLFDlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKE 191
Cdd:cd14180   78 LVMELLrgGELLDRIKK--KARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGA--VLKVIDFGFARL 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 192 YIDPETKKHIPyrehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK 253
Cdd:cd14180  154 RPQGSRPLQTP-------CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKR 208
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
47-260 1.39e-05

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: 46.23  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPmKSRAPQLHLE--YR---FYKQLgSGDGIPQVYYFGPCGKYNAMVLELlgP 121
Cdd:cd14071    6 RTIGKGNFAVVKLARHRITKTEVAIKIID-KSQLDEENLKkiYRevqIMKML-NHPHIIKLYQVMETKDMLYLVTEY--A 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKk 199
Cdd:cd14071   82 SNGEIFDYLAQHgrMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN-----IKIADFGFSNFFKPGELL- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 200 hipyrehKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQGLKADTLKER 260
Cdd:cd14071  156 -------KTWCGSPPYAAPEVFEGKEYEGPQlDIWSLGVVLYVLVCGALPFDGSTLQTLRDR 210
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-187 1.40e-05

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 46.93  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLepMKSRAP---QLHLEYRFYKQLGSGDgipqvyyfgPCGKYN------------- 112
Cdd:cd14226   21 IGKGSFGQVVKAYDHVEQEWVAIKI--IKNKKAflnQAQIEVRLLELMNKHD---------TENKYYivrlkrhfmfrnh 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 -AMVLELLGPSLEDL-----FdlcdRTFSLKTVLMIAIQLISRMEYVHSKNL--IYRDVKPENFLIGRPgNKTQqvIHII 184
Cdd:cd14226   90 lCLVFELLSYNLYDLlrntnF----RGVSLNLTRKFAQQLCTALLFLSTPELsiIHCDLKPENILLCNP-KRSA--IKII 162

                 ...
gi 530379706 185 DFG 187
Cdd:cd14226  163 DFG 165
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
152-250 1.41e-05

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: 46.44  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 152 YVHSKNLIYRDVKPENFLI--GRpgnktqqvIHIIDFGLAKEyIDPETkKHIpYREHKSltGTARYMS------INTHLG 223
Cdd:cd14131  118 TIHEEGIVHSDLKPANFLLvkGR--------LKLIDFGIAKA-IQNDT-TSI-VRDSQV--GTLNYMSpeaikdTSASGE 184
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530379706 224 KEQ----SRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14131  185 GKPkskiGRPSDVWSLGCILYQMVYGKTPFQ 215
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
43-250 1.41e-05

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 46.98  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQ---LHLEYRFYKQLGSGDGIP----QVYYFGPCGKYnAM 114
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQgetLALNERIMLSLVSTGDCPfivcMTYAFHTPDKL-CF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELL-GPSLEdlFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtqqviHIIDFGLAKEY 192
Cdd:cd05633   86 ILDLMnGGDLH--YHLSQHgVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV-----RISDLGLACDF 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 idpeTKKhipyREHKSLtGTARYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd05633  159 ----SKK----KPHASV-GTHGYMAPEVlQKGTAYDSSADWFSLGCMLFKLLRGHSPFR 208
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
145-217 1.44e-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: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYiDPETKKHIP-------YREHKSLTGTARYMS 217
Cdd:cd07853  111 QILRGLKYLHSAGILHRDIKPGNLLV-----NSNCVLKICDFGLARVE-EPDESKHMTqevvtqyYRAPEILMGSRHYTS 184
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
49-192 1.49e-05

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: 46.49  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVA---IKLEPMKSRApQLHLEYRFYKQLGSGDGIpQVYYFGPCGKYNAMVLELLGPSleD 125
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAakiIKVKGAKERE-EVKNEINIMNQLNHVNLI-QLYDAFESKTNLTLIMEYVDGG--E 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFD-LCDRTFSLKT--VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgNKTQQVIHIIDFGLAKEY 192
Cdd:cd14192   88 LFDrITDESYQLTEldAILFTRQICEGVHYLHQHYILHLDLKPENILCV---NSTGNQIKIIDFGLARRY 154
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
134-254 1.69e-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: 46.28  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYidpeTKKhipyREHKSLtGTA 213
Cdd:cd05606   95 FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGH-----VRISDLGLACDF----SKK----KPHASV-GTH 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530379706 214 RYMSINTHL-GKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 254
Cdd:cd05606  161 GYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKT 202
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
49-190 1.80e-05

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: 46.10  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGknLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSgdgiPQVYYFGPCGKYNAMVLELLGP--SLEDL 126
Cdd:cd14068    2 LGDGGFGSVYRA--VYRGEDVAVKIFNKHTSFRLLRQELVVLSHLHH----PSLVALLAAGTAPRMLVMELAPkgSLDAL 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530379706 127 FDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAK 190
Cdd:cd14068   76 LQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIAKIADYGIAQ 139
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
114-257 1.80e-05

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: 46.10  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLgpSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHI--IDFGLA 189
Cdd:cd14196   85 LILELV--SGGELFDFLAQKESLseEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML---LDKNIPIPHIklIDFGLA 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 190 KEYIDPEtkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 257
Cdd:cd14196  160 HEIEDGV--------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
109-191 1.87e-05

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: 46.47  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 GKYNAMVLELL-GpslEDLFD--LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNkTQQVIHIID 185
Cdd:cd14091   66 GNSVYLVTELLrG---GELLDriLRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESG-DPESLRICD 141

                 ....*.
gi 530379706 186 FGLAKE 191
Cdd:cd14091  142 FGFAKQ 147
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-187 1.92e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 46.62  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSR-APQLHLEYRFYKQLGSGDG--------IPQVYYFGpcgKYNAMVLELL 119
Cdd:cd14225   51 IGKGSFGQVVKALDHKTNEHVAIKIIRNKKRfHHQALVEVKILDALRRKDRdnshnvihMKEYFYFR---NHLCITFELL 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 120 GPSLEDLFDLCD-RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktQQVIHIIDFG 187
Cdd:cd14225  128 GMNLYELIKKNNfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRG---QSSIKVIDFG 193
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
125-251 2.07e-05

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: 46.07  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFD-LCDRTFSLKTV--LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgNKTQQVIHIIDFGLAKEYiDPETKKHI 201
Cdd:cd14190   87 ELFErIVDEDYHLTEVdaMVFVRQICEGIQFMHQMRVLHLDLKPENILCV---NRTGHQVKIIDFGLARRY-NPREKLKV 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 PYrehksltGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14190  163 NF-------GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLG 205
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
47-190 2.10e-05

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: 46.22  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGK----NLYTNEYVAIK-LEPMKSRAPQ--LHLEYRFYKQLgSGDGIpqVYYFGPC----GKYNAMV 115
Cdd:cd05038   10 KQLGEGHFGSVELCRydplGDNTGEQVAVKsLQPSGEEQHMsdFKREIEILRTL-DHEYI--VKYKGVCespgRRSLRLI 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 116 LELLgP--SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 190
Cdd:cd05038   87 MEYL-PsgSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILV-----ESEDLVKISDFGLAK 157
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
86-198 2.15e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 44.56  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  86 EYRFYKQL-GSGDGIPQVYYFGPCGKYnaMVLELL-GPSLEDLFDlcdrTFSLKTVLMIAI-QLISRMeyvHSKNLIYRD 162
Cdd:COG3642    6 EARLLRELrEAGVPVPKVLDVDPDDAD--LVMEYIeGETLADLLE----EGELPPELLRELgRLLARL---HRAGIVHGD 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530379706 163 VKPENFLIGRPGnktqqvIHIIDFGLAKEYIDPETK 198
Cdd:COG3642   77 LTTSNILVDDGG------VYLIDFGLARYSDPLEDK 106
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
42-250 2.23e-05

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: 46.19  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQ---LHLEYRFYKQLGSGDGIPQV----YYFGPCGKYNA 113
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcLDKKRIKMKQgetLALNERIMLSLVSTGDCPFIvcmsYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEdlFDLCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd14223   81 ILDLMNGGDLH--YHLSQHgVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH-----VRISDLGLACDF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 193 idpeTKKhipyREHKSLtGTARYMSINT-HLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd14223  154 ----SKK----KPHASV-GTHGYMAPEVlQKGVAYDSSADWFSLGCMLFKLLRGHSPFR 203
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
143-283 2.56e-05

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: 45.80  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKN---LIYRDVKPENFLIGRP------GNKTqqvIHIIDFGLAKEYidpetkkhipYREHK-SLTGT 212
Cdd:cd14146  108 AVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiehddiCNKT---LKITDFGLAREW----------HRTTKmSAAGT 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 213 ARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC-ENFPEM 283
Cdd:cd14146  175 YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI--DGLAVAY-GVAVNKLTLPIPSTCpEPFAKL 243
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
125-192 2.61e-05

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: 45.67  E-value: 2.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 125 DLFD-LCDRTFSLK---TVLMIAiQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKtqqvIHIIDFGLAKEY 192
Cdd:cd14193   87 ELFDrIIDENYNLTeldTILFIK-QICEGIQYMHQMYILHLDLKPENILcVSREANQ----VKIIDFGLARRY 154
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-203 2.65e-05

