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Conserved domains on  [gi|32476378|ref|NP_869372|]
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protein kinase-like protein [Rhodopirellula baltica SH 1]

Protein Classification

serine/threonine protein kinase (domain architecture ID 10195858)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
24-274 3.16e-49

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: 173.16  E-value: 3.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQR 103
Cdd:cd14014  14 GEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 104 RGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLS-PVLID---VRDVDGTPPFRSGPYhvsrppsIGQMM 179
Cdd:cd14014  94 RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDfgiARALGDSGLTQTGSV-------LGTPA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 180 RSAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDRLVMQLLNKDPG 259
Cdd:cd14014 167 YMAPEQAR-GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPE 245
                       250
                ....*....|....*
gi 32476378 260 QRPVSAAAVKLQLAE 274
Cdd:cd14014 246 ERPQSAAELLAALRA 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
24-274 3.16e-49

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: 173.16  E-value: 3.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQR 103
Cdd:cd14014  14 GEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 104 RGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLS-PVLID---VRDVDGTPPFRSGPYhvsrppsIGQMM 179
Cdd:cd14014  94 RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDfgiARALGDSGLTQTGSV-------LGTPA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 180 RSAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDRLVMQLLNKDPG 259
Cdd:cd14014 167 YMAPEQAR-GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPE 245
                       250
                ....*....|....*
gi 32476378 260 QRPVSAAAVKLQLAE 274
Cdd:cd14014 246 ERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
24-262 1.82e-22

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 97.60  E-value: 1.82e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378     24 ARVWRAVHIKMRKAVAVRVfqMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQR 103
Cdd:smart00220  13 GKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    104 RGRLPWESVLELAEPLIDALMYLHDRDIVHgR--------ITPDKVI-IA--GLSPVLID---VRDVDGTPPFRsgpyhv 169
Cdd:smart00220  91 RGRLSEDEARFYLRQILSALEYLHSKGIVH-RdlkpenilLDEDGHVkLAdfGLARQLDPgekLTTFVGTPEYM------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    170 srppsigqmmrsAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDRL 249
Cdd:smart00220 164 ------------APEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|...
gi 32476378    250 VMQLLNKDPGQRP 262
Cdd:smart00220 231 IRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-283 7.28e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 94.42  E-value: 7.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMrkaVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHP-AIVKCYGGGFEESEAYLAHELVEGSTLAEEIQ 102
Cdd:COG0515  14 GEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGR---LPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIA--GLSPVLID---VRDVDGTPPFRSGPYHVSrpPS 174
Cdd:COG0515  91 KIGRkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrdGRVVKLIDfglAKLLPDPGSTSSIPALPS--TS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 175 IGQMMRSAPE--APTPNDPVTARTDLYLFGALLYEALTGAPPITG----STVQEVTSNLKYQSPTSVASTV-----MECP 243
Cdd:COG0515 169 VGTPGYMAPEvlLGLSLAYASSSSDIWSLGITLYELLTGLPPFEGeknsSATSQTLKIILELPTPSLASPLspsnpELIS 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32476378 244 VWMDRLVMQLLNKDPGQRPVSAAAVKLQLAEVRKRSMSRS 283
Cdd:COG0515 249 KAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDL 288
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-276 1.88e-18

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 89.52  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378     37 AVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLA-HELVEGSTLAEEIQRRGRLPWESVLEL 115
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAvFEYVPGRTLREVLAADGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    116 AEPLIDALMYLHDRDIVHGRITPDKVIIA-------------GLSPVLIDVRDVDGTPPFRSGPYhvsrppsIGQMMRSA 182
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSqtgvrphakvldfGIGTLLPGVRDADVATLTRTTEV-------LGTPTYCA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    183 PEApTPNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTsnLKYQSPTSVAstvmeCPVWMD-----RLVMQLLNKD 257
Cdd:TIGR03903  158 PEQ-LRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIL--YQQLSPVDVS-----LPPWIAghplgQVLRKALNKD 229
                          250
                   ....*....|....*....
gi 32476378    258 PGQRPVSAAAVKLQLAEVR 276
Cdd:TIGR03903  230 PRQRAASAPALAERFRALE 248
Pkinase pfam00069
Protein kinase domain;
24-262 1.54e-15

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 76.48  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    24 ARVWRAVHIKMRKAVAVRVFqmpfggtqESRQAFAEEWDR-------LKRLDHPAIVKCYGGGFEESEAYLAHELVEGST 96
Cdd:pfam00069  13 GTVYKAKHRDTGKIVAIKKI--------KKEKIKKKKDKNilreikiLKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    97 LAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIA----------GLSPVLI---DVRDVDGTPPFR 163
Cdd:pfam00069  85 LFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDedgnlkitdfGLARQLNsgsSLTSFVGTPWYM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   164 sgpyhvsrppsigqmmrsAPEAPTPNdPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTS-VASTVMEc 242
Cdd:pfam00069 165 ------------------APEVLRGN-PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSpRPSSISE- 224
                         250       260
                  ....*....|....*....|
gi 32476378   243 pvWMDRLVMQLLNKDPGQRP 262
Cdd:pfam00069 225 --EAKDLLKKLLKKDPSKRL 242
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
64-214 1.64e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061  Cd Length: 968  Bit Score: 70.26  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   64 LKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQrrgRLPWESVLELAEPLIDALMYLHDR---DIVHGRITPDK 140
Cdd:PLN00113 737 MGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVLR---NLSWERRRKIAIGIAKALRFLHCRcspAVVVGNLSPEK 813
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  141 VIiaglspvlIDVRDVdgtppfrsgPYHVSRPPSI-----GQMMRSAPEAPTPNDP--VTARTDLYLFGALLYEALTGAP 213
Cdd:PLN00113 814 II--------IDGKDE---------PHLRLSLPGLlctdtKCFISSAYVAPETRETkdITEKSDIYGFGLILIELLTGKS 876

                 .
gi 32476378  214 P 214
Cdd:PLN00113 877 P 877
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
24-274 3.16e-49

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: 173.16  E-value: 3.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQR 103
Cdd:cd14014  14 GEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 104 RGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLS-PVLID---VRDVDGTPPFRSGPYhvsrppsIGQMM 179
Cdd:cd14014  94 RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDfgiARALGDSGLTQTGSV-------LGTPA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 180 RSAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDRLVMQLLNKDPG 259
Cdd:cd14014 167 YMAPEQAR-GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPE 245
                       250
                ....*....|....*
gi 32476378 260 QRPVSAAAVKLQLAE 274
Cdd:cd14014 246 ERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
24-262 1.82e-22

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 97.60  E-value: 1.82e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378     24 ARVWRAVHIKMRKAVAVRVfqMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQR 103
Cdd:smart00220  13 GKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    104 RGRLPWESVLELAEPLIDALMYLHDRDIVHgR--------ITPDKVI-IA--GLSPVLID---VRDVDGTPPFRsgpyhv 169
Cdd:smart00220  91 RGRLSEDEARFYLRQILSALEYLHSKGIVH-RdlkpenilLDEDGHVkLAdfGLARQLDPgekLTTFVGTPEYM------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    170 srppsigqmmrsAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDRL 249
Cdd:smart00220 164 ------------APEVLL-GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|...
gi 32476378    250 VMQLLNKDPGQRP 262
Cdd:smart00220 231 IRKLLVKDPEKRL 243
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
24-272 4.89e-21

