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Conserved domains on  [gi|23199991|ref|NP_689407|]
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casein kinase I isoform epsilon [Homo sapiens]

Protein Classification

STKc_CK1_delta_epsilon domain-containing protein (domain architecture ID 10197527)

STKc_CK1_delta_epsilon domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

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  Cd Length: 275  Bit Score: 649.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125   1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125  81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125 161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23199991 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125 241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

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  Cd Length: 275  Bit Score: 649.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125   1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125  81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125 161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23199991 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125 241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
8-285 1.04e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 136.80  E-value: 1.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIasgEEVAIK-----LECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVM 82
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKvlakkLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  83 ELL-GPSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDA 159
Cdd:COG0515  78 EYVdGGSLEDLLKKIGRkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 160 RTHQHIPYRENKNLtGTARYASINTHLGIEQ---SRRDDLESLGYVLMYFNLGSLPWQGLKAA-TKRQKYERISEKKMST 235
Cdd:COG0515 156 GSTSSIPALPSTSV-GTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsATSQTLKIILELPTPS 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23199991 236 PIEVLCKGYPSEFSTYLN--FCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYD 285
Cdd:COG0515 235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-238 6.07e-27

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 108.39  E-value: 6.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991      9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     86 -GPSLEDLFNFCsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYRDARTHqh 164
Cdd:smart00220  80 eGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23199991    165 ipyrenKNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY-FNLGSLPWQGlkAATKRQKYERISEKKMSTPIE 238
Cdd:smart00220 154 ------TTFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
Pkinase pfam00069
Protein kinase domain;
9-249 1.12e-23

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 99.21  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKleCVKTKHPQLHIESKFY---KMMQ--GGVGIPSIKWCGAEGDYNVMVME 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK--KIKKEKIKKKKDKNILreiKILKklNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991    84 LLGPSleDLFNFCSRK--FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKYrdart 161
Cdd:pfam00069  79 YVEGG--SLFDLLSEKgaFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENIL--IDEDGNL-KITDFGLARQL----- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   162 HQHIPYrenKNLTGTARYAS----INTHLGIEQsrrdDLESLGYVLMYFNLGSLPWQGlkaATKRQKYERISEKKMSTPI 237
Cdd:pfam00069 149 NSGSSL---TSFVGTPWYMApevlRGNPYGPKV----DVWSLGCILYELLTGKPPFPG---INGNEIYEKIIDQDFDSPR 218
                         250
                  ....*....|..
gi 23199991   238 evlckgyPSEFS 249
Cdd:pfam00069 219 -------PSSIS 223
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 9.62e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 97.33  E-value: 9.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991    6 GNKYRLGRKIGSGSFGDIY---LGANIASGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23199991  219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
119-155 4.86e-03

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 37.96  E-value: 4.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 23199991   119 IHSKNFIHRDVKPDNFLMGLGKkgnlVYIIDFGLAKK 155
Cdd:TIGR03724 106 LHKAGIVHGDLTTSNIIVRDDK----VYLIDFGLGKY 138
 
Name Accession Description Interval E-value
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
8-282 0e+00

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  Cd Length: 275  Bit Score: 649.43  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14125   1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14125  81 SLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLAKKYRDPRTHQHIPY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14125 161 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPIEVLCKGFPSE 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23199991 248 FSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGF 282
Cdd:cd14125 241 FATYLNYCRSLRFDDKPDYSYLRRLFRDLFHREGF 275
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
8-273 0e+00

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  Cd Length: 266  Bit Score: 543.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14016  81 SLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAKKYRDPRTGKHIPY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14016 161 REGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQSKKEKYEKIGEKKMNTSPEELCKGLPKE 240
                       250       260
                ....*....|....*....|....*.
gi 23199991 248 FSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14016 241 FAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
8-273 2.73e-179

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  Cd Length: 266  Bit Score: 504.73  E-value: 2.73e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14128   1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPY 167
Cdd:cd14128  81 SLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDSRTRQHIPY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 168 RENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSE 247
Cdd:cd14128 161 REDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAE 240
                       250       260
                ....*....|....*....|....*.
gi 23199991 248 FSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14128 241 FAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
9-290 5.30e-149

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  Cd Length: 288  Bit Score: 428.38  E-value: 5.30e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPS 88
Cdd:cd14126   2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLELLGPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  89 LEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGL--GKKGNLVYIIDFGLAKKYRDARTHQHIP 166
Cdd:cd14126  82 LEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRqsTKKQHVIHIIDFGLAKEYIDPETNKHIP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 167 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPS 246
Cdd:cd14126 162 YREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPE 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23199991 247 EFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDW 290
Cdd:cd14126 242 EMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDW 285
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
9-281 3.53e-136