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: 45.79  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKS---RAPQLHLEYRFYKQLGSGD--GIPQVYyfgPCGKYNAMVLELLgpSL 123
Cdd:cd14167   11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlegKETSIENEIAVLHKIKHPNivALDDIY---ESGGHLYLIMQLV--SG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 124 EDLFD-LCDRTF-SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK----------- 190
Cdd:cd14167   86 GELFDrIVEKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSK--IMISDFGLSKiegsgsvmsta 163
                        170
                 ....*....|....*..
gi 530379706 191 ----EYIDPETKKHIPY 203
Cdd:cd14167  164 cgtpGYVAPEVLAQKPY 180
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
120-189 2.75e-05

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: 45.46  E-value: 2.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPEN-FLigrpgnKTQQVIHIIDFGLA 189
Cdd:cd14062   72 GSSLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNiFL------HEDLTVKIGDFGLA 136
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
47-312 2.83e-05

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: 45.83  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGkNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFgPCGKYNAMVLELL--GPSLE 124
Cdd:cd05070   15 KRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAV-VSEEPIYIVTEYMskGSLLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPEtkkhipYR 204
Cdd:cd05070   93 FLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG-----NGLICKIADFGLARLIEDNE------YT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 205 EHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFL-RGSLPWQGLKADTLKERYQKigDTKRATPievlcENFP-E 282
Cdd:cd05070  162 ARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMNNREVLEQVER--GYRMPCP-----QDCPiS 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 530379706 283 MATYLRYVRRLDFFEKPDYDYLRKLFTDLF 312
Cdd:cd05070  235 LHELMIHCWKKDPEERPTFEYLQGFLEDYF 264
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
47-190 2.84e-05

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: 45.69  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRL------GKNlyTNEYVAIK-LEPMK--SRAPQLHLEYRFYKQL--------------GSGDGIPQVY 103
Cdd:cd05079   10 RDLGEGHFGKVELcrydpeGDN--TGEQVAVKsLKPESggNHIADLKKEIEILRNLyhenivkykgicteDGGNGIKLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 104 YFGPCGkynamvlellgpSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHI 183
Cdd:cd05079   88 EFLPSG------------SLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV-----ESEHQVKI 150

                 ....*..
gi 530379706 184 IDFGLAK 190
Cdd:cd05079  151 GDFGLTK 157
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
105-217 2.89e-05

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: 45.79  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 105 FGPCGKYNAMVLELlgpsledlfdlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHII 184
Cdd:cd06644   90 FCPGGAVDAIMLEL------------DRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD-----IKLA 152
                         90       100       110
                 ....*....|....*....|....*....|...
gi 530379706 185 DFGLAKEYIDPETKKhipyrehKSLTGTARYMS 217
Cdd:cd06644  153 DFGVSAKNVKTLQRR-------DSFIGTPYWMA 178
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
49-187 3.28e-05

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: 43.58  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFY---KQLGSGDGIPQVYYFGPCGKYNAMVLELL-GPSLE 124
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDilrRLKGLELNIPKVLVTEDVDGPNILLMELVkGGTLI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 125 DLfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFG 187
Cdd:cd13968   81 AY--TQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN-----VKLIDFG 136
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
43-268 3.36e-05

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: 45.39  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRF-YKQLGSGDGIPQVYyfgPCGKYNAMVLELL-G 120
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMrYGQHPNIITLKDVY---DDGRYVYLVTELMkG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL-IGRPGNKTQqvIHIIDFGLAKEYIDPETKK 199
Cdd:cd14177   83 GELLDRI-LRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADS--IRICDFGFAKQLRGENGLL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 200 HIPyrehkslTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTK 268
Cdd:cd14177  160 LTP-------CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGK 221
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
134-217 3.37e-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: 45.42  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyrehKSLTGTA 213
Cdd:cd05605   99 FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGH-----VRISDLGLAVEIPEGETI--------RGRVGTV 165

                 ....
gi 530379706 214 RYMS 217
Cdd:cd05605  166 GYMA 169
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-190 3.43e-05

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 45.31  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLePMKSR---------APQLHLEYRFYKQLGSGdGIPQV-----YYFGP 107
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKF-VPKSRvtewamingPVPVPLEIALLLKASKP-GVPGVirlldWYERP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 108 CGKynAMVLELLGPSlEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIID 185
Cdd:cd14005   79 DGF--LLIMERPEPC-QDLFDFITERGALseNLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI----NLRTGEVKLID 151

                 ....*
gi 530379706 186 FGLAK 190
Cdd:cd14005  152 FGCGA 156
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
109-250 3.50e-05

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: 45.56  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 GKYNAMVLELL-GPSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL--IGRPGnktQQVIHI 183
Cdd:cd13988   65 TRHKVLVMELCpCGSLYTVLEEPSNAYGLpeSEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDG---QSVYKL 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 184 IDFGLAKEYIDPEtkkhipyrEHKSLTGTARYMS--------INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ 250
Cdd:cd13988  142 TDFGAARELEDDE--------QFVSLYGTEEYLHpdmyeravLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
145-203 3.63e-05

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: 45.49  E-value: 3.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQ-QVIHIIDFGLAKE----------------YIDPETKKHIPY 203
Cdd:cd14086  108 QILESVNHCHQNGIVHRDLKPENLLL---ASKSKgAAVKLADFGLAIEvqgdqqawfgfagtpgYLSPEVLRKDPY 180
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
43-275 3.69e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 46.27  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706   43 FRVGKKIGCGNFGELRLGKNLYTNEYV---AIKLEPMKSR-APQLHLEYRFYKQLGSGDGIPQVYYFgpCGKYNAMVLEL 118
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFcwkAISYRGLKEReKSQLVIEVNVMRELKHKNIVRYIDRF--LNKANQKLYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  119 LgpSLEDLFDL------CDRTFSL---KTVLMIAIQLISRMEYVHS-------KNLIYRDVKPEN-FL---IGRPGNKTQ 178
Cdd:PTZ00266   93 M--EFCDAGDLsrniqkCYKMFGKieeHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNiFLstgIRHIGKITA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  179 Q--------VIHIIDFGLAKEyIDPETKKHipyrehkSLTGTARYMS--INTHLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:PTZ00266  171 QannlngrpIAKIGDFGLSKN-IGIESMAH-------SCVGTPYYWSpeLLLHETKSYDDKSDMWALGCIIYELCSGKTP 242
                         250       260
                  ....*....|....*....|....*..
gi 530379706  249 WQglKADTLKeryQKIGDTKRATPIEV 275
Cdd:PTZ00266  243 FH--KANNFS---QLISELKRGPDLPI 264
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
47-190 3.82e-05

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: 45.09  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGknLYTNEY-VAIKLEPMKSRAPQLHL-EYRFYKQLGSGDGIpQVYyfGPCGKYNAM--VLELLG-P 121
Cdd:cd05068   14 RKLGSGQFGEVWEG--LWNNTTpVAVKTLKPGTMDPEDFLrEAQIMKKLRHPKLI-QLY--AVCTLEEPIyiITELMKhG 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd05068   89 SLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENN-----ICKVADFGLAR 152
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
143-277 3.83e-05

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: 45.08  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKN---LIYRDVKPENFLIGRP---GNKTQQVIHIIDFGLAKEYidpetkkhipYREHK-SLTGTARY 215
Cdd:cd14061   98 AIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienEDLENKTLKITDFGLAREW----------HKTTRmSAAGTYAW 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 216 MS---INTHLgkeQSRRDDLEALGHMFMYFLRGSLPWQGLkaDTLKERYqKIGDTKRATPIEVLC 277
Cdd:cd14061  168 MApevIKSST---FSKASDVWSYGVLLWELLTGEVPYKGI--DGLAVAY-GVAVNKLTLPIPSTC 226
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
49-191 4.02e-05

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: 45.16  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSgdgiPQVYYF-GPC---GKYNAMVLELLGPSLE 124
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREVQLMNRLSH----PNILRFmGVCvhqGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 125 DLFDlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHiiDFGLAKE 191
Cdd:cd14155   77 QLLD-SNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVG--DFGLAEK 140
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
88-251 4.16e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 45.78  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  88 RFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLedlfdlcdrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPEN 167
Cdd:PTZ00267 129 KHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHL---------PFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSAN 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 168 FLIGRPGnktqqVIHIIDFGLAKEYIDPetkkhIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSL 247
Cdd:PTZ00267 200 IFLMPTG-----IIKLGDFGFSKQYSDS-----VSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHR 269

                 ....
gi 530379706 248 PWQG 251
Cdd:PTZ00267 270 PFKG 273
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
47-196 4.46e-05

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: 44.91  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGK-NLYTNeyVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYF---GPCgkynAMVLELL--G 120
Cdd:cd14203    1 VKLGQGCFGEVWMGTwNGTTK--VAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVvseEPI----YIVTEFMskG 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 121 PSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPE 196
Cdd:cd14203   75 SLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVG-----DNLVCKIADFGLARLIEDNE 145
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-190 4.47e-05

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 45.06  E-value: 4.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 114 MVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd07844   75 LVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE-----LKLADFGLAR 146
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
145-276 4.69e-05