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: 92.72  E-value: 4.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVfqMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEI-Q 102
Cdd:cd00180   7 GKVYKARDKETGKKVAVKV--IPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLkE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVII-AGLSPVLID---VRDVDgtppfrSGPYHVSRPPSIGQM 178
Cdd:cd00180  85 NKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLdSDGTVKLADfglAKDLD------SDDSLLKTTGGTTPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 179 MRSAPEAPTpNDPVTARTDLYLFGALLYEaltgappitgstvqevtsnlkyqsptsvastvMECpvwMDRLVMQLLNKDP 258
Cdd:cd00180 159 YYAPPELLG-GRYYGPKVDIWSLGVILYE--------------------------------LEE---LKDLIRRMLQYDP 202
                       250
                ....*....|....
gi 32476378 259 GQRPvSAAAVKLQL 272
Cdd:cd00180 203 KKRP-SAKELLEHL 215
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-283 7.28e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 94.42  E-value: 7.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMrkaVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHP-AIVKCYGGGFEESEAYLAHELVEGSTLAEEIQ 102
Cdd:COG0515  14 GEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGR---LPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIA--GLSPVLID---VRDVDGTPPFRSGPYHVSrpPS 174
Cdd:COG0515  91 KIGRkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrdGRVVKLIDfglAKLLPDPGSTSSIPALPS--TS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 175 IGQMMRSAPE--APTPNDPVTARTDLYLFGALLYEALTGAPPITG----STVQEVTSNLKYQSPTSVASTV-----MECP 243
Cdd:COG0515 169 VGTPGYMAPEvlLGLSLAYASSSSDIWSLGITLYELLTGLPPFEGeknsSATSQTLKIILELPTPSLASPLspsnpELIS 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32476378 244 VWMDRLVMQLLNKDPGQRPVSAAAVKLQLAEVRKRSMSRS 283
Cdd:COG0515 249 KAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDL 288
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-276 1.88e-18

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 89.52  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378     37 AVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLA-HELVEGSTLAEEIQRRGRLPWESVLEL 115
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAvFEYVPGRTLREVLAADGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    116 AEPLIDALMYLHDRDIVHGRITPDKVIIA-------------GLSPVLIDVRDVDGTPPFRSGPYhvsrppsIGQMMRSA 182
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSqtgvrphakvldfGIGTLLPGVRDADVATLTRTTEV-------LGTPTYCA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    183 PEApTPNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTsnLKYQSPTSVAstvmeCPVWMD-----RLVMQLLNKD 257
Cdd:TIGR03903  158 PEQ-LRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIL--YQQLSPVDVS-----LPPWIAghplgQVLRKALNKD 229
                          250
                   ....*....|....*....
gi 32476378    258 PGQRPVSAAAVKLQLAEVR 276
Cdd:TIGR03903  230 PRQRAASAPALAERFRALE 248
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
21-269 2.04e-18

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  Cd Length: 265  Bit Score: 85.60  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  21 ARDARVWRAVHIKMRKAVAvrvfqmpfgGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEE 100
Cdd:cd14098  21 EVETGKMRAIKQIVKRKVA---------GNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDF 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPVLIDVRDVDGTPPFRSGPYHVSrppSIGQMMR 180
Cdd:cd14098  92 IMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIHTGTFLVT---FCGTMAY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 181 SAPE---APTPNDP--VTARTDLYLFGALLYEALTGAPPITGST---VQEVTSNLKYQSPTSVASTVMEcpvwMDR-LVM 251
Cdd:cd14098 169 LAPEilmSKEQNLQggYSNLVDMWSVGCLVYVMLTGALPFDGSSqlpVEKRIRKGRYTQPPLVDFNISE----EAIdFIL 244
                       250
                ....*....|....*...
gi 32476378 252 QLLNKDPGQRPVSAAAVK 269
Cdd:cd14098 245 RLLDVDPEKRMTAAQALD 262
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
64-268 2.03e-17

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  Cd Length: 273  Bit Score: 82.73  E-value: 2.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  64 LKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWES---VLELAEPLIDALMYLHDRDIVHGRITPDK 140
Cdd:cd13996  58 LAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTLRDWIDRRNSSSKNDrklALELFKQILKGVSYIHSKGIVHRDLKPSN 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 141 VIIA-----------GLSPVLIDVRDVDGTPPFRSGPYHVSRPPSIGQMMRSAPEApTPNDPVTARTDLYLFGALLYEAL 209
Cdd:cd13996 138 IFLDnddlqvkigdfGLATSIGNQKRELNNLNNNNNGNTSNNSVGIGTPLYASPEQ-LDGENYNEKADIYSLGIILFEML 216
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 210 tgAPPITGSTVQEVTSNL-KYQSPTSVAStvmECPVWMDrLVMQLLNKDPGQRPvSAAAV 268
Cdd:cd13996 217 --HPFKTAMERSTILTDLrNGILPESFKA---KHPKEAD-LIQSLLSKNPEERP-SAEQL 269
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
24-266 6.67e-17

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: 80.98  E-value: 6.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMpFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGgFEESEA-YLAHELVEGSTLAEEIQ 102
Cdd:cd05117  14 GVVRLAVHKKTGEEYAVKIIDK-KKLKSEDEEMLRREIEILKRLDHPNIVKLYEV-FEDDKNlYLVMELCTGGELFDRIV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITP-----------DKVIIA--GLSPVL---IDVRDVDGTppfrsgP 166
Cdd:cd05117  92 KKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPenillaskdpdSPIKIIdfGLAKIFeegEKLKTVCGT------P 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 167 YHVsrppsigqmmrsAPEaptpndpVTART------DLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTsvastvM 240
Cdd:cd05117 166 YYV------------APE-------VLKGKgygkkcDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYS------F 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 32476378 241 ECPVWMDR------LVMQLLNKDPGQRPvSAA 266
Cdd:cd05117 221 DSPEWKNVseeakdLIKRLLVVDPKKRL-TAA 251
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
24-261 4.32e-16

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  Cd Length: 251  Bit Score: 78.42  E-value: 4.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPfGGTQESRQAFAEEWDRLKRLDHPAIVKCYGggFEESEA--YLAHELVEGSTLAEEI 101
Cdd:cd14009   7 ATVWKGRHKQTGEVVAIKEISRK-KLNKKLQENLESEIAILKSIKHPNIVRLYD--VQKTEDfiYLVLEYCAGGDLSQYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 102 QRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLS--PVL----------IDVRDVDGTppFRSGPYHV 169
Cdd:cd14009  84 RKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddPVLkiadfgfarsLQPASMAET--LCGSPLYM 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 170 SrpPSIGQMMRsapeaptpndpVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKyqSPTSVASTVMECPVWMD-- 247
Cdd:cd14009 162 A--PEILQFQK-----------YDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIE--RSDAVIPFPIAAQLSPDck 226
                       250
                ....*....|....
gi 32476378 248 RLVMQLLNKDPGQR 261
Cdd:cd14009 227 DLLRRLLRRDPAER 240
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
60-262 7.19e-16

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  Cd Length: 254  Bit Score: 77.79  E-value: 7.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  60 EWDRLKRLDHPAIVKCYGGGFEESEA------YLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVH 133
Cdd:cd14012  48 ELESLKKLRHPNLVSYLAFSIERRGRsdgwkvYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 134 GRITPDKviiaglspVLIDVRDVDGTPpfRSGPYHVSRPPSIGQMMRS----------APEAPTPNDPVTARTDLYLFGA 203
Cdd:cd14012 128 KSLHAGN--------VLLDRDAGTGIV--KLTDYSLGKTLLDMCSRGSldefkqtywlPPELAQGSKSPTRKTDVWDLGL 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32476378 204 LLYEALTGAPpitgsTVQevtsnlKYQSPTSVaSTVMECPVWMDRLVMQLLNKDPGQRP 262
Cdd:cd14012 198 LFLQMLFGLD-----VLE------KYTSPNPV-LVSLDLSASLQDFLSKCLSLDPKKRP 244
Pkinase pfam00069
Protein kinase domain;
24-262 1.54e-15