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  Cd Length: 277  Bit Score: 395.32  E-value: 3.53e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPS 88
Cdd:cd14127   2 YKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGPS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  89 LEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGL--GKKGNLVYIIDFGLAKKYRDARTHQHIP 166
Cdd:cd14127  82 LEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRpgTKNANVIHVVDFGMAKQYRDPKTKQHIP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 167 YRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPS 246
Cdd:cd14127 162 YREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQSTPIRDLCEGFPE 241
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23199991 247 EFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQG 281
Cdd:cd14127 242 EFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
8-274 6.15e-77

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  Cd Length: 263  Bit Score: 242.93  E-value: 6.15e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLF-NFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLG-KKGNLVYIIDFGLAKKYRDARTHQHI 165
Cdd:cd14017  81 NLAELRrSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGpSDERTVYILDFGLARQYTNKDGEVER 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 166 PYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKaatkrqKYERISEKKMSTPIEVLCKGYP 245
Cdd:cd14017 161 PPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLK------DKEEVGKMKEKIDHEELLKGLP 234
                       250       260
                ....*....|....*....|....*....
gi 23199991 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLFR 274
Cdd:cd14017 235 KEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
5-273 5.33e-55

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  Cd Length: 300  Bit Score: 186.72  E-value: 5.33e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   5 VGNKYRLGRKIGSGSFGDIYLGANiASGEEVAIKLECVKTKHPQ----LHIESKFY----------KMMQGG----VGIP 66
Cdd:cd14015   8 TKRQWKLGKSIGQGGFGEIYLASD-DSTLSVGKDAKYVVKIEPHsngpLFVEMNFYqrvakpemikKWMKAKklkhLGIP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  67 SikwCGAEG-------DYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLG 139
Cdd:cd14015  87 R---YIGSGsheykgeKYRFLVMPRFGRDLQKIFEKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 140 KKGNLVYIIDFGLAKKYRDarTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLK 217
Cdd:cd14015 164 KNKDQVYLVDYGLASRYCP--NGKHKEYKEDprKAHNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWEDNL 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23199991 218 AAT---KRQKyerisEKKMSTPIEVL--C---KGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14015 242 KNPeyvQKQK-----EKYMDDIPLLLkkCfpgKDVPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
8-273 2.50e-45

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  Cd Length: 262  Bit Score: 160.22  E-value: 2.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14129   1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMG-LGKKGNLVYIIDFGLAKKYRDARTHQHI 165
Cdd:cd14129  81 NLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRKCYMLDFGLARQFTNSCGDVRP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 166 PyRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAAtkrqkyERISEKKMSTPIEVLCKGYP 245
Cdd:cd14129 161 P-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYEHRLMLKHLP 233
                       250       260
                ....*....|....*....|....*...
gi 23199991 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14129 234 PEFSVFLDHISGLDYFTKPDYQLLVSVF 261
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
8-273 6.33e-45

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  Cd Length: 262  Bit Score: 159.04  E-value: 6.33e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd14130   1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  88 SLEDLFNFCSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMG-LGKKGNLVYIIDFGLAKKYRDArTHQHI 165
Cdd:cd14130  81 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLARQYTNT-TGEVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 166 PYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMstpievLCKGYP 245
Cdd:cd14130 160 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRM------LLKHMP 233
                       250       260
                ....*....|....*....|....*...
gi 23199991 246 SEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14130 234 SEFHLFLDHIASLDYFTKPDYQLIMSVF 261
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
6-272 1.03e-37