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 45.25  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidPETKKHipyREHKSLTGTARYMSINTHLG- 223
Cdd:cd05586  104 ELVLALEHLHKNDIVYRDLKPENILLDANGH-----IALCDFGLSK----ADLTDN---KTTNTFCGTTEYLAPEVLLDe 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530379706 224 KEQSRRDDLEALGHMFMYFLRGslpWQGLKADTLKERYQKIGDTKRATPIEVL 276
Cdd:cd05586  172 KGYTKMVDFWSLGVLVFEMCCG---WSPFYAEDTQQMYRNIAFGKVRFPKDVL 221
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
131-248 4.74e-05

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: 44.98  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKTQQVIHIIDFGLAKEYIDP---ETKKHIPYREHK 207
Cdd:cd14172   97 DQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLY--TSKEKDAVLKLTDFGFAKETTVQnalQTPCYTPYYVAP 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530379706 208 SLTGTARYmsinthlgkeqSRRDDLEALGhMFMYFLRGSLP 248
Cdd:cd14172  175 EVLGPEKY-----------DKSCDMWSLG-VIMYILLCGFP 203
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
143-249 5.08e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 45.36  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYidpETKKHipyrehkSLTGTARYMSINTHL 222
Cdd:PTZ00426 137 AAQIVLIFEYLQSLNIVYRDLKPENLLLDKDG-----FIKMTDFGFAKVV---DTRTY-------TLCGTPEYIAPEILL 201
                         90       100
                 ....*....|....*....|....*..
gi 530379706 223 GKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:PTZ00426 202 NVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
114-257 5.09e-05

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: 45.01  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSleDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPEN-FLIGRpgNKTQQVIHIIDFGLAK 190
Cdd:cd14194   85 LILELVAGG--ELFDFLAEKESLteEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDR--NVPKPRIKIIDFGLAH 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 191 EyIDPETkkhipyrEHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWQG-LKADTL 257
Cdd:cd14194  161 K-IDFGN-------EFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPFLGdTKQETL 220
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
47-205 5.24e-05

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: 45.01  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGK----NLYTNEYVAIKlEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPC---GKYN-AMVLEL 118
Cdd:cd14205   10 QQLGKGNFGSVEMCRydplQDNTGEVVAVK-KLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCysaGRRNlRLIMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LgP--SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyIDPE 196
Cdd:cd14205   89 L-PygSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV-----ENENRVKIGDFGLTK--VLPQ 160

                 ....*....
gi 530379706 197 TKKHIPYRE 205
Cdd:cd14205  161 DKEYYKVKE 169
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-205 5.26e-05

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: 44.80  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLCDRT---FSLKTVLMIAIQLISRMEYVH-SKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGL 188
Cdd:cd08528   86 IVMELIeGAPLGEHFSSLKEKnehFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLG-----EDDKVTITDFGL 160
                         90       100       110
                 ....*....|....*....|....*....|...
gi 530379706 189 AKE----------------YIDPETKKHIPYRE 205
Cdd:cd08528  161 AKQkgpesskmtsvvgtilYSCPEIVQNEPYGE 193
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
43-187 6.15e-05

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: 44.64  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL----------EPMKSRAPQ----LHLE--YRFYKQLGSGDGIPQVYYFG 106
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKIldktkldqktQRLLSREISsmekLHHPniIRLYEVVETLSKLHLVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 107 PCGKYNAMVLElLGPSLEdlfDLCDRTFSlktvlmiaiQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDF 186
Cdd:cd14075   84 SGGELYTKIST-EGKLSE---SEAKPLFA---------QIVSAVKHMHENNIIHRDLKAENVFYASNN-----CVKVGDF 145

                 .
gi 530379706 187 G 187
Cdd:cd14075  146 G 146
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
142-189 6.47e-05

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: 44.86  E-value: 6.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLA 189
Cdd:cd07852  112 IMYQLLKALKYLHSGGVIHRDLKPSNILL-----NSDCRVKLADFGLA 154
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
42-215 6.54e-05

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 44.91  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEY-RFYKQLGSGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd05599    2 DFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKlrkSEMLEKEQVAHVRAeRDILAEADNPWVVKLYYSFQDEENLYLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 118 LL--GpsleDLFDLCDR--TFSLK-TVLMIAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKey 192
Cdd:cd05599   82 FLpgG----DMMTLLMKkdTLTEEeTRFYIA-ETVLAIESIHKLGYIHRDIKPDNLLLDARGH-----IKLSDFGLCT-- 149
                        170       180
                 ....*....|....*....|...
gi 530379706 193 idPETKKHIPYrehkSLTGTARY 215
Cdd:cd05599  150 --GLKKSHLAY----STVGTPDY 166
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
145-200 6.94e-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: 44.82  E-value: 6.94e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAKEYIDPETKKH 200
Cdd:cd07834  111 QILRGLKYLHSAGVIHRDLKPSNILV----NSNCDL-KICDFGLARGVDPDEDKGF 161
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
145-196 7.00e-05

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: 44.48  E-value: 7.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPE 196
Cdd:cd14080  110 QLALAVQYLHSLDIAHRDLKCENILLDSNNN-----VKLSDFGFARLCPDDD 156
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
148-220 7.36e-05

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: 44.52  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 148 SRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqvIH-IIDFGLAK---------------EYIDPEtkkhipYREHKSLTG 211
Cdd:cd14039  110 SGIQYLHENKIIHRDLKPENIVLQEINGKI---VHkIIDLGYAKdldqgslctsfvgtlQYLAPE------LFENKSYTV 180

                 ....*....
gi 530379706 212 TARYMSINT 220
Cdd:cd14039  181 TVDYWSFGT 189
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
126-284 7.72e-05

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 44.21  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKkhipyre 205
Cdd:cd05631   91 IYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGH-----IRISDLGLAVQIPEGETV------- 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 206 hKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYqkigDTKRATPIEVLCENFPEMA 284
Cdd:cd05631  159 -RGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEV----DRRVKEDQEEYSEKFSEDA 232
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
150-216 8.06e-05

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: 44.27  E-value: 8.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 150 MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyREHKSLTGTARYM 216
Cdd:cd06610  115 LEYLHSNGQIHRDVKAGNILLGEDGS-----VKIADFGVSASLATGGDRTR---KVRKTFVGTPCWM 173
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
43-208 8.13e-05

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: 44.56  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK--LEPMKSR--APQLHLEYRFYKQLGSGDGIPQVYYFGP---CGKYNA-- 113
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKklYRPFQSElfAKRAYRELRLLKHMKHENVIGLLDVFTPdlsLDRFHDfy 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDLcdRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyI 193
Cdd:cd07880   97 LVMPFMGTDLGKLMKH--EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCE-----LKILDFGLARQ-T 168
                        170
                 ....*....|....*
gi 530379706 194 DPETKKHIPYREHKS 208
Cdd:cd07880  169 DSEMTGYVVTRWYRA 183
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
114-215 8.34e-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: 44.25  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL--GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrPGNKTQQVIHIIDFGLAKE 191
Cdd:cd14170   76 IVMECLdgGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY--TSKRPNAILKLTDFGFAKE 153
                         90       100
                 ....*....|....*....|....*..
gi 530379706 192 ---YIDPETKKHIPYREHKSLTGTARY 215
Cdd:cd14170  154 ttsHNSLTTPCYTPYYVAPEVLGPEKY 180
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
49-189 8.35e-05

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: 44.63  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGDG----IPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd14229    8 LGRGTFGQVVKCWKRGTNEIVAVKiLKNHPSYARQGQIEVGILARLSNENAdefnFVRAYECFQHRNHTCLVFEMLEQNL 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 124 EDLfdLCDRTFS---LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLA 189
Cdd:cd14229   88 YDF--LKQNKFSplpLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRV-KVIDFGSA 153
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
47-190 8.37e-05

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: 44.18  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLG--KNLYTNEYVAIKLEPMKSRAP----QLHLEYRFYKQLgsgDGIPQVYYFGPCGKYNAM-VLEL- 118
Cdd:cd05116    1 GELGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPalkdELLREANVMQQL---DNPYIVRMIGICEAESWMlVMEMa 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 119 -LGPSleDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 190
Cdd:cd05116   78 eLGPL--NKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL-----VTQHYAKISDFGLSK 143
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-248 8.67e-05

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 44.28  E-value: 8.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKN-LIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 220
Cdd:cd06650  108 VSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 173
                         90       100
                 ....*....|....*....|....*...
gi 530379706 221 HLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06650  174 LQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
48-190 9.02e-05

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: 44.17  E-value: 9.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRlgKNLYTNEY----VAIKL---EPMKSRAPQLHLEYRFYKQLgsgDGIPQVYYFGPCGKYNAM-VLELL 119
Cdd:cd05115   11 ELGSGNFGCVK--KGVYKMRKkqidVAIKVlkqGNEKAVRDEMMREAQIMHQL---DNPYIVRMIGVCEAEALMlVMEMA 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 120 --GPsLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 190
Cdd:cd05115   86 sgGP-LNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL-----VNQHYAKISDFGLSK 152
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
130-236 9.21e-05

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: 43.96  E-value: 9.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 130 CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEyIDPEtkkhipYREHKSL 209
Cdd:cd08221   94 KNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD-----LVKLGDFGISKV-LDSE------SSMAESI 161
                         90       100
                 ....*....|....*....|....*..
gi 530379706 210 TGTARYMSINTHLGKEQSRRDDLEALG 236
Cdd:cd08221  162 VGTPYYMSPELVQGVKYNFKSDIWAVG 188
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
142-273 9.81e-05