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 76.48  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    24 ARVWRAVHIKMRKAVAVRVFqmpfggtqESRQAFAEEWDR-------LKRLDHPAIVKCYGGGFEESEAYLAHELVEGST 96
Cdd:pfam00069  13 GTVYKAKHRDTGKIVAIKKI--------KKEKIKKKKDKNilreikiLKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    97 LAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIA----------GLSPVLI---DVRDVDGTPPFR 163
Cdd:pfam00069  85 LFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDedgnlkitdfGLARQLNsgsSLTSFVGTPWYM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   164 sgpyhvsrppsigqmmrsAPEAPTPNdPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTS-VASTVMEc 242
Cdd:pfam00069 165 ------------------APEVLRGN-PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSpRPSSISE- 224
                         250       260
                  ....*....|....*....|
gi 32476378   243 pvWMDRLVMQLLNKDPGQRP 262
Cdd:pfam00069 225 --EAKDLLKKLLKKDPSKRL 242
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
38-214 3.56e-15

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: 75.63  E-value: 3.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  38 VAVRvfQMPFGG-TQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPwESVLEL- 115
Cdd:cd06606  28 MAVK--EVELSGdSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLASLLKKFGKLP-EPVVRKy 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 116 AEPLIDALMYLHDRDIVHGRITPDKVIIA----------GLSPVLIDVRDVDGTPPFRSGPYhvsrppsigqMMrsAPEA 185
Cdd:cd06606 105 TRQILEGLEYLHSNGIVHRDIKGANILVDsdgvvkladfGCAKRLAEIATGEGTKSLRGTPY----------WM--APEV 172
                       170       180
                ....*....|....*....|....*....
gi 32476378 186 PTpNDPVTARTDLYLFGALLYEALTGAPP 214
Cdd:cd06606 173 IR-GEGYGRAADIWSLGCTVIEMATGKPP 200
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
67-261 4.15e-15

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  Cd Length: 269  Bit Score: 75.41  E-value: 4.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  67 LDHPAIVKCYgggfeesEAY-------LAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPD 139
Cdd:cd14010  51 LKHPNVLKFY-------EWYetsnhlwLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPS 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 140 KVIIA----------GLSPVLIdvrDVDGTPPFRSGPYHVSRPPSIGQMMRSAPEAPTP----NDPVTARTDLYLFGALL 205
Cdd:cd14010 124 NILLDgngtlklsdfGLARREG---EILKELFGQFSDEGNVNKVSKKQAKRGTPYYMAPelfqGGVHSFASDLWALGCVL 200
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32476378 206 YEALTGAPPITGSTVQEVTSNL---KYQSPTSVASTVMECPVWmdRLVMQLLNKDPGQR 261
Cdd:cd14010 201 YEMFTGKPPFVAESFTELVEKIlneDPPPPPPKVSSKPSPDFK--SLLKGLLEKDPAKR 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
24-262 4.78e-15

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  Cd Length: 245  Bit Score: 74.88  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIkmRKAVAVRVFQmPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQ- 102
Cdd:cd13999   7 GEVYKGKWR--GTDVAIKKLK-VEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHk 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGRLPWESVLELAeplID---ALMYLHDRDIVHGRITPD----------KVIIAGLSpvlidvRDVDGTPPFRSGPyhv 169
Cdd:cd13999  84 KKIPLSWSLRLKIA---LDiarGMNYLHSPPIIHRDLKSLnilldenftvKIADFGLS------RIKNSTTEKMTGV--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 170 srppsIG--QMMrsAPEAPTpNDPVTARTDLYLFGALLYEALTGAPP---ITGSTV--QEVTSNLKYQSPTSvastvmeC 242
Cdd:cd13999 152 -----VGtpRWM--APEVLR-GEPYTEKADVYSFGIVLWELLTGEVPfkeLSPIQIaaAVVQKGLRPPIPPD-------C 216
                       250       260
                ....*....|....*....|
gi 32476378 243 PVWMDRLVMQLLNKDPGQRP 262
Cdd:cd13999 217 PPELSKLIKRCWNEDPEKRP 236
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
26-262 7.71e-15

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: 74.94  E-value: 7.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVFQMPFGgTQESRQAFAE-EWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRR 104
Cdd:cd05581  17 VVLAKEKETGKEYAIKVLDKRHI-IKEKKVKYVTiEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNGDLLEYIRKY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 105 GRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAG-LSPVLID---VRDVDGTPPFRSGPYHVSRPPSIGQMMR 180
Cdd:cd05581  96 GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEdMHIKITDfgtAKVLGPDSSPESTKGDADSQIAYNQARA 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 181 S---------APEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGS----TVQEVTsNLKYQSPTSVASTVMEcpvwmd 247
Cdd:cd05581 176 AsfvgtaeyvSPELLN-EKPAGKSSDLWALGCIIYQMLTGKPPFRGSneylTFQKIV-KLEYEFPENFPPDAKD------ 247
                       250
                ....*....|....*
gi 32476378 248 rLVMQLLNKDPGQRP 262
Cdd:cd05581 248 -LIQKLLVLDPSKRL 261
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
24-261 8.43e-15

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  Cd Length: 252  Bit Score: 74.25  E-value: 8.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKM-RKAVAVRVFQMPfGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQ 102
Cdd:cd14121   9 ATVYKAYRKSGaREVVAVKCVSKS-SLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDLSRFIR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPVLIDVRDVdgtppfrsGPYHVSRPPSIGQMMRSA 182
Cdd:cd14121  88 SRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADF--------GFAQHLKPNDEAHSLRGS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 183 PEAPTP----NDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMECPVWMDrLVMQLLNKDP 258
Cdd:cd14121 160 PLYMAPemilKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKPIEIPTRPELSADCRD-LLLRLLQRDP 238

                ...
gi 32476378 259 GQR 261
Cdd:cd14121 239 DRR 241
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
68-214 1.06e-14

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  Cd Length: 259  Bit Score: 74.28  E-value: 1.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  68 DHPAIVKCYGGGFEESEAYL-AHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVII--A 144
Cdd:cd13987  48 VHPHIIKTYDVAFETEDYYVfAQEYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdK 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32476378 145 GLSPV-LID---VRDVDGTPPFRSG--PYHvsrPPSIGQMMrsapeaptPNDPVTAR--TDLYLFGALLYEALTGAPP 214
Cdd:cd13987 128 DCRRVkLCDfglTRRVGSTVKRVSGtiPYT---APEVCEAK--------KNEGFVVDpsIDVWAFGVLLFCCLTGNFP 194
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
25-262 1.43e-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  Cd Length: 253  Bit Score: 73.66  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  25 RVWRAVHIKMRKAVAVRV-FQMPFGGTQESRQafaeewdrLKR-------LDHPAIVKCYGGGFEESEAYLAHELVEGST 96
Cdd:cd14007  15 NVYLAREKKSGFIVALKViSKSQLQKSGLEHQ--------LRReieiqshLRHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  97 LAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKviiaglspVLIDVRDV----DgtppFrsGpYHVSRP 172
Cdd:cd14007  87 LYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPEN--------ILLGSNGElklaD----F--G-WSVHAP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 173 PSigqmMRS---------APEApTPNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEV---TSNLKYQSPTSVASTVM 240
Cdd:cd14007 152 SN----RRKtfcgtldylPPEM-VEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETykrIQNVDIKFPSSVSPEAK 226
                       250       260
                ....*....|....*....|..
gi 32476378 241 EcpvwmdrLVMQLLNKDPGQRP 262
Cdd:cd14007 227 D-------LISKLLQKDPSKRL 241
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
26-262 1.77e-14

Protein tyrosine kinase;