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  Cd Length: 302  Bit Score: 140.37  E-value: 1.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   6 GNKYRLGRKIGSGSFGDIYLGA---NIASGEEV--AIKLEcvKTKHPQLHIESKFY----------KMMQ----GGVGIP 66
Cdd:cd14123  11 KKNWRLGKMIGKGGFGLIYLASpqvNVPVEDDAvhVIKVE--YHENGPLFSELKFYqraakpdtisKWMKskqlDYLGIP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  67 SIkWCGAEGDYN-----VMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgKK 141
Cdd:cd14123  89 TY-WGSGLTEFNgtsyrFMVMDRLGTDLQKILIDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY-RN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 142 GNLVYIIDFGLAkkYRDARTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPW-QGLK- 217
Cdd:cd14123 167 PNEVYLADYGLS--YRYCPNGNHKEYKENprKGHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeQNLKn 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23199991 218 -AATKRQKYERISE-----KKMSTPIEVLCkgypsEFSTYLNFCRSLRFDDKPDYSYLRQL 272
Cdd:cd14123 245 pVAVQEAKAKLLSNlpdsvLKWSTGGSSSM-----EIAQFLSRVKDLAYDEKPDYQALKKI 300
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
8-285 1.04e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 136.80  E-value: 1.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIasgEEVAIK-----LECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVM 82
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKvlakkLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  83 ELL-GPSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDA 159
Cdd:COG0515  78 EYVdGGSLEDLLKKIGRkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 160 RTHQHIPYRENKNLtGTARYASINTHLGIEQ---SRRDDLESLGYVLMYFNLGSLPWQGLKAA-TKRQKYERISEKKMST 235
Cdd:COG0515 156 GSTSSIPALPSTSV-GTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsATSQTLKIILELPTPS 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23199991 236 PIEVLCKGYPSEFSTYLN--FCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYD 285
Cdd:COG0515 235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
8-273 4.41e-34

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  Cd Length: 301  Bit Score: 130.39  E-value: 4.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLgANIASGEEVAIKLECVKTKHPQ----LHIESKFY------KMMQGGVGIPSIKWCGAE--- 74
Cdd:cd14122  11 EWKLGLPIGQGGFGRLYL-ADENSSESVGSDAPYVVKVEPSdngpLFTELKFYmraakpDQIQKWIKSHKLKYLGVPkyw 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  75 ---------GDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgKKGNLV 145
Cdd:cd14122  90 gsglhekngKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSY-KNPDQV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 146 YIIDFGLAkkYRDARTHQHIPYREN--KNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGlkaATKRQ 223
Cdd:cd14122 169 YLVDYGLA--YRYCPEGVHKEYKEDpkRCHDGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWED---NLKDP 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23199991 224 KYERISEKKMSTPIEVL---C---KGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:cd14122 244 NYVRDSKIRYRDNISELmekCfpgKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
15-207 1.24e-33

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  Cd Length: 215  Bit Score: 126.62  E-value: 1.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  15 IGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL-GPSLE 90
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKvipKEKLKKLLEELLREIEILKKLNH-PNIVKLYDVFETENFLYLVMEYCeGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  91 DLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYRDARTHQHIPYRen 170
Cdd:cd00180  80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSLLKTTGG-- 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23199991 171 knlTGTARYASINTHLGIEQSRRDDLESLGYVLMYFN 207
Cdd:cd00180 155 ---TTPPYYAPPELLGGRYYGPKVDIWSLGVILYELE 188
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
8-215 5.30e-27

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  Cd Length: 260  Bit Score: 108.83  E-value: 5.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLecvktKHPQLHIESKFYKMMQ---------GGVGIPSIKWCGAEGDYN 78
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKV-----LRPELAEDEEFRERFLrearalarlSHPNIVRVYDVGEDDGRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  79 VMVMELL-GPSLEDLFNFcSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYR 157
Cdd:cd14014  76 YIVMEYVeGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL--LTEDGR-VKLTDFGIARALG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 158 DAR-THQHIPYrenknltGTARYASINTHLGIEQSRRDDLESLGyVLMYFNL-GSLPWQG 215
Cdd:cd14014 152 DSGlTQTGSVL-------GTPAYMAPEQARGGPVDPRSDIYSLG-VVLYELLtGRPPFDG 203
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-238 6.07e-27

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 108.39  E-value: 6.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991      9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     86 -GPSLEDLFNFCsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYRDARTHqh 164
Cdd:smart00220  80 eGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23199991    165 ipyrenKNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY-FNLGSLPWQGlkAATKRQKYERISEKKMSTPIE 238
Cdd:smart00220 154 ------TTFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
63-270 1.87e-25

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  Cd Length: 298  Bit Score: 104.92  E-value: 1.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  63 VGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:cd14124  82 LGIPSCVGFGVHDSYRFLVFPSLGQSLQSALDEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFVDPEDQS 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 143 NlVYIIDFGLAkkYRDARTHQHIPYRENKNLT--GTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAAT 220
Cdd:cd14124 162 E-VYLAGYGFA--FRYCPGGKHVEYREGSRSPheGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHNT 238
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23199991 221 KRQKYERisEKKMSTPIEVLCKGY-----PSEFSTYLNFCRSLRFDDKPDYSYLR 270
Cdd:cd14124 239 EDIMKQK--ERFMDDVPGFLGPCFhqkkvSEALQKYLKVVMALQYEEKPDYAMLR 291
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
8-236 1.90e-25