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: 43.92  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKeyidpETKKHIPYREhkslTGTARYMSINTH 221
Cdd:cd08530  108 IFIQMLRGLKALHDQKILHRDLKSANILLSAGD-----LVKIGDLGISK-----VLKKNLAKTQ----IGTPLYAAPEVW 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530379706 222 LGKEQSRRDDLEALGHMFMYFLRGSLPWQglkADTLKERYQKIGDTKrATPI 273
Cdd:cd08530  174 KGRPYDYKSDIWSLGCLLYEMATFRPPFE---ARTMQELRYKVCRGK-FPPI 221
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
125-249 1.11e-04

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: 43.75  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFD-LCDR-TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEyIDPETKKhip 202
Cdd:cd14182   96 ELFDyLTEKvTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN-----IKLTDFGFSCQ-LDPGEKL--- 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 203 yrehKSLTGTARYM-------SINTH---LGKEQsrrdDLEALGHMFMYFLRGSLPW 249
Cdd:cd14182  167 ----REVCGTPGYLapeiiecSMDDNhpgYGKEV----DMWSTGVIMYTLLAGSPPF 215
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
142-257 1.13e-04

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: 43.92  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLIsrmeYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTH 221
Cdd:cd05587  106 IAVGLF----FLHSKGIIYRDLKLDNVMLDAEGH-----IKIADFGMCKEGIFGGKTT-------RTFCGTPDYIAPEII 169
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 530379706 222 LGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05587  170 AYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDEL 205
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
142-216 1.14e-04

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 44.23  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 142 IAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipYREHkSLTGTARYM 216
Cdd:cd05598  107 IA-ELVCAIESVHKMGFIHRDIKPDNILIDRDGH-----IKLTDFGLCTGFRWTHDSKY--YLAH-SLVGTPNYI 172
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
121-257 1.19e-04

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: 43.80  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFD---LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-----EY 192
Cdd:cd05099  115 PGPDYTFDitkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLV-----TEDNVMKIADFGLARgvhdiDY 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 193 IDPETKKHIPYrehKSLTGTARYMSINTHlgkeQSRRDDLEALghMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05099  190 YKKTSNGRLPV---KWMAPEALFDRVYTH----QSDVWSFGIL--MWEIFTLGGSPYPGIPVEEL 245
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
137-192 1.23e-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: 43.87  E-value: 1.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 137 KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd07862  110 ETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ-----IKLADFGLARIY 160
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
142-196 1.26e-04

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: 43.56  E-value: 1.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA--------------KEYIDPE 196
Cdd:cd14052  111 ILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT-----LKIGDFGMAtvwplirgieregdREYIAPE 174
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
121-257 1.31e-04

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: 43.86  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 121 PSLEDLFDLC---DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK-----EY 192
Cdd:cd05100  115 PGMDYSFDTCklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV-----TEDNVMKIADFGLARdvhniDY 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 193 IDPETKKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05100  190 YKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLLWEIFTLGGSPYPGIPVEEL 245
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
47-215 1.35e-04

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 43.67  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHL-EYRFYKQLGSG--------------DGIPQVYyfgpc 108
Cdd:cd07837    7 EKIGEGTYGKVYKARDKNTGKLVALKktrLEMEEEGVPSTALrEVSLLQMLSQSiyivrlldvehveeNGKPLLY----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 gkynaMVLELLGPSLEDLFDLCDRTFS----LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHII 184
Cdd:cd07837   82 -----LVFEYLDTDLKKFIDSYGRGPHnplpAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLV----DKQKGLLKIA 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530379706 185 DFGLAKEYIDPeTKKH------IPYREHKSLTGTARY 215
Cdd:cd07837  153 DLGLGRAFTIP-IKSYtheivtLWYRAPEVLLGSTHY 188
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
145-192 1.45e-04

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: 43.55  E-value: 1.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd07857  113 QILCGLKYIHSANVLHRDLKPGNLLVNADCE-----LKICDFGLARGF 155
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
49-189 1.49e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 43.59  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGDG----IPQVYYFGPCGKYNAMVLELLGPSL 123
Cdd:cd14211    7 LGRGTFGQVVKCWKRGTNEIVAIKiLKNHPSYARQGQIEVSILSRLSQENAdefnFVRAYECFQHKNHTCLVFEMLEQNL 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 124 EDLfdLCDRTFS---LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLA 189
Cdd:cd14211   87 YDF--LKQNKFSplpLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPYRV-KVIDFGSA 152
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
75-312 1.56e-04

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: 43.81  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  75 PMKSRAPQLHLEYRFYKQLGSGD-----GIPQVYYFGPCGKYNAmvlellgPSLEDLFDLCDRTFSLKTVLMIAIQLISR 149
Cdd:cd05102  112 PYRERSPRTRSQVRSMVEAVRADrrsrqGSDRVASFTESTSSTN-------QPRQEVDDLWQSPLTMEDLICYSFQVARG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 150 MEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-YIDPEtkkhipYREHKSLTGTARYMSINTHLGKEQSR 228
Cdd:cd05102  185 MEFLASRKCIHRDLAARNILLSE-----NNVVKICDFGLARDiYKDPD------YVRKGSARLPLKWMAPESIFDKVYTT 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 229 RDDLEALG-HMFMYFLRGSLPWQGLKADtlKERYQKIGDTKRATPievlcenfPEMATYLRYVRRL-----DFFEKPDYD 302
Cdd:cd05102  254 QSDVWSFGvLLWEIFSLGASPYPGVQIN--EEFCQRLKDGTRMRA--------PEYATPEIYRIMLscwhgDPKERPTFS 323
                        250
                 ....*....|
gi 530379706 303 YLRKLFTDLF 312
Cdd:cd05102  324 DLVEILGDLL 333
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
145-192 1.62e-04

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: 43.41  E-value: 1.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd07863  116 QFLRGLDFLHANCIVHRDLKPENILVTSGGQ-----VKLADFGLARIY 158
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
145-195 1.72e-04

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: 43.43  E-value: 1.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKtQQVIHIIDFGLAKEYIDP 195
Cdd:cd07842  116 QILNGIHYLHSNWVLHRDLKPANILVMGEGPE-RGVVKIGDLGLARLFNAP 165
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
43-254 1.73e-04

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: 43.17  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGelRLGKNLYTNEY------VAIKlEPMKSRAPQLHLEY-RFYKQLGSGDGIPQVYYFGPC-GKYNAM 114
Cdd:cd05057    9 LEKGKVLGSGAFG--TVYKGVWIPEGekvkipVAIK-VLREETGPKANEEIlDEAYVMASVDHPHLVRLLGIClSSQVQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLEL--LGPSLEDLFDLCDRTFSlKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeY 192
Cdd:cd05057   86 ITQLmpLGCLLDYVRNHRDNIGS-QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLV-----KTPNHVKITDFGLAK-L 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 193 IDPEtKKHIPYREHKSltgTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKA 254
Cdd:cd05057  159 LDVD-EKEYHAEGGKV---PIKWMALESIQYRIYTHKSDVWSYGvTVWELMTFGAKPYEGIPA 217
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
131-191 1.85e-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: 1.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 131 DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktQQVIHIIDFGLAKE 191
Cdd:cd14089   94 DSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGP--NAILKLTDFGFAKE 152
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
49-205 1.87e-04

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: 43.34  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRL------GKNlyTNEYVAIKlEPMKSRAPQL---HLEYRFYKQLGSgDGIpqVYYFGPCGKYNAMVLELL 119
Cdd:cd05081   12 LGKGNFGSVELcrydplGDN--TGALVAVK-QLQHSGPDQQrdfQREIQILKALHS-DFI--VKYRGVSYGPGRRSLRLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 gpsLEDLFDLCDRTFSLK--------TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKe 191
Cdd:cd05081   86 ---MEYLPSGCLRDFLQRhrarldasRLLLYSSQICKGMEYLGSRRCVHRDLAARNILV-----ESEAHVKIADFGLAK- 156
                        170
                 ....*....|....
gi 530379706 192 yIDPETKKHIPYRE 205
Cdd:cd05081  157 -LLPLDKDYYVVRE 169
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
114-326 1.91e-04

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: 43.07  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLgpSLEDLFDLCDRTFSL--KTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgRPGNKTQQVIHIIDFGLAke 191
Cdd:cd14195   85 LILELV--SGGELFDFLAEKESLteEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML-LDKNVPNPRIKLIDFGIA-- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 192 yidpetKKHIPYREHKSLTGTARYMS---INTH-LGKEQsrrdDLEALGHMFMYFLRGSLPWqglkadtlkeryqkIGDT 267
Cdd:cd14195  160 ------HKIEAGNEFKNIFGTPEFVApeiVNYEpLGLEA----DMWSIGVITYILLSGASPF--------------LGET 215
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 268 KRATPIEVLCENFPEMATYLRYVRRLdffekpDYDYLRKLFT-DLFDRKGYMFDYEYDWI 326
Cdd:cd14195  216 KQETLTNISAVNYDFDEEYFSNTSEL------AKDFIRRLLVkDPKKRMTIAQSLEHSWI 269
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
138-190 2.09e-04