Pssm-ID: 311583  Cd Length: 258  Bit Score: 73.30  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378    26 VWRAVHIKMRKAVAVRVfqMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRG 105
Cdd:pfam07714  19 TLKGDGEGTKIKVAVKT--LKEGADEEEREDFLEEASIMKKLSHPNIVRLLGVCTQGEPLYIVTEYMPGGDLLDFLRKHK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   106 R-LPWESVLELAEPLIDALMYLHDRDIVHGRI--------TPDKVIIA--GLSpvlidvRDVDgtppfrSGPYHVSRPPS 174
Cdd:pfam07714  97 GkLTLPDLLQMALQIAKGMEYLESKNFVHRDLaarnclvtENLVVKISdfGLS------RDIY------DDDYYRKRGGG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   175 IGQ---MmrsAPEAptPNDPV-TARTDLYLFGALLYEALT-GAPPITGSTVQEVTSNLK--YQSPTSvastvMECPVWMD 247
Cdd:pfam07714 165 KLPikwM---APES--LKDGKfTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEdgYRLPQP-----ENCPDELY 234
                         250
                  ....*....|....*
gi 32476378   248 RLVMQLLNKDPGQRP 262
Cdd:pfam07714 235 DLMTQCWAYDPEDRP 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
26-143 4.21e-14

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  Cd Length: 264  Bit Score: 72.24  E-value: 4.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVFQMPfgGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRG 105
Cdd:cd06623  17 VYKVRHKPTGKIYALKKIHVD--GDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLADLLKKVG 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32476378 106 RLPwESVL-ELAEPLIDALMYLH-DRDIVHGRITPDKVII 143
Cdd:cd06623  95 KIP-EPVLaYIARQILKGLDYLHtKRHIIHRDIKPSNLLI 133
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
54-271 1.21e-13

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015  Cd Length: 263  Bit Score: 71.16  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  54 RQAFAEEWDRLKRLDHPAIVKCYGGgFEESEAY-LAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIV 132
Cdd:cd14113  47 RDQVTHELGVLQSLQHPQLVGLLDT-FETPTSYiLVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 133 HGRITPDKVII-AGLSPVLIDVRDVDGTPPFRSGPYhvsrppsIGQMMRSaPEAPTPN----DPVTARTDLYLFGALLYE 207
Cdd:cd14113 126 HLDLKPENILVdQSLSKPTIKLADFGDAVQLNTTYY-------IHQLLGS-PEFAAPEiilgNPVSLTSDLWSIGVLTYV 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32476378 208 ALTGAPPITGSTVQEVTSN---LKYQSPTSVASTVMECPvwmDRLVMQLLNKDPGQRPVSAAAVKLQ 271
Cdd:cd14113 198 LLSGVSPFLDESVEETCLNicrLDFSFPDDYFKGVSQKA---KDFVCFLLQMDPAKRPSAALCLQEQ 261
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
33-261 5.19e-13

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


Pssm-ID: 270693  Cd Length: 250  Bit Score: 68.70  E-value: 5.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  33 KMRKAVAVRvfqmpfggTQESRQAFAEEwDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLP-WES 111
Cdd:cd05123  25 VLRKKEIIK--------RKEVEHTLNER-NILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGELFSHLSKEGRFPeERA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 112 VLELAEpLIDALMYLHDRDIVHGRITPDKVIIA----------GLSPVLIDVRDVD----GTPPFRSgpyhvsrpPSIGQ 177
Cdd:cd05123  96 RFYAAE-IVLALEYLHSLGIIYRDLKPENILLDsdghikltdfGLAKELSSDGDRTytfcGTPEYLA--------PEVLL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 178 mmrsapeaptpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTsvastvmeCPVWMDR----LVMQL 253
Cdd:cd05123 167 -----------GKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLK--------FPEYVSPeaksLISGL 227

                ....*...
gi 32476378 254 LNKDPGQR 261
Cdd:cd05123 228 LQKDPTKR 235
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
26-262 6.07e-13

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  Cd Length: 251  Bit Score: 68.62  E-value: 6.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVFQMPFggTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRG 105
Cdd:cd05041  11 VYRGVLKPDNTEVAVKTCRETL--PPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLTFLRKKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 106 -RLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPVLID----VRDVDGtppfrsGPYHVSrpPSIGQM-- 178
Cdd:cd05041  89 aRLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISdfgmSREEED------GEYTVS--DGLKQIpi 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 179 MRSAPEAPTPNDpVTARTDLYLFGALLYEALT-GAPPITGSTVQE----VTSNLKYQSPTSvastvmeCPVWMDRLVMQL 253
Cdd:cd05041 161 KWTAPEALNYGR-YTSESDVWSFGILLWEIFSlGATPYPGMSNQQtreqIESGYRMPAPEL-------CPEAVYRLMLQC 232

                ....*....
gi 32476378 254 LNKDPGQRP 262
Cdd:cd05041 233 WAYDPENRP 241
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
25-268 8.70e-13

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  Cd Length: 258  Bit Score: 68.26  E-value: 8.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  25 RVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEwDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRR 104
Cdd:cd08215  15 SAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEV-KLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDLAQKIKKQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 105 GR----LPWESVLELAEPLIDALMYLHDRDIVHgR--------ITPDKVI-IA--GLSPVLIDVRD----VDGTppfrsg 165
Cdd:cd08215  94 KKkgqpFPEEQILDWFVQICLALKYLHSRKILH-RdlktqnifLTKDGVVkLGdfGISKVLESTTDlaktVVGT------ 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 166 PYHVSrpPSIGQmmrsapeaptpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTS---NLKYQSPTSVASTVMEc 242
Cdd:cd08215 167 PYYLS--PELCE-----------NKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYkivKGQYPPIPSQYSSELR- 232
                       250       260
                ....*....|....*....|....*.
gi 32476378 243 pvwmdRLVMQLLNKDPGQRPvSAAAV 268
Cdd:cd08215 233 -----DLVNSMLQKDPEKRP-SANEI 252
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
25-261 1.26e-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  Cd Length: 253  Bit Score: 67.66  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  25 RVWRAVHIKMRKAVAVRvFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGgFE-ESEAYLAHELVEGStLAEEIQR 103
Cdd:cd14002  16 KVYKGRRKYTGQVVALK-FIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDS-FEtKKEFVVVTEYAQGE-LFQILED 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 104 RGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPV-LID-------------VRDVDGTPPFrsgpyhv 169
Cdd:cd14002  93 DGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVkLCDfgfaramscntlvLTSIKGTPLY------- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 170 srppsigqMmrsAPEApTPNDPVTARTDLYLFGALLYEALTGAPPI-TGSTVQEVT----SNLKYQSPTSvastvmecPV 244
Cdd:cd14002 166 --------M---APEL-VQEQPYDHTADLWSLGCILYELFVGQPPFyTNSIYQLVQmivkDPVKWPSNMS--------PE 225
                       250
                ....*....|....*..
gi 32476378 245 WMDrLVMQLLNKDPGQR 261
Cdd:cd14002 226 FKS-FLQGLLNKDPSKR 241
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
64-214 1.64e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061  Cd Length: 968  Bit Score: 70.26  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   64 LKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQrrgRLPWESVLELAEPLIDALMYLHDR---DIVHGRITPDK 140
Cdd:PLN00113 737 MGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEVLR---NLSWERRRKIAIGIAKALRFLHCRcspAVVVGNLSPEK 813
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  141 VIiaglspvlIDVRDVdgtppfrsgPYHVSRPPSI-----GQMMRSAPEAPTPNDP--VTARTDLYLFGALLYEALTGAP 213
Cdd:PLN00113 814 II--------IDGKDE---------PHLRLSLPGLlctdtKCFISSAYVAPETRETkdITEKSDIYGFGLILIELLTGKS 876

                 .
gi 32476378  214 P 214
Cdd:PLN00113 877 P 877
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
24-262 2.28e-12