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  Cd Length: 252  Bit Score: 104.14  E-value: 1.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK------LECVKTK-------------HPqlHIeSKFYKMMQggvgipsi 68
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkskLKEEIEEkikreieimkllnHP--NI-IKLYEVIE-------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  69 kwcgaEGDYNVMVMELLgpSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVy 146
Cdd:cd14003  70 -----TENKIYLVMEYA--SGGELFDYIVNngRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL--LDKNGNLK- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 147 IIDFGLAKKYRDARTHQhipyrenknlT--GTARYASINTHLGIE-QSRRDDLESLGyVLMYFNL-GSLPWQGlkaATKR 222
Cdd:cd14003 140 IIDFGLSNEFRGGSLLK----------TfcGTPAYAAPEVLLGRKyDGPKADVWSLG-VILYAMLtGYLPFDD---DNDS 205
                       250
                ....*....|....
gi 23199991 223 QKYERISEKKMSTP 236
Cdd:cd14003 206 KLFRKILKGKYPIP 219
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
8-232 1.92e-24

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  Cd Length: 258  Bit Score: 101.40  E-value: 1.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK-----------LECVKT--------KHPqlHIeSKFYKMMQggvgipsi 68
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkkklksedEEMLRReieilkrlDHP--NI-VKLYEVFE-------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  69 kwcgaEGDYNVMVMELL--GpsleDLFNF-CSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNL 144
Cdd:cd05117  70 -----DDKNLYLVMELCtgG----ELFDRiVKKgSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991 145 VYIIDFGLAKKYRDARTHQHipyrenknLTGTARYAS--INTHLGIeqSRRDDLESLGyVLMYFNL-GSLPWQGlkaATK 221
Cdd:cd05117 141 IKIIDFGLAKIFEEGEKLKT--------VCGTPYYVApeVLKGKGY--GKKCDIWSLG-VILYILLcGYPPFYG---ETE 206
                       250
                ....*....|.
gi 23199991 222 RQKYERISEKK 232
Cdd:cd05117 207 QELFEKILKGK 217
Pkinase pfam00069
Protein kinase domain;
9-249 1.12e-23

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 99.21  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKleCVKTKHPQLHIESKFY---KMMQ--GGVGIPSIKWCGAEGDYNVMVME 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIK--KIKKEKIKKKKDKNILreiKILKklNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991    84 LLGPSleDLFNFCSRK--FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKYrdart 161
Cdd:pfam00069  79 YVEGG--SLFDLLSEKgaFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENIL--IDEDGNL-KITDFGLARQL----- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   162 HQHIPYrenKNLTGTARYAS----INTHLGIEQsrrdDLESLGYVLMYFNLGSLPWQGlkaATKRQKYERISEKKMSTPI 237
Cdd:pfam00069 149 NSGSSL---TSFVGTPWYMApevlRGNPYGPKV----DVWSLGCILYELLTGKPPFPG---INGNEIYEKIIDQDFDSPR 218
                         250
                  ....*....|..
gi 23199991   238 evlckgyPSEFS 249
Cdd:pfam00069 219 -------PSSIS 223
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 9.62e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 97.33  E-value: 9.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991    6 GNKYRLGRKIGSGSFGDIY---LGANIASGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23199991  219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
8-167 2.51e-22

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


Pssm-ID: 270692  Cd Length: 254  Bit Score: 95.35  E-value: 2.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK---LEcVKTKHPQLHIESKFYKMMQGgvgiPSI-KWCGA--EGDYNVMV 81
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKkinLE-SKEKKESILNEIAILKKCKH----PNIvKYYGSylKKDELWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  82 MELL-GPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGnLVYIIDFGLAKKYRDAR 160
Cdd:cd05122  76 MEFCsGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTS--DG-EVKLIDFGLSAQLSDGK 152
                       170
                ....*....|
gi 23199991 161 THQHI---PY 167
Cdd:cd05122 153 TRNTFvgtPY 162
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
8-200 3.58e-21

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  Cd Length: 258  Bit Score: 92.20  E-value: 3.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKH-PQLHIESKFYKMMQGgvgiPSI-KWCGAEGD---YNV 79
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEElEALEREIRILSSLKH----PNIvRYLGTERTentLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  80 mVMELL-GPSLEDLF-NFcsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYR 157
Cdd:cd06606  77 -FLEYVpGGSLASLLkKF--GKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL--VDSDGV-VKLADFGCAKRLA 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23199991 158 DARTHQhipyrENKNLTGTARYAS---INthlGIEQSRRDDLESLG 200
Cdd:cd06606 151 EIATGE-----GTKSLRGTPYWMApevIR---GEGYGRAADIWSLG 188
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
9-168 4.70e-20