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: 42.79  E-value: 2.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530379706 138 TVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 190
Cdd:cd05052  105 VLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGE-----NHLVKVADFGLSR 152
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
49-217 2.21e-04

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: 42.81  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRlgKNLYTNEYVAIKLEPMKSRAPQLHLEYRfykQLGSGDGIPQVYYFGPCGKYNA--MVLELL-GPSLED 125
Cdd:cd14058    1 VGRGSFGVVC--KARWRNQIVAVKIIESESEKKAFEVEVR---QLSRVDHPNIIKLYGACSNQKPvcLVMEYAeGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LF--DLCDRTFSLKTVLMIAIQLISRMEYVHS---KNLIYRDVKPENFLIGRPGnktqQVIHIIDFGLAkeyidpeTKKH 200
Cdd:cd14058   76 VLhgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGG----TVLKICDFGTA-------CDIS 144
                        170
                 ....*....|....*..
gi 530379706 201 IPYREHKsltGTARYMS 217
Cdd:cd14058  145 THMTNNK---GSAAWMA 158
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
114-251 2.21e-04

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: 42.63  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELlgPSLEDLFD-LCDRT-FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd14161   79 IVMEY--ASRGDLYDyISERQrLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN-----IKIADFGLSNL 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530379706 192 YidpETKKHIpyrehKSLTGTARYMSINTHLGKEQSRRD-DLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14161  152 Y---NQDKFL-----QTYCGSPLYASPEIVNGRPYIGPEvDSWSLGVLLYILVHGTMPFDG 204
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
43-203 2.31e-04

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: 43.11  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEP---MKSRAPQLHLEYRFYKQLGSGDGIP-QVYYFGPCGKYnaMVLEL 118
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPkkaLKGKESSIENEIAVLRKIKHENIVAlEDIYESPNHLY--LVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 LgpSLEDLFD-LCDRTF-SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKE----- 191
Cdd:cd14168   90 V--SGGELFDrIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESK--IMISDFGLSKMegkgd 165
                        170       180
                 ....*....|....*....|..
gi 530379706 192 ----------YIDPETKKHIPY 203
Cdd:cd14168  166 vmstacgtpgYVAPEVLAQKPY 187
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
114-189 2.42e-04

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: 42.67  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSleDLFDLCDRT--FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI--GRPGNKTqqvIHIIDFGLA 189
Cdd:cd14183   81 LVMELVKGG--DLFDAITSTnkYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSKS---LKLGDFGLA 155
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
45-257 2.47e-04

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: 43.08  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGKNLYTN-----EYVAIKLEPMKSRAPQLHL-----EYRFYKQLGSGDGIpqVYYFGPCGKYNAM 114
Cdd:cd05101   28 LGKPLGEGCFGQVVMAEAVGIDkdkpkEAVTVAVKMLKDDATEKDLsdlvsEMEMMKMIGKHKNI--INLLGACTQDGPL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 --VLELLG-------------PSLEDLFDLC---DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnK 176
Cdd:cd05101  106 yvIVEYASkgnlreylrarrpPGMEYSYDINrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV-----T 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 177 TQQVIHIIDFGLAK-----EYIDPETKKHIPYrehKSLTGTARYMSINTHlgkeqsrRDDLEALG-HMFMYFLRGSLPWQ 250
Cdd:cd05101  181 ENNVMKIADFGLARdinniDYYKKTTNGRLPV---KWMAPEALFDRVYTH-------QSDVWSFGvLMWEIFTLGGSPYP 250

                 ....*..
gi 530379706 251 GLKADTL 257
Cdd:cd05101  251 GIPVEEL 257
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
45-257 2.64e-04

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: 42.69  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGKNL-----YTNEYVAIKLEPMKSRAPQLHL-----EYRFYKQLGSGDGIpqVYYFGPCGKYNAM 114
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAIgldkdKPNRVTKVAVKMLKSDATEKDLsdlisEMEMMKMIGKHKNI--INLLGACTQDGPL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 --VLELLG-------------PSLEDLFD---LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnK 176
Cdd:cd05098   95 yvIVEYASkgnlreylqarrpPGMEYCYNpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV-----T 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 177 TQQVIHIIDFGLAKEYidpetkKHIPYREhKSLTG--TARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLK 253
Cdd:cd05098  170 EDNVMKIADFGLARDI------HHIDYYK-KTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGvLLWEIFTLGGSPYPGVP 242

                 ....
gi 530379706 254 ADTL 257
Cdd:cd05098  243 VEEL 246
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
150-191 2.98e-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: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530379706 150 MEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKE 191
Cdd:cd05589  114 LQFLHEHKIVYRDLKLDNLLLDTEG-----YVKIADFGLCKE 150
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
109-236 3.00e-04

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: 42.49  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 GKYNAMVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFG 187
Cdd:cd14154   62 DKKLNLITEYIpGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLV-----REDKTVVVADFG 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 188 LAKEYIDP----------ETKKHIPYREHK---SLTGTARYMSINTHLGKEQSRRDDLEALG 236
Cdd:cd14154  137 LARLIVEErlpsgnmspsETLRHLKSPDRKkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFG 198
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
148-251 3.17e-04

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: 42.32  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 148 SRMEYVHSKNLIYRDVKPENFLIGRPgNKTQQViHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMS-----INTHL 222
Cdd:cd14174  111 SALDFLHTKGIAHRDLKPENILCESP-DKVSPV-KICDFDLGSGVKLNSACTPITTPELTTPCGSAEYMApevveVFTDE 188
                         90       100
                 ....*....|....*....|....*....
gi 530379706 223 GKEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14174  189 ATFYDKRCDLWSLGVILYIMLSGYPPFVG 217
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
42-191 3.24e-04

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: 42.47  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELR------LGKNLYTNEyVAIKLEPMKSRAPQ---LHLEYRFYKQLGSGDGIpqVYYFGPCGKYN 112
Cdd:cd05055   36 NLSFGKTLGAGAFGKVVeataygLSKSDAVMK-VAVKMLKPTAHSSEreaLMSELKIMSHLGNHENI--VNLLGACTIGG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLGPSLEDLFDLCDRT----FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnkTQ-QVIHIIDFG 187
Cdd:cd05055  113 PILVITEYCCYGDLLNFLRRKresfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL------THgKIVKICDFG 186

                 ....
gi 530379706 188 LAKE 191
Cdd:cd05055  187 LARD 190
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
132-285 3.36e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 42.93  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 132 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYIDPETKKhipyrEHKSLTG 211
Cdd:PTZ00283 138 RTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG-----LVKLGDFGFSKMYAATVSDD-----VGRTFCG 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 212 TARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-----TLKERYQKIGDTKRatpievlcenfPEMAT 285
Cdd:PTZ00283 208 TPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEevmhkTLAGRYDPLPPSIS-----------PEMQE 275
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
42-254 3.39e-04

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: 42.38  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQ-------LHLEYRFYKQLGSGDgipQVYYFGPCGKYNAM 114
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPEtskevsaLECEIQLLKNLQHER---IVQYYGCLRDRAEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 115 VLELL-----GPSLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLA 189
Cdd:cd06651   85 TLTIFmeympGGSVKDQLKAYG-ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGN-----VKLGDFGAS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 190 KEYidpeTKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKA 254
Cdd:cd06651  159 KRL----QTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEA 219
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
42-217 3.63e-04

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: 42.34  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRApQLHLEYRFYKQLGSGDgipQVYYFGPCGKYNAMVLEL 118
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKvikLEPGEDFA-VVQQEIIMMKDCKHSN---IVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 119 L---GPSLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDP 195
Cdd:cd06645   88 EfcgGGSLQDIYHVTG-PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGH-----VKLADFGVSAQITAT 161
                        170       180
                 ....*....|....*....|..
gi 530379706 196 ETKKhipyrehKSLTGTARYMS 217
Cdd:cd06645  162 IAKR-------KSFIGTPYWMA 176
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
134-250 3.86e-04

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: 41.86  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 134 FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYIDPetkkhipyrEHKSLTGT- 212
Cdd:cd05112   97 FSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGE-----NQVVKVSDFGMTRFVLDD---------QYTSSTGTk 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530379706 213 --ARYMSINTHLGKEQSRRDDLEALGhMFMY--FLRGSLPWQ 250
Cdd:cd05112  163 fpVKWSSPEVFSFSRYSSKSDVWSFG-VLMWevFSEGKIPYE 203
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
133-204 3.98e-04

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: 42.02  E-value: 3.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 133 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE--YID---PETKKHIPYR 204
Cdd:cd05053  129 QLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE-----DNVMKIADFGLARDihHIDyyrKTTNGRLPVK 200
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
114-217 4.19e-04

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: 42.04  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELL-GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd06611   79 ILIEFCdGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD-----VKLADFGVSAKN 153
                         90       100
                 ....*....|....*....|....*
gi 530379706 193 IDPETKKHipyrehkSLTGTARYMS 217
Cdd:cd06611  154 KSTLQKRD-------TFIGTPYWMA 171
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
132-193 4.31e-04