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: 66.77  E-value: 2.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFqmpfggtqESRQAFAEEWDRLKR-------LDHPAIVKCYGGGFEESEAYLAHELVEGST 96
Cdd:cd14003  14 GKVKLARHKLTGEKVAIKII--------DKSKLKEEIEEKIKReieimklLNHPNIIKLYEVIETENKIYLVMEYASGGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  97 LAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPD----------KVIIAGLSpvlIDVRDVD------GTP 160
Cdd:cd14003  86 LFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLEnilldkngnlKIIDFGLS---NEFRGGSllktfcGTP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 161 PFrsgpyhvsrppsigqmmrSAPE--APTPNDpvTARTDLYLFGALLYEALTGAPPITGSTVqevtSNLKYQsptsVAST 238
Cdd:cd14003 163 AY------------------AAPEvlLGRKYD--GPKADVWSLGVILYAMLTGYLPFDDDND----SKLFRK----ILKG 214
                       250       260
                ....*....|....*....|....*...
gi 32476378 239 VMECPVWMD----RLVMQLLNKDPGQRP 262
Cdd:cd14003 215 KYPIPSHLSpdarDLIRRMLVVDPSKRI 242
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-262 3.15e-12

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  Cd Length: 270  Bit Score: 66.76  E-value: 3.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  40 VRVFQMPFGGT-QESRQAFAEEWDRLK----RLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEI----QRRGRLPWE 110
Cdd:cd08528  34 INMTNPAFGRTeQERDKSVGDIISEVNiikeQLRHPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFsslkEKNEHFTED 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 111 SVLELAEPLIDALMYLH-DRDIVHGRITPDKVIIAGLSPVLIdvrdVDGTPPFRSGPYHVSRPPSIGQMMRSAPEApTPN 189
Cdd:cd08528 114 RIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTI----TDFGLAKQKGPESSKMTSVVGTILYSCPEI-VQN 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32476378 190 DPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTS---NLKYQSPTSVASTVMecpvwMDRLVMQLLNKDPGQRP 262
Cdd:cd08528 189 EPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATkivEAEYEPLPEGMYSDD-----ITFVIRSCLTPDPEARP 259
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
26-264 7.18e-12

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


Pssm-ID: 270968  Cd Length: 272  Bit Score: 65.76  E-value: 7.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVhIKMRKAVAVRVFQMpfGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRG 105
Cdd:cd14066   9 VYKGV-LENGTVVAVKRLNE--MNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHCHK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 106 R---LPWESVLELAEPLIDALMYLH---DRDIVHGRITPDKVIIA----------GLSPVLIDVRDVDGTPPFRSgpyhv 169
Cdd:cd14066  86 GsppLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDedfepkltdfGLARLIPPSESVSKTSAVKG----- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 170 srppSIGQMmrsAPEAPTPNDpVTARTDLYLFGALLYEALTGAPPI--------TGSTVQEVTSNLKYQ----------S 231
Cdd:cd14066 161 ----TIGYL---APEYIRTGR-VSTKSDVYSFGVVLLELLTGKPAVdenrenasRKDLVEWVESKGKEEledildkrlvD 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 32476378 232 PTSVASTVMECpvwMDRLVMQLLNKDPGQRPVS 264
Cdd:cd14066 233 DDGVEEEEVEA---LLRLALLCTRSDPSLRPSM 262
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
26-287 7.74e-12

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  Cd Length: 300  Bit Score: 66.03  E-value: 7.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVF------QMPFGGTQEsrqaFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAE 99
Cdd:cd14094  19 VRRCIHRETGQQFAVKIVdvakftSSPGLSTED----LKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 100 EIQRR---GRLPWESVL-ELAEPLIDALMYLHDRDIVHGRITPDKVIIAglspvlidvrDVDGTPPFRSGPYHVSRPPSI 175
Cdd:cd14094  95 EIVKRadaGFVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLA----------SKENSAPVKLGGFGVAIQLGE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 176 GQMMRS---------APEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPtsvastvMECPVWM 246
Cdd:cd14094 165 SGLVAGgrvgtphfmAPEVVK-REPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYK-------MNPRQWS 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32476378 247 D------RLVMQLLNKDPGQRPVSAAAVKLQLAEVRKRSMSRSGVAE 287
Cdd:cd14094 237 HisesakDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPE 283
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
24-262 1.49e-11

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  Cd Length: 258  Bit Score: 64.50  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGgFEESE-AYLAHELVEGSTLAEEIQ 102
Cdd:cd14099  15 AKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDC-FEDEEnVYILLELCSNGSLMELLK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 103 RRGRLPWESVLELAEPLIDALMYLHDRDIVH-----GRITPDK---VIIA--GLSPVLIDV----RDVDGTPPFrsgpyh 168
Cdd:cd14099  94 RRKALTEPEVRYFMRQILSGVKYLHSNRIIHrdlklGNLFLDEnmnVKIGdfGLAARLEYDgerkKTLCGTPNY------ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 169 vsrppsIgqmmrsAPEaptpndpVTART-------DLYLFGALLYEALTGAPPITGSTVQEVTSNLK---YQSPTSVA-S 237
Cdd:cd14099 168 ------I------APE-------VLEKKkghsfevDIWSLGVILYTLLVGKPPFETSDVKETYKRIKkneYSFPSHLSiS 228
                       250       260
                ....*....|....*....|....*
gi 32476378 238 TVMECpvwmdrLVMQLLNKDPGQRP 262
Cdd:cd14099 229 DEAKD------LIRSMLQPDPTKRP 247
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
24-214 2.49e-11

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


Pssm-ID: 270797  Cd Length: 254  Bit Score: 63.78  E-value: 2.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRvfQMPFGG-TQESRQAFAEEWDRLKRLDHPAIVKCYggGFEESEAYL--AHELVEGSTLAEE 100
Cdd:cd06627  14 GSVYKGLNLNTGEFVAIK--QISLEKiPKSDLKSVMGEIDLLKKLNHPNIVKYI--GSVKTKDSLyiILEYVENGSLASI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPwesvlelaEPLI--------DALMYLHDRDIVHGRI-------TPDKVI-IA--GLSPVLIDVR----DVDG 158
Cdd:cd06627  90 IKKFGKFP--------ESLVavyiyqvlEGLAYLHEQGVIHRDIkganiltTKDGLVkLAdfGVATKLNEVEkdenSVVG 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32476378 159 TppfrsgPYhvsrppsigqMMrsAPEApTPNDPVTARTDLYLFGALLYEALTGAPP 214
Cdd:cd06627 162 T------PY----------WM--APEV-IEMSGVTTASDIWSVGCTVIELLTGNPP 198
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
22-269 2.79e-11

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017  Cd Length: 248  Bit Score: 63.83  E-value: 2.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  22 RDARVWRAVHIKMRKAVAVRVFQMPFggtQESRQAfAEEWDRLKRLDHPAIVKCYGGgFEESEAY-LAHELVEGSTLAEE 100
Cdd:cd14115   5 RFSIVKKCLHKATRKDVAVKFVSKKM---KKKEQA-AHEAALLQHLQHPQYITLHDT-YESPTSYiLVLELMDDGRLLDY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPV----LIDVRDVDGTppfrSGPYHVSRppSIG 176
Cdd:cd14115  80 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprvkLIDLEDAVQI----SGHRHVHH--LLG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 177 QMMRSAPEApTPNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSN---LKYQSPTSVASTVMECPvwmDRLVMQL 253
Cdd:cd14115 154 NPEFAAPEV-IQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINvcrVDFSFPDEYFGDVSQAA---RDFINVI 229
                       250
                ....*....|....*.
gi 32476378 254 LNKDPGQRPVSAAAVK 269
Cdd:cd14115 230 LQEDPRRRPTAATCLQ 245
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
10-143 3.83e-11

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  Cd Length: 262  Bit Score: 63.44  E-value: 3.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  10 AIESPLGpdpSARDARVWRAVHIKMRKAVA---VRVFQMpfgGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAY 86
Cdd:cd08224   3 EIEKKIG---KGQFSVVYRARCLLDGRLVAlkkVQIFEM---MDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELN 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32476378  87 LAHELVEGSTLAEEI---QRRGRL-PWESVLELAEPLIDALMYLHDRDIVHGRITPDKVII 143
Cdd:cd08224  77 IVLELADAGDLSRLIkhfKKQKRLiPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFI 137
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
67-262 4.06e-11