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  Cd Length: 249  Bit Score: 88.83  E-value: 4.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK-LECVKTKHPQLHIESKFYKMMQGGVGIP-------SIKWcgAEGDYNVM 80
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKkIKNDFRHPKAALREIKLLKHLNDVEGHPnivklldVFEH--RGGNHLCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  81 VMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGNLVYIIDFGLAKKY-RDA 159
Cdd:cd05118  79 VFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINL--ELGQLKLADFGLARSFtSPP 156
                       170
                ....*....|.
gi 23199991 160 RTH--QHIPYR 168
Cdd:cd05118 157 YTPyvATRWYR 167
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
7-215 1.85e-19

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  Cd Length: 278  Bit Score: 87.66  E-value: 1.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   7 NKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLeCVKT------KHPQLHIEsKFYKMMQGGVGIPSIKWCGAEGDYNVM 80
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKV-LDKRhiikekKVKYVTIE-KEVLSRLAHPGIVKLYYTFQDESKLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  81 VMELL-GPSLEDLFNFCSRkFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVyIIDFGLAKKY--- 156
Cdd:cd05581  79 VLEYApNGDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL--LDEDMHIK-ITDFGTAKVLgpd 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23199991 157 -------RDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQG 215
Cdd:cd05581 155 sspestkGDADSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRG 220
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
9-157 7.43e-19

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  Cd Length: 283  Bit Score: 86.05  E-value: 7.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKL---------ECVKTKhpqlhiESKFYKMMQGGVGIPSIKWCGAEGDYNV 79
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKmkkkfysweECMNLR------EVKSLRKLNEHPNIVKLKEVFRENDELY 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23199991  80 MVMELLGPSLEDLF-NFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYR 157
Cdd:cd07830  75 FVFEYMEGNLYQLMkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV---SGPEVVKIADFGLAREIR 150
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
8-213 2.21e-18

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  Cd Length: 265  Bit Score: 84.28  E-value: 2.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991   8 KYRLGRKIGSGSFGDIYLGANIASGEEVA---IKLECVKTK-HPQLHIESKFYKMMQGgvgiPSI-KWCGAEGDYNVMV- 81
Cdd:cd06626   1 RWQRGNKIGEGTFGKVYTAVNLDTGELMAmkeIRFQDNDPKtIKEIADEMKVLEGLDH----PNLvRYYGVEVHREEVYi 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991  82 -MELL-GPSLEDLFNF-------CSRKFSLktvllladQMISRIEYIHSKNFIHRDVKPDNFLMGlgkKGNLVYIIDFGL 152
Cdd:cd06626  77 fMEYCqEGTLEELLRHgrildeaVIRVYTL--------QLLEGLAYLHENGIVHRDIKPANIFLD---SNGLIKLGDFGS 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23199991 153 AKKYRDARThqHIPYRENKNLTGTARYAS---INTHLGIEQSRRDDLESLGYVLMYFNLGSLPW 213
Cdd:cd06626 146 AVKLKNNTT--TMAPGEVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
10-219 2.29e-18

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


Pssm-ID: 197581  Cd Length: 257  Bit Score: 84.12  E-value: 2.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     10 RLGRKIGSGSFGDIYLG----ANIASGEEVAIKleCVKTKHPQLHIEsKFY---KMMQG----------GVgipsikwCG 72
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGklkgKGGKKKVEVAVK--TLKEDASEQQIE-EFLreaRIMRKldhpnvvkllGV-------CT 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23199991     73 AEGDYnVMVMELL-GPSLEDLFNFCSRKFSLKTVLLLADQmISR-IEYIHSKNFIHRDVKPDNFLMGlgkKGNLVYIIDF 150
Cdd:smart00219  72 EEEPL-YIVMEYMeGGDLLSYLRKNRPKLSLSDLLSFALQ-IARgMEYLESKNFIHRDLAARNCLVG---ENLVVKISDF 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23199991    151 GLAKKYRDAR----THQHIPYR----EnknltgtaryaSINTHLGIEQSrrdDLESLGyVLMY--FNLGSLPWQGLKAA 219
Cdd:smart00219 147 GLSRDLYDDDyyrkRGGKLPIRwmapE-----------SLKEGKFTSKS---DVWSFG-VLLWeiFTLGEQPYPGMSNE 210
STKc_CCRK