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: 42.20  E-value: 4.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 132 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI 193
Cdd:cd05590   91 RRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGH-----CKLADFGMCKEGI 147
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
43-189 4.31e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. 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 HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 42.38  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEY--RFYKQLGSGDGIPQVYYFGPCGKYNAMVLE 117
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIlknHPSYARQGQIEVSIlaRLSTESADDYNFVRAYECFQHKNHTCLVFE 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 118 LLGPSLEDLfdLCDRTFS---LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLA 189
Cdd:cd14227   97 MLEQNLYDF--LKQNKFSplpLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRV-KVIDFGSA 168
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
45-251 4.77e-04

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: 42.02  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFGELRLGKNLYTNEYVAIKL---EPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYnAMVLELL-- 119
Cdd:cd14090    6 TGELLGEGAYASVQTCINLYTGKEYAVKIiekHPGHSRSRVFREVETLHQCQGHPNILQLIEYFEDDERF-YLVFEKMrg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDlcDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqQV--IHIIDFGLAK------E 191
Cdd:cd14090   85 GPLLSHIEK--RVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMD----KVspVKICDFDLGSgiklssT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530379706 192 YIDPETKKhipyrEHKSLTGTARYMS---INTHLGKEQS--RRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14090  159 SMTPVTTP-----ELLTPVGSAEYMApevVDAFVGEALSydKRCDLWSLGVILYIMLCGYPPFYG 218
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
125-190 4.84e-04

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: 41.84  E-value: 4.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRT----FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd05574   87 ELFRLLQKQpgkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGH-----IMLTDFDLSK 151
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
140-191 5.15e-04

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: 41.98  E-value: 5.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530379706 140 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKE 191
Cdd:cd05048  127 LHIAIQIAAGMEYLSSHHYVHRDLAARNCLVG-----DGLTVKISDFGLSRD 173
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
143-264 5.40e-04

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: 41.82  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKHipyrehkSLTGTARYMSINTHL 222
Cdd:cd05570  102 AAEICLALQFLHERGIIYRDLKLDNVLLDAEGH-----IKIADFGMCKEGIWGGNTTS-------TFCGTPDYIAPEILR 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530379706 223 GKEQSRRDDLEALGHMFMYFLRGSLPWQGlkaDTLKERYQKI 264
Cdd:cd05570  170 EQDYGFSVDWWALGVLLYEMLAGQSPFEG---DDEDELFEAI 208
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
113-190 5.73e-04

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: 41.57  E-value: 5.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 113 AMVLEL-LGPSLEDLFDlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktQQVIHIIDFGLAK 190
Cdd:cd14106   84 ILILELaAGGELQTLLD-EEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFP--LGDIKLCDFGISR 159
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
111-189 5.81e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 41.90  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQ--LISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 188
Cdd:PHA03212 154 YNKFTCLILPRYKTDLYCYLAAKRNIAICDILAIErsVLRAIQYLHENRIIHRDIKAENIFINHPGD-----VCLGDFGA 228

                 .
gi 530379706 189 A 189
Cdd:PHA03212 229 A 229
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
43-187 5.87e-04

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: 41.51  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK--LEPMK-SRAPQLHlEYRFYKQLGSGDGIP----QVYYFGPCGKYNAMV 115
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKkiLCHSKeDVKEAMR-EIENYRLFNHPNILRlldsQIVKEAGGKKEVYLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 116 LE--LLGpSLEDLFDLCDRT---FSLKTVLMIAIQLISRMEYVHSKNLI---YRDVKPENFLIGRPGnktqqVIHIIDFG 187
Cdd:cd13986   81 LPyyKRG-SLQDEIERRLVKgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDD-----EPILMDLG 154
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
145-198 6.13e-04

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 41.91  E-value: 6.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQViHIIDFGLAKeYIDPETK 198
Cdd:cd07849  114 QILRGLKYIHSANVLHRDLKPSNLLL----NTNCDL-KICDFGLAR-IADPEHD 161
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
47-189 6.60e-04

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: 41.54  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKnlyTNEYVAIKLEPMKSRAPQLHLEYRFYKQ-LGSGDGIPQVYYFGPCGKYNAMVLELL--GPSL 123
Cdd:cd14150    6 KRIGTGSFGTVFRGK---WHGDVAVKILKVTEPTPEQLQAFKNEMQvLRKTRHVNILLFMGFMTRPNFAIITQWceGSSL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 124 EDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLA 189
Cdd:cd14150   83 YRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFL-----HEGLTVKIGDFGLA 143
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
128-190 7.19e-04

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: 41.46  E-value: 7.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 128 DLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpGNKTqqvIHIIDFGLAK 190
Cdd:cd05096  129 AHCLPAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLVG--ENLT---IKIADFGMSR 186
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
127-195 8.43e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 41.60  E-value: 8.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 127 FDLCDRTFsLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDP 195
Cdd:PHA03210 258 FDWKDRPL-LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGK-----IVLGDFGTAMPFEKE 320
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
44-189 8.65e-04

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 40.96  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  44 RVGKKIGCGNFGELRLGKNLYTNEYVAIKL----EPMKSRApqLHLEYRFYKQLGSGDGIPQVY---YFGP------CGK 110
Cdd:cd14036    3 RIKRVIAEGGFAFVYEAQDVGTGKEYALKRllsnEEEKNKA--IIQEINFMKKLSGHPNIVQFCsaaSIGKeesdqgQAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 111 YnAMVLELLGPSLEDLFDLCD--RTFSLKTVLMIAIQLISRMEYVHSKN--LIYRDVKPENFLIGrpgnkTQQVIHIIDF 186
Cdd:cd14036   81 Y-LLLTELCKGQLVDFVKKVEapGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG-----NQGQIKLCDF 154

                 ...
gi 530379706 187 GLA 189
Cdd:cd14036  155 GSA 157
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
132-190 9.13e-04

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: 41.13  E-value: 9.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 132 RTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 190
Cdd:cd05095  126 LTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK-----NYTIKIADFGMSR 179
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
142-249 9.50e-04

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: 40.89  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpETKKHIPYRehKSLTGTARYMSINTH 221
Cdd:cd06648  108 VCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGR-----VKLSDFGFCA-----QVSKEVPRR--KSLVGTPYWMAPEVI 175
                         90       100
                 ....*....|....*....|....*...
gi 530379706 222 LGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06648  176 SRLPYGTEVDIWSLGIMVIEMVDGEPPY 203
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
42-189 9.52e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. 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 HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 41.23  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGDG----IPQVYYFGPCGKYNAMVL 116
Cdd:cd14228   16 SYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKiLKNHPSYARQGQIEVSILSRLSSENAdeynFVRSYECFQHKNHTCLVF 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 117 ELLGPSLEDLfdLCDRTFS---LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQViHIIDFGLA 189
Cdd:cd14228   96 EMLEQNLYDF--LKQNKFSplpLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRV-KVIDFGSA 168
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
42-190 9.57e-04

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: 40.63  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKnlYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGP 121
Cdd:cd05083    7 KLTLGEIIGEGEFGAVLQGE--YMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLYIVMELMSKGN 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 122 SLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd05083   85 LVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG-----VAKISDFGLAK 148
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
143-249 9.59e-04

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: 41.16  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 143 AIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHL 222
Cdd:cd05617  122 AAEICIALNFLHERGIIYRDLKLDNVLLDADGH-----IKLTDYGMCKEGLGPGDTT-------STFCGTPNYIAPEILR 189
                         90       100
                 ....*....|....*....|....*..
gi 530379706 223 GKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd05617  190 GEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
145-236 9.72e-04

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: 41.13  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKKHIPYrehkslTGTARYMSINTHLGK 224
Cdd:cd07848  108 QLIKAIHWCHKNDIVHRDIKPENLLI-----SHNDVLKLCDFGFARNLSEGSNANYTEY------VATRWYRSPELLLGA 176
                         90
                 ....*....|..
gi 530379706 225 EQSRRDDLEALG 236
Cdd:cd07848  177 PYGKAVDMWSVG 188
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
135-197 1.05e-03

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: 40.87  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 135 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPgnktqQVIHIIDFGLAKeYIDPET 197
Cdd:cd05056  105 DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSP-----DCVKLGDFGLSR-YMEDES 161
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
48-249 1.10e-03

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: 40.78  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKnlyTNEYVAIKLEPMKSRAPQLHLEYRF-YKQLGSGDGIPQVYYFGPCGKYN-AMVLELL-GPSLE 124
Cdd:cd14149   19 RIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQFQAFRNeVAVLRKTRHVNILLFMGYMTKDNlAIVTQWCeGSSLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKEYIDPETKKHIpyr 204
Cdd:cd14149   96 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLTVKIGDFGLATVKSRWSGSQQV--- 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 530379706 205 ehKSLTGTARYMS---INTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd14149  168 --EQPTGSILWMApevIRMQDNNPFSFQSDVYSYGIVLYELMTGELPY 213
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
49-194 1.15e-03

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 40.81  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIK---LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVY--YF--GPCgkynAMVLELLGP 121
Cdd:cd06616   14 IGRGAFGTVNKMLHKPSGTIMAVKrirSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYgaLFreGDC----WICMELMDI 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 122 SLEDLFDLC----DRTFSLKTVLMIAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYID 194
Cdd:cd06616   90 SLDKFYKYVyevlDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGN-----IKLCDFGISGQLVD 162
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
145-326 1.40e-03