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  Cd Length: 258  Bit Score: 63.44  E-value: 4.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  67 LDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGL 146
Cdd:cd14116  62 LRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSA 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 147 SPVLI-DVRDVDGTPPFRsgpyhvsRPPSIGQMMRSAPEAptpndpVTART-----DLYLFGALLYEALTGAPPITGSTV 220
Cdd:cd14116 142 GELKIaDFGWSVHAPSSR-------RTTLCGTLDYLPPEM------IEGRMhdekvDLWSLGVLCYEFLVGKPPFEANTY 208
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32476378 221 QEV---TSNLKYQSPTSVASTVMEcpvwmdrLVMQLLNKDPGQRP 262
Cdd:cd14116 209 QETykrISRVEFTFPDFVTEGARD-------LISRLLKHNPSQRP 246
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
51-266 6.96e-11

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  Cd Length: 259  Bit Score: 62.81  E-value: 6.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  51 QESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRD 130
Cdd:cd06632  43 RESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRN 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 131 IVH-----GRITPDK---VIIA--GLSPVlidVRDVDGTPPFRSGPYHVsrppsigqmmrsAPEAPTP-NDPVTARTDLY 199
Cdd:cd06632 123 TVHrdikgANILVDTngvVKLAdfGMAKH---VEAFSFAKSFKGSPYWM------------APEVIMQkNSGYGLAVDIW 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32476378 200 LFGALLYEALTGAPPItgSTVQEVTSNLKYQSPTsvastvmECPVWMDRL-------VMQLLNKDPGQRPVSAA 266
Cdd:cd06632 188 SLGCTVLEMATGKPPW--SQYEGVAAIFKIGNSG-------ELPPIPDHLspdakdfIRLCLQRDPEDRPTASQ 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
64-261 9.93e-11

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  Cd Length: 267  Bit Score: 62.19  E-value: 9.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  64 LKRLDHPAIVKCYgggfE------ESEAYLAHELVEGSTLAE--EIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGR 135
Cdd:cd14008  58 MKKLDHPNIVRLY----EviddpeSDKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRD 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 136 ITPDKVIIA----------GLSPVLID----VRDVDGTPPFrsgpyhvsrppsigqmmrSAPEAPTPNDPvTAR---TDL 198
Cdd:cd14008 134 IKPENLLLTadgtvkisdfGVSEMFEDgndtLQKTAGTPAF------------------LAPELCDGDSK-TYSgkaADI 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32476378 199 YLFGALLYEALTGAPPITGSTVQEVTSNLKYQSPTSVASTVMEcPVWMDrLVMQLLNKDPGQR 261
Cdd:cd14008 195 WALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPELS-PELKD-LLRRMLEKDPEKR 255
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
24-269 1.28e-10

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  Cd Length: 256  Bit Score: 61.65  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMpfggTQESRQAFAEEWDR----LKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAE 99
Cdd:cd14663  14 AKVKFARNTKTGESVAIKIIDK----EQVAREGMVEQIKReiaiMKLLRHPNIVELHEVMATKTKIFFVMELVTGGELFS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 100 EIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPD----------KVIIAGLSpVLIDVRDVDGTPPFRSG-PYH 168
Cdd:cd14663  90 KIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPEnllldedgnlKISDFGLS-ALSEQFRQDGLLHTTCGtPNY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 169 VsrppsigqmmrsAPEAPTPNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVtsnlkYQsptSVASTVMECPVWMD- 247
Cdd:cd14663 169 V------------APEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMAL-----YR---KIMKGEFEYPRWFSp 228
                       250       260
                ....*....|....*....|....*
gi 32476378 248 ---RLVMQLLNKDPGQRpVSAAAVK 269
Cdd:cd14663 229 gakSLIKRILDPNPSTR-ITVEQIM 252
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
14-269 3.29e-10

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  Cd Length: 256  Bit Score: 60.79  E-value: 3.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  14 PLGPD--PSARDARVWRAVHIKMRKAVAVRVFQMP-FGGTQESRQAfaeewdrlkRLDHPAIVKCYGGGFEESEAYLAHE 90
Cdd:cd13995   6 NIGSDfiPRGAFGKVYLAQDTKTKKRMACKLIPVEqFKPSDVEIQA---------CFRHENIAELYGALLWEETVHLFME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  91 LVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPVLIDV-------------RDVD 157
Cdd:cd13995  77 AGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLVDFglsvqmtedvyvpKDLR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 158 GTPPFRSGPYHVSRppsiGQmmrsapeaptpndpvTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKY----QSPt 233
Cdd:cd13995 157 GTEIYMSPEVILCR----GH---------------NTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYiihkQAP- 216
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32476378 234 SVASTVMECPVWMDRLVMQLLNKDPGQRPVSAAAVK 269
Cdd:cd13995 217 PLEDIAQDCSPAMRELLEAALERNPNHRSSAAELLK 252
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
53-261 3.81e-10

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  Cd Length: 269  Bit Score: 60.80  E-value: 3.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  53 SRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIV 132
Cdd:cd14194  51 SREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 133 HGRITPD--------------KVIIAGLSPVLI---DVRDVDGTPPFrsgpyhvsrppsigqmmrSAPEApTPNDPVTAR 195
Cdd:cd14194 131 HFDLKPEnimlldrnvpkpriKIIDFGLAHKIDfgnEFKNIFGTPEF------------------VAPEI-VNYEPLGLE 191
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32476378 196 TDLYLFGALLYEALTGAPPITGSTVQEVTSNL---------KYQSPTSVASTvmecpvwmdRLVMQLLNKDPGQR 261
Cdd:cd14194 192 ADMWSIGVITYILLSGASPFLGDTKQETLANVsavnyefedEYFSNTSALAK---------DFIRRLLVKDPKKR 257
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
106-266 3.86e-10

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  Cd Length: 270  Bit Score: 60.71  E-value: 3.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 106 RLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPvLIDVRDVDgtppfrsgpYHVSRPPSIGQMMRS---A 182
Cdd:cd14198 106 MVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYP-LGDIKIVD---------FGMSRKIGHACELREimgT 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 183 PEAPTPN----DPVTARTDLYLFGALLYEALTGAPPITGSTVQEV-----TSNLKYQSPTsvASTVMECPVwmdRLVMQL 253
Cdd:cd14198 176 PEYLAPEilnyDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETflnisQVNVDYSEET--FSSVSQLAT---DFIQKL 250
                       170
                ....*....|...
gi 32476378 254 LNKDPGQRPVSAA 266
Cdd:cd14198 251 LVKNPEKRPTAEI 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
24-269 5.88e-10

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  Cd Length: 272  Bit Score: 59.92  E-value: 5.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVfqMPFGGTQESR---QAFAEEwDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEE 100
Cdd:cd05579   7 GRVYLAKKKSTGDLYAIKV--IKKRDMIRKNqvdSVLAER-NILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPwESV--LELAEpLIDALMYLHDRDIVHGRITPDKVIIA----------GLSPV-LIDVRDVDGTPPFRSGPY 167
Cdd:cd05579  84 LENVGALD-EDVarIYIAE-IVLALEYLHSHGIIHRDLKPDNILIDanghlkltdfGLSKVgLVRRQIKLSIQKKSNGAP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 168 HVSRPPSIGQMMRSAPEAPTpNDPVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNL---KYQSPTSVASTvmecPV 244
Cdd:cd05579 162 EKEDRRIVGTPDYLAPEILL-GQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNIlngKIEWPEDPEVS----DE 236
                       250       260
                ....*....|....*....|....*..
gi 32476378 245 WMDrLVMQLLNKDPGQRPV--SAAAVK 269
Cdd:cd05579 237 AKD-LISKLLTPDPEKRLGakGIEEIK 262
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
56-262 7.31e-10

