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Conserved domains on  [gi|13507987|ref|NP_109936|]
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serine/threonine-protein kinase [Mycoplasma pneumoniae M129]

Protein classification: 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 ...
14-322 2.01e-64

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 208.59  E-value: 2.01e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHvqefgpLQKRqftrLVLKVVQRTDKINDNNWKKFLDGTITTTRVSHKNLVQTFDVV 93
Cdd:cd14014   1 RYRLVRLLGRGGM-GEVYRARDTL------LGRP----VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsenqviVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFT 173
Cdd:cd14014  70 -------------EDDGRPYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHR--AGIVHRDIKPANILLT 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 174 SNLTdIKLLDFGIASAVirnaeKTEVLTDENSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDIYSLGVILFEMLVGR 253
Cdd:cd14014 135 EDGR-VKLTDFGIARAL-----GDSGLTQTGSVLGTPAYMAPEQARG----------GPVDPRSDIYSLGVVLYELLTGR 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987 254 VPFNKSIDPkkerETIQKARNFDVPLMGNLRSDVPVSLENIVFKCTAVKRENSkwmYSDTKQLLADLAQ 322
Cdd:cd14014 199 PPFDGDSPA----AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEER---PQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
80-298 4.43e-42

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 149.22  E-value: 4.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987     80 RVSHKNLVQTFDVvsprlsvlsenqvIVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:smart00220  53 KLKHPNIVRLYDV-------------FEDEDKLYLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS--KG 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987    160 IIHRDLKPENILFTSNlTDIKLLDFGIASAVIRNAEKTevltdenSLFGTVSYMTPEVLEstvnkegkriRKPPTVQYDI 239
Cdd:smart00220 118 IVHRDLKPENILLDED-GHVKLADFGLARQLDPGEKLT-------TFVGTPEYMAPEVLL----------GKGYGKAVDI 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987    240 YSLGVILFEMLVGRVPFNksiDPKKERETIQKARNFDVPLMGNlRSDVPVSLENIVFKC 298
Cdd:smart00220 180 WSLGVILYELLTGKPPFP---GDDQLLELFKKIGKPKPPFPPP-EWDISPEAKDLIRKL 234
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
14-322 2.01e-64

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 208.59  E-value: 2.01e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHvqefgpLQKRqftrLVLKVVQRTDKINDNNWKKFLDGTITTTRVSHKNLVQTFDVV 93
Cdd:cd14014   1 RYRLVRLLGRGGM-GEVYRARDTL------LGRP----VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsenqviVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFT 173
Cdd:cd14014  70 -------------EDDGRPYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHR--AGIVHRDIKPANILLT 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 174 SNLTdIKLLDFGIASAVirnaeKTEVLTDENSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDIYSLGVILFEMLVGR 253
Cdd:cd14014 135 EDGR-VKLTDFGIARAL-----GDSGLTQTGSVLGTPAYMAPEQARG----------GPVDPRSDIYSLGVVLYELLTGR 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987 254 VPFNKSIDPkkerETIQKARNFDVPLMGNLRSDVPVSLENIVFKCTAVKRENSkwmYSDTKQLLADLAQ 322
Cdd:cd14014 199 PPFDGDSPA----AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEER---PQSAAELLAALRA 260
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
114-187 9.01e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 53.76  E-value: 9.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507987  114 IVMEYVDGPSLREMLNQKGYfsvqEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNltDIKLLDFGIA 187