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 40.78  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAKeyIDPETKKHIPYrehkslTGTARYMSINTHLGK 224
Cdd:cd07876  131 QMLCGIKHLHSAGIIHRDLKPSNIVV-----KSDCTLKILDFGLAR--TACTNFMMTPY------VVTRYYRAPEVILGM 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQGlkADTLkERYQKIgdtkratpIEVLCENFPEMATYLRYVRRLDFFEKPDYDYL 304
Cdd:cd07876  198 GYKENVDIWSVGCIMGELVKGSVIFQG--TDHI-DQWNKV--------IEQLGTPSAEFMNRLQPTVRNYVENRPQYPGI 266
                        170       180
                 ....*....|....*....|..
gi 530379706 305 RklFTDLFDRKGYMFDYEYDWI 326
Cdd:cd07876  267 S--FEELFPDWIFPSESERDKL 286
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
46-193 1.41e-03

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: 40.47  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  46 GKKIGCGNFGELRLGKNLYTNEYVAIK-LEPMK----SRApQLHLEYRFYKqLGSGDGIPQVYYFGPCGKYNAMVLELlG 120
Cdd:cd14074    8 EETLGRGHFAVVKLARHVFTGEKVAVKvIDKTKlddvSKA-HLFQEVRCMK-LVQHPNVVRLYEVIDTQTKLYLILEL-G 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 121 PSlEDLFDLC---DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEYI 193
Cdd:cd14074   85 DG-GDMYDYImkhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVF----FEKQGLVKLTDFGFSNKFQ 155
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
48-249 1.46e-03

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: 40.41  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  48 KIGCGNFGELRLGKNLYTNEYVAIK-LEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELL-GPSLED 125
Cdd:cd06658   29 KIGEGSTGIVCIATEKHTGKQVAVKkMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLeGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 126 LfdLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKeyidpETKKHIPYRe 205
Cdd:cd06658  109 I--VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR-----IKLSDFGFCA-----QVSKEVPKR- 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530379706 206 hKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06658  176 -KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY 218
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
45-306 1.49e-03

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: 40.30  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  45 VGKKIGCGNFG---ELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEY-------------RFYKQLG-----SGDGIPQVY 103
Cdd:cd14204   11 LGKVLGEGEFGsvmEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFlseaacmkdfnhpNVIRLLGvclevGSQRIPKPM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 104 YFGPCGKYNAMVLELLGPSLEDlfdlCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHI 183
Cdd:cd14204   91 VILPFMKYGDLHSFLLRSRLGS----GPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCML-----RDDMTVCV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 184 IDFGLAKEYIDPETkkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALG-HMFMYFLRGSLPWQGLKADTLKErYQ 262
Cdd:cd14204  162 ADFGLSKKIYSGDY-----YRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGvTMWEIATRGMTPYPGVQNHEIYD-YL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 530379706 263 KIGDTKRATPievlcENFPEMATYLRYVRRLDFFEKPDYDYLRK 306
Cdd:cd14204  236 LHGHRLKQPE-----DCLDELYDIMYSCWRSDPTDRPTFTQLRE 274
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
88-249 1.56e-03

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: 40.38  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  88 RFYKQLGSGDGIPQVYYFGPCGKYNAMvLELLGPSLEDLFDLCDRT----FSLKTVLMIAIQLISRMEYVHSKNLIYRDV 163
Cdd:cd05094   71 KFYGVCGDGDPLIMVFEYMKHGDLNKF-LRAHGPDAMILVDGQPRQakgeLGLSQMLHIATQIASGMVYLASQHFVHRDL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 164 KPENFLIGrpgnkTQQVIHIIDFGLAKEYIDPETkkhipYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGH-MFMYF 242
Cdd:cd05094  150 ATRNCLVG-----ANLLVKIGDFGMSRDVYSTDY-----YRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGViLWEIF 219

                 ....*..
gi 530379706 243 LRGSLPW 249
Cdd:cd05094  220 TYGKQPW 226
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
133-191 1.64e-03

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: 40.40  E-value: 1.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 133 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGrpgnkTQQVIHIIDFGLAKE 191
Cdd:cd05051  127 TLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVG-----PNYTIKIADFGMSRN 180
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
147-243 1.97e-03

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: 39.96  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 147 ISRMEYVhSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYI-DPETKKHIPYREHKSLT-GTARYMS---INTH 221
Cdd:cd14037  121 VAAMHYL-KPPLIHRDLKVENVLISDSGN-----YKLCDFGSATTKIlPPQTKQGVTYVEEDIKKyTTLQYRApemIDLY 194
                         90       100
                 ....*....|....*....|..
gi 530379706 222 LGKEQSRRDDLEALGhMFMYFL 243
Cdd:cd14037  195 RGKPITEKSDIWALG-CLLYKL 215
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
42-236 1.98e-03

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: 39.70  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGEL-----RLGKNLYTNEYVAIKLEPMKSRAPQLHlEYRFYKQLGSgdgiPQV--YY--FGPCGKYN 112
Cdd:cd08529    1 DFEILNKLGKGSFGVVykvvrKVDGRVYALKQIDISRMSRKMREEAID-EARVLSKLNS----PYVikYYdsFVDKGKLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 aMVLELL-GPSLEDLFDL-CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAK 190
Cdd:cd08529   76 -IVMEYAeNGDLHSLIKSqRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN-----VKIGDLGVAK 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 191 eYIDPETKKhipyreHKSLTGTARYMSINTHLGKEQSRRDDLEALG 236
Cdd:cd08529  150 -ILSDTTNF------AQTIVGTPYYLSPELCEDKPYNEKSDVWALG 188
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
114-210 2.11e-03

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 40.13  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 114 MVLELLGPSLEDLFDLCDRtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAKEYI 193
Cdd:PTZ00024  97 LVMDIMASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKG-----ICKIADFGLARRYG 170
                         90
                 ....*....|....*..
gi 530379706 194 DPETKKHIPYREHKSLT 210
Cdd:PTZ00024 171 YPPYSDTLSKDETMQRR 187
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
136-189 2.22e-03

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: 40.11  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530379706 136 LKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLA 189
Cdd:cd14013  119 NVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIV----SEGDGQFKIIDLGAA 168
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
139-187 2.30e-03

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 40.03  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 139 VLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRP-----------GNKTqQVIHIIDFG 187
Cdd:cd13981  108 AMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEicadwpgegenGWLS-KGLKLIDFG 166
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
145-255 2.32e-03

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 39.83  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAKEYidPETKKHIPYRehkslTGTARYMSINTHLGK 224
Cdd:cd14094  117 QILEALRYCHDNNIIHRDVKPHCVLLASKENSAP--VKLGGFGVAIQL--GESGLVAGGR-----VGTPHFMAPEVVKRE 187
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQGLKAD 255
Cdd:cd14094  188 PYGKPVDVWGCGVILFILLSGCLPFYGTKER 218
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
42-192 2.41e-03

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 39.77  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSR--APQLHL-EYRFYKQLgSGDGIPQVYYFGPCGKYNAMVLEL 118
Cdd:cd07836    1 NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEegTPSTAIrEISLMKEL-KHENIVRLHDVIHTENKLMLVFEY 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 119 LGPSLEDLFDL--CDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEY 192
Cdd:cd07836   80 MDKDLKKYMDThgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE-----LKLADFGLARAF 150
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
133-191 2.54e-03

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: 39.52  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 133 TFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKE 191
Cdd:cd05074  119 TLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT-----VCVADFGLSKK 172
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
135-190 2.71e-03

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: 39.57  E-value: 2.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530379706 135 SLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAK 190
Cdd:cd05097  127 SIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGN-----HYTIKIADFGMSR 177
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
152-257 2.72e-03

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: 39.60  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 152 YVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIdpetkkhIPYREHKSLTGTARYMSINTHLGKEQSRRDD 231
Cdd:cd05615  126 FLHKKGIIYRDLKLDNVMLDSEGH-----IKIADFGMCKEHM-------VEGVTTRTFCGTPDYIAPEIIAYQPYGRSVD 193
                         90       100
                 ....*....|....*....|....*.
gi 530379706 232 LEALGHMFMYFLRGSLPWQGLKADTL 257
Cdd:cd05615  194 WWAYGVLLYEMLAGQPPFDGEDEDEL 219
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
145-190 2.83e-03

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: 39.34  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGnktqqVIHIIDFGLAK 190
Cdd:cd06631  111 QILEGVAYLHNNNVIHRDIKGNNIMLMPNG-----VIKLIDFGCAK 151
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-248 2.85e-03

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 39.65  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSKN-LIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 220
Cdd:cd06649  108 VSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 173
                         90       100
                 ....*....|....*....|....*...
gi 530379706 221 HLGKEQSRRDDLEALGHMFMYFLRGSLP 248
Cdd:cd06649  174 LQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
145-258 2.92e-03

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: 39.49  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpGNKTQQVIHIIDFGLAKEyIDPEtkkhipyREHKSLTGTARYMSINTHLGK 224
Cdd:cd14114  108 QVCEGLCHMHENNIVHLDIKPENIMC---TTKRSNEVKLIDFGLATH-LDPK-------ESVKVTTGTAEFAAPEIVERE 176
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530379706 225 EQSRRDDLEALGHMFMYFLRGSLPWQGLKAD-TLK 258
Cdd:cd14114  177 PVGFYTDMWAVGVLSYVLLSGLSPFAGENDDeTLR 211
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
140-306 2.98e-03