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


Pssm-ID: 270633  Cd Length: 259  Bit Score: 59.80  E-value: 7.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  56 AFAEEWDRLKRLDHPAIVKCYGGGFEEsEAYLAHELVEGSTLAEEIQRRGRLPWES-VLELAEPLIDALMYLHDRDIVHG 134
Cdd:cd05037  48 SFFETASLMSQISHKHLVKLYGVCVAD-ENIMVQEYVRYGPLDKYLRRMGNNVPLSwKLQVAKQLASALHYLEDKKLIHG 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 135 RITPDKVIIAGLSPvlidvrdvDGTPPF------------RSGPYHVSRPPSIgqmmrsAPEA-PTPNDPVTARTDLYLF 201
Cdd:cd05037 127 NVRGRNILLAREGL--------DGYPPFiklsdpgvpitvLSREERVDRIPWI------APEClRNLQANLTIAADKWSF 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32476378 202 GALLYEALTGAP-PITGSTVQEvtSNLKYQsptsvASTVMECPVW--MDRLVMQLLNKDPGQRP 262
Cdd:cd05037 193 GTTLWEICSGGEePLSALSSQE--KLQFYE-----DQHQLPAPDCaeLAELIMQCWTYEPTKRP 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
25-214 7.39e-10

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: 59.62  E-value: 7.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  25 RVWRAVHIKMRKAVAVRvfQMPFggtQESRQA----FAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLaEE 100
Cdd:cd06626  15 KVYTAVNLDTGELMAMK--EIRF---QDNDPKtikeIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTL-EE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPWESVLEL-AEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPV-LID----VRDVDGTPPFRSGPYHVSRpps 174
Cdd:cd06626  89 LLRHGRILDEAVIRVyTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIkLGDfgsaVKLKNNTTTMAPGEVNSLV--- 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 32476378 175 iGQMMRSAPEAPTpNDPVTAR---TDLYLFGALLYEALTGAPP 214
Cdd:cd06626 166 -GTPAYMAPEVIT-GNKGEGHgraADIWSLGCVVLEMATGKRP 206
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-262 7.88e-10

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  Cd Length: 268  Bit Score: 59.66  E-value: 7.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   6 LGPLAIESPLGpdpSARDARVWRAVHIKMRKAVA---VRVFQMPfggTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEE 82
Cdd:cd08228   1 LANFQIEKKIG---RGQFSEVYRATCLLDRKPVAlkkVQIFEMM---DAKARQDCVKEIDLLKQLNHPNVIKYLDSFIED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  83 SEAYLAHELVEGSTLAEEI----QRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSPV-LIDVrdvd 157
Cdd:cd08228  75 NELNIVLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVkLGDL---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 158 GTPPFRSGPYHVSRpPSIGQMMRSAPEAPTPNDpVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLKYQS------ 231
Cdd:cd08228 151 GLGRFFSSKTTAAH-SLVGTPYYMSPERIHENG-YNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQcdyppl 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 32476378 232 PTSVASTVMEcpvwmdRLVMQLLNKDPGQRP 262
Cdd:cd08228 229 PTEHYSEKLR------ELVSMCIYPDPDQRP 253
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
53-261 7.92e-10

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


Pssm-ID: 271097  Cd Length: 271  Bit Score: 59.63  E-value: 7.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  53 SRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIV 132
Cdd:cd14195  51 SREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 133 HGRITPDKVIIAGLSPVLIDVRDVDgtppfrSGPYHVSRPPSIGQMMRSAPEAPTPN----DPVTARTDLYLFGALLYEA 208
Cdd:cd14195 131 HFDLKPENIMLLDKNVPNPRIKLID------FGIAHKIEAGNEFKNIFGTPEFVAPEivnyEPLGLEADMWSIGVITYIL 204
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32476378 209 LTGAPPITGSTVQEVTSNL---KYQSPTSVASTVMECPvwmDRLVMQLLNKDPGQR 261
Cdd:cd14195 205 LSGASPFLGETKQETLTNIsavNYDFDEEYFSNTSELA---KDFIRRLLVKDPKKR 257
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
53-227 1.06e-09

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


Pssm-ID: 271098  Cd Length: 269  Bit Score: 59.20  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  53 SRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIV 132
Cdd:cd14196  51 SREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 133 HGRITPD--------------KVIIAGLSPVL---IDVRDVDGTPPFrsgpyhvsrppsigqmmrSAPEApTPNDPVTAR 195
Cdd:cd14196 131 HFDLKPEnimlldknipiphiKLIDFGLAHEIedgVEFKNIFGTPEF------------------VAPEI-VNYEPLGLE 191
                       170       180       190
                ....*....|....*....|....*....|..
gi 32476378 196 TDLYLFGALLYEALTGAPPITGSTVQEVTSNL 227
Cdd:cd14196 192 ADMWSIGVITYILLSGASPFLGDTKQETLANI 223
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
26-214 1.09e-09

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: 59.14  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVfqMPFGgTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQ-RR 104
Cdd:cd05122  16 VYKARHKKTGQIVAIKK--INLE-SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKnTN 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 105 GRLP-------WESVLElaeplidALMYLHDRDIVHGRITPD----------KVIIAGLSPVLIDVRDVD---GTPPFrs 164
Cdd:cd05122  93 KTLTeqqiayvCKEVLK-------GLEYLHSHGIIHRDIKAAnilltsdgevKLIDFGLSAQLSDGKTRNtfvGTPYW-- 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 32476378 165 gpyhvsrppsigqMmrsAPEAPTpNDPVTARTDLYLFGALLYEALTGAPP 214
Cdd:cd05122 164 -------------M---APEVIQ-GKPYGFKADIWSLGITAIEMAEGKPP 196
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
26-262 1.27e-09

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  Cd Length: 265  Bit Score: 58.90  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVFQMpfGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRG 105
Cdd:cd06605  17 VSKVRHRPSGQIMAVKVIRL--EIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLDKILKEVG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 106 RLPwESVL-ELAEPLIDALMYLHD-RDIVHGRITPDKVIIA----------GLSPVLIDvrDVDGTppfrsgpyhvsrpp 173
Cdd:cd06605  95 RIP-ERILgKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNsrgqvklcdfGVSGQLVD--SLAKT-------------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 174 SIGQMMRSAPEAPTPNDpVTARTDLYLFGALLYEALTGA---PPITGSTVQEVTSNLKY--QSPTSVASTVMECPVWMDr 248
Cdd:cd06605 158 FVGTRSYMAPERISGGK-YTVKSDIWSLGLSLVELATGRfpyPPPNAKPSMMIFELLSYivDEPPPLLPSGKFSPDFQD- 235
                       250
                ....*....|....
gi 32476378 249 LVMQLLNKDPGQRP 262
Cdd:cd06605 236 FVSQCLQKDPTERP 249
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
52-261 1.31e-09

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  Cd Length: 267  Bit Score: 58.87  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  52 ESRQAFAEEWDRLKRLDHPAIVKCYGggFEE--SEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDR 129
Cdd:cd14202  43 KSQTLLGKEIKILKELKHENIVALYD--FQEiaNSVYLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSK 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 130 DIVHGRITPDKVIIA-----GLSPVLIDVRDVD-GTPPFRSGpyHVSRPPSIGQMMRSAPEAPTPNDpVTARTDLYLFGA 203
Cdd:cd14202 121 GIIHRDLKPQNILLSysggrKSNPNNIRIKIADfGFARYLQN--NMMAATLCGSPMYMAPEVIMSQH-YDAKADLWSIGT 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32476378 204 LLYEALTGAPPITGSTVQEVtsNLKYQSPTSVASTV-MECPVWMDRLVMQLLNKDPGQR 261
Cdd:cd14202 198 IIYQCLTGKAPFQASSPQDL--RLFYEKNKSLSPNIpRETSSHLRQLLLGLLQRNQKDR 254
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
64-262 2.25e-09

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  Cd Length: 275  Bit Score: 58.56  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  64 LKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPwESVLEL-AEPLIDALMYLHDRDIVHGRITPDKVI 142
Cdd:cd14084  65 LKKLSHPCIIKIEDFFDAEDDYYIVLELMEGGELFDRVVSNKRLK-EAICKLyFYQMLLAVKYLHSNGIIHRDLKPENVL 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 143 IA-------------GLSPVLID---VRDVDGTPPFrsgpyhvsrppsigqmmrSAPEAPTPNDPV--TARTDLYLFGAL 204
Cdd:cd14084 144 LSsqeeeclikitdfGLSKILGEtslMKTLCGTPTY------------------LAPEVLRSFGTEgyTRAVDCWSLGVI 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32476378 205 LYEALTGAPPI----TGSTVQEVTSNLKYqspTSVASTVMECPVWMDRLVMQLLNKDPGQRP 262
Cdd:cd14084 206 LFICLSGYPPFseeyTQMSLKEQILSGKY---TFIPKAWKNVSEEAKDLVKKMLVVDPSRRP 264
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
53-262 2.67e-09

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


Pssm-ID: 270881  Cd Length: 265  Bit Score: 58.16  E-value: 2.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  53 SRQAFAEEWDRLkRLDHPAIVKCYG---GGFEESEAYLAHELVEGSTLAEEI-QRRGRLPWESVLELAEPLIDALMYLHD 128
Cdd:cd13979  43 SRQSFWAELNAA-RLRHENIVRVLAaetGTDFASLGLIIMEYCGNGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHS 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 129 RDIVHGRITPDKVIIA----------GLSPVLIDVRDVD-GTPPFRSGPYHVsrppsigqmmrsAPEApTPNDPVTARTD 197
Cdd:cd13979 122 HGIVHLDVKPANILISeqgvcklcdfGCSVKLGEGNEVGtPRSHIGGTYTYR------------APEL-LKGERVTPKAD 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32476378 198 LYLFGALLYEALTGAPPITG--STV--QEVTSNLKyqsPTSVASTVMECPVWMDRLVMQLLNKDPGQRP 262
Cdd:cd13979 189 IYSFGITLWQMLTRELPYAGlrQHVlyAVVAKDLR---PDLSGLEDSEFGQRLRSLISRCWSAQPAERP 254
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-262 2.87e-09

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  Cd Length: 292  Bit Score: 58.50  E-value: 2.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378   1 MPRSRLGPLAIESPLGpdpSARDARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGF 80
Cdd:cd08229  18 MGYNTLANFRIEKKIG---RGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  81 EESEAYLAHELVEGSTLAEEI----QRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSpvLIDVRDV 156
Cdd:cd08229  95 EDNELNIVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG--VVKLGDL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 157 dGTPPFRSGPYHVSRpPSIGQMMRSAPEAPTPNDpVTARTDLYLFGALLYEALTGAPPITGSTVqevtsNLkyqspTSVA 236
Cdd:cd08229 173 -GLGRFFSSKTTAAH-SLVGTPYYMSPERIHENG-YNFKSDIWSLGCLLYEMAALQSPFYGDKM-----NL-----YSLC 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32476378 237 STVMEC---PVWMD-------RLVMQLLNKDPGQRP 262
Cdd:cd08229 240 KKIEQCdypPLPSDhyseelrQLVNMCINPDPEKRP 275
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
24-270 3.02e-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  Cd Length: 252  Bit Score: 57.78  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  24 ARVWRAVHIKMRKAVAVRVFQMPFGGTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESEAYLAHELVEGSTLA---EE 100
Cdd:cd13997  14 SEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSLQdalEE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 101 IQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIaglspvlidvrDVDGTppFRSGPY-HVSRPPSIGQMM 179
Cdd:cd13997  94 LSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI-----------SNKGT--CKIGDFgLATRLETSGDVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 180 RS-----APEAPTPNDPVTARTDLYLFGALLYEALTGAP-PITGSTVQEVTSNLKYQSPTSVASTVmecpvwMDRLVMQL 253
Cdd:cd13997 161 EGdsrylAPELLNENYTHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQLRQGKLPLPPGLVLSQE------LTRLLKVM 234
                       250
                ....*....|....*..
gi 32476378 254 LNKDPGQRPVSAAAVKL 270
Cdd:cd13997 235 LDPDPTRRPTADQLLAH 251
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
26-261 3.04e-09

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  Cd Length: 266  Bit Score: 57.94  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKMRKAVAVRVFQMPFGGTQESRqAFAEEWDRLKRLDHPAIVKcYGGGFEESE-AYLAHELVEGSTLAEEIQRR 104
Cdd:cd14097  17 VIEATHKETQTKWAIKKINREKAGSSAVK-LLEREVDILKHVNHAHIIH-LEEVFETPKrMYLVMELCEDGELKELLLRK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 105 GRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGlSPV------LIDVRDVdGTPPFRSGPYHVSRPPSIGQM 178
Cdd:cd14097  95 GFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKS-SIIdnndklNIKVTDF-GLSVQKYGLGEDMLQETCGTP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 179 MRSAPEAPTPNDpVTARTDLYLFGALLYEALTGAPPITGSTVQEVTSNLK---YQSPTSVASTVMECPvwmDRLVMQLLN 255
Cdd:cd14097 173 IYMAPEVISAHG-YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRkgdLTFTQSVWQSVSDAA---KNVLQQLLK 248

                ....*.
gi 32476378 256 KDPGQR 261
Cdd:cd14097 249 VDPAHR 254
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
26-265 3.15e-09

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  Cd Length: 252  Bit Score: 57.65  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  26 VWRAVHIKmrKAVAVRVFQmpfggTQESRQAFAEEWDRLKRLDHPAIVKCYGGGFEESeaYLAHELVEGSTLAEEIQR-R 104
Cdd:cd14068  10 VYRAVYRG--EDVAVKIFN-----KHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSLDALLQQdN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 105 GRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIAGLSP-----------------VLIDVRDVDGTPPFRsgpy 167
Cdd:cd14068  81 ASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPncaiiakiadygiaqycCRMGIKTSEGTPGFR---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 168 hvsrppsigqmmrsAPEAPTPNDPVTARTDLYLFGALLYEALTGAPPITG-----STVQEVTSNLKYQSPTSVAStvmeC 242
Cdd:cd14068 157 --------------APEVARGNVIYNQQADVYSFGLLLYDILTCGERIVEglkfpNEFDELAIQGKLPDPVKEYG----C 218
                       250       260
                ....*....|....*....|....*
gi 32476378 243 PVW--MDRLVMQLLNKDPGQRPVSA 265
Cdd:cd14068 219 APWpgVEALIKDCLKENPQCRPTSA 243
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
68-227 3.19e-09

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  Cd Length: 268  Bit Score: 57.75  E-value: 3.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378  68 DHPAIVKCYGGGFEESEAYLAHELVEGSTLAEEIQRRGRLPWESVLELAEPLIDALMYLHDRDIVHGRITPDKVIIA--- 144
Cdd:cd14106  66 DCPRVVNLHEVYETRSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTsef 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476378 145 ----------GLSPVL---IDVRDVDGTPPFrsgpyhvsrppsigqmmrSAPEAPTpNDPVTARTDLYLFGALLYEALTG 211
Cdd:cd14106 146 plgdiklcdfGISRVIgegEEIREILGTPDY------------------VAPEILS-YEPISLATDMWSIGVLTYVLLTG 206
                       170
                ....*....|....*.
gi 32476378 212 APPITGSTVQEVTSNL 227
Cdd:cd14106 207 HSPFGGDDKQETFLNI 222
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
25-133 3.19e-09

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 phosphot