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: 39.64  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 140 LMIAIQLISRMEYVHsknliyRDVKPENFLIGRPGNktqqvIHIIDFG----LAK-------------EYIDPETKKHIP 202
Cdd:cd05597  111 MVLAIDSIHQLGYVH------RDIKPDNVLLDRNGH-----IRLADFGsclkLREdgtvqssvavgtpDYISPEILQAME 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 203 yrehkslTGTARYmsinthlGKEQsrrdDLEALGhMFMY-FLRGSLPWQglkADTLKERYQKIGDTKRATPIEVLCENFP 281
Cdd:cd05597  180 -------DGKGRY-------GPEC----DWWSLG-VCMYeMLYGETPFY---AESLVETYGKIMNHKEHFSFPDDEDDVS 237
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530379706 282 EMATYLryVRRL-------------------DFFEKPDYDYLRK 306
Cdd:cd05597  238 EEAKDL--IRRLicsrerrlgqngiddfkkhPFFEGIDWDNIRD 279
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
122-276 3.34e-03

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: 39.27  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 122 SLEDLFDLCDrTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTqqVIHIIDFGLAKEYIDPETKKHI 201
Cdd:cd14012   90 SLSELLDSVG-SVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTG--IVKLTDYSLGKTLLDMCSRGSL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 202 pyREHKSltgTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQglKADT---------LKERYQ-------KIG 265
Cdd:cd14012  167 --DEFKQ---TYWLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLE--KYTSpnpvlvsldLSASLQdflskclSLD 239
                        170
                 ....*....|.
gi 530379706 266 DTKRATPIEVL 276
Cdd:cd14012  240 PKKRPTALELL 250
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
150-249 3.41e-03

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: 39.63  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 150 MEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKKhipyrehKSLTGTARYMSINTHLGKEQSRR 229
Cdd:cd05618  134 LNYLHERGIIYRDLKLDNVLLDSEGH-----IKLTDYGMCKEGLRPGDTT-------STFCGTPNYIAPEILRGEDYGFS 201
                         90       100
                 ....*....|....*....|
gi 530379706 230 DDLEALGHMFMYFLRGSLPW 249
Cdd:cd05618  202 VDWWALGVLMFEMMAGRSPF 221
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
145-190 3.47e-03

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 39.32  E-value: 3.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIgrpgnKTQQVIHIIDFGLAK 190
Cdd:cd07850  110 QMLCGIKHLHSAGIIHRDLKPSNIVV-----KSDCTLKILDFGLAR 150
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
140-204 3.80e-03

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: 39.22  E-value: 3.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 140 LMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKE-----YIDPETKKHIPYR 204
Cdd:cd05090  127 LHIAIQIAAGMEYLSSHFFVHKDLAARNILVGE-----QLHVKISDLGLSREiyssdYYRVQNKSLLPIR 191
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
43-187 3.91e-03

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 39.34  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSR-APQLHLEYRFYKQL------GSGDGIPQVYYFgPCGKYNAMV 115
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRfHRQAAEEIRILEHLkkqdkdNTMNVIHMLESF-TFRNHICMT 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 116 LELLGpslEDLFDLCDRT----FSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLI---GRPGnktqqvIHIIDFG 187
Cdd:cd14224  146 FELLS---MNLYELIKKNkfqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLkqqGRSG------IKVIDFG 215
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
47-188 3.93e-03

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 39.26  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  47 KKIGCGNFGELRLGKNLYTNEYVAIKLEPMKS---RAPQLHLE--------------YRFYKQLGSGDGIPQVYYFGPCG 109
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDvllRNQVAHVKaerdilaeadnewvVRLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530379706 110 KYNAMVLELlGPSLEDLfdlcdrtfslkTVLMIAiQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGL 188
Cdd:cd05625   87 DMMSLLIRM-GVFPEDL-----------ARFYIA-ELTCAVESVHKMGFIHRDIKPDNILIDRDGH-----IKLTDFGL 147
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
120-239 4.47e-03

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: 38.78  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETKK 199
Cdd:cd14221   74 GGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKS-----VVVADFGLARLMVDEKTQP 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530379706 200 HIPYREHK-------SLTGTARYMSINTHLGKEQSRRDDLEALGHMF 239
Cdd:cd14221  149 EGLRSLKKpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
Pkinase pfam00069
Protein kinase domain;
43-72 4.99e-03

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 38.38  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 530379706   43 FRVGKKIGCGNFGELRLGKNLYTNEYVAIK 72
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK 30
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
145-190 5.35e-03

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: 38.65  E-value: 5.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQqvIHIIDFGLAK 190
Cdd:cd14085  106 QILEAVAYLHENGIVHRDLKPENLLYATPAPDAP--LKIADFGLSK 149
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-304 5.42e-03

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: 38.51  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPetkkhipyREHKSLTGTARYMS--- 217
Cdd:cd06618  119 MTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGN-----VKLCDFGISGRLVDS--------KAKTRSAGCAAYMAper 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 218 INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTlkERYQKIGDTkrATPIEVLCENF-PEMATYLRYVRRLDFF 296
Cdd:cd06618  186 IDPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEF--EVLTKILNE--EPPSLPPNEGFsPDFCSFVDLCLTKDHR 261

                 ....*...
gi 530379706 297 EKPDYDYL 304
Cdd:cd06618  262 YRPKYREL 269
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
129-190 5.44e-03

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: 38.69  E-value: 5.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530379706 129 LCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgNKTQQVIHIIDFGLAK 190
Cdd:cd13977  126 LLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISH--KRGEPILKVADFGLSK 185
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
125-202 5.48e-03

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: 38.75  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 125 DLFDLC----DRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFL---IGRPGNktqqvIHIIDFGLAK------- 190
Cdd:cd14198   94 EIFNLCvpdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGD-----IKIVDFGMSRkighace 168
                         90       100
                 ....*....|....*....|
gi 530379706 191 --------EYIDPETKKHIP 202
Cdd:cd14198  169 lreimgtpEYLAPEILNYDP 188
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
136-172 5.60e-03

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: 38.54  E-value: 5.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530379706 136 LKTVLMiaiQLISRMEYVHSKNLIYRDVKPENFLIGR 172
Cdd:cd14051  106 LKDLLL---QVAQGLKYIHSQNLVHMDIKPGNIFISR 139
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
109-190 5.78e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 38.70  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 109 GKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIhIIDFGL 188
Cdd:PHA03209 129 GAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFI----NDVDQVC-IGDLGA 203

                 ..
gi 530379706 189 AK 190
Cdd:PHA03209 204 AQ 205
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
42-196 5.89e-03

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: 38.51  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  42 NFRVGKKIGCGNFGELRLGKNLYTNEyVAIKLEPMKSRAPQLHL-EYRFYKQLgSGDGIPQVYYFgPCGKYNAMVLELL- 119
Cdd:cd05071   10 SLRLEVKLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMSPEAFLqEAQVMKKL-RHEKLVQLYAV-VSEEPIYIVTEYMs 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530379706 120 -GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRpgnktQQVIHIIDFGLAKEYIDPE 196
Cdd:cd05071   87 kGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE-----NLVCKVADFGLARLIEDNE 159
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
142-236 6.25e-03

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 38.57  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 142 IAIQLISRMEYVHSK-NLIYRDVKPENFLIGRPGNktqqvIHIIDFGLAKEYIDPETkkhipyrehKSLTGTARYMSINT 220
Cdd:cd06615  104 ISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGE-----IKLCDFGVSGQLIDSMA---------NSFVGTRSYMSPER 169
                         90
                 ....*....|....*.
gi 530379706 221 HLGKEQSRRDDLEALG 236
Cdd:cd06615  170 LQGTHYTVQSDIWSLG 185
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
113-249 7.01e-03

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: 38.18  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 113 AMVLELLGPsledlfdlcdrtFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIgrpgNKTQQVIHIIDFGLAKEY 192
Cdd:cd06630   91 ASLLSKYGA------------FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV----DSTGQRLRIADFGAAARL 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530379706 193 idpETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPW 249
Cdd:cd06630  155 ---ASKGTGAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
145-251 8.14e-03

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: 37.92  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706 145 QLISRMEYVHSKNLIYRDVKPENFL-IGRPGNktqqVIHIIDFGLAKEyIDPETKKHIPYRehksltgTARYMSINTHLG 223
Cdd:cd14104  105 QVCEALEFLHSKNIGHFDIRPENIIyCTRRGS----YIKIIEFGQSRQ-LKPGDKFRLQYT-------SAEFYAPEVHQH 172
                         90       100
                 ....*....|....*....|....*...
gi 530379706 224 KEQSRRDDLEALGHMFMYFLRGSLPWQG 251
Cdd:cd14104  173 ESVSTATDMWSLGCLVYVLLSGINPFEA 200
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
49-190 9.89e-03

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: 37.73  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379706  49 IGCGNFGELRLGKNLYTNEYVAIKLEPMK-----SRAPQLH----LEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELL 119
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKIHQLNkswrdEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYC 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530379706 120 GPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKN--LIYRDVKPENFLIgRPGNKTQQvIHIIDFGLAK 190
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-VDGTACGE-IKITDFGLSK 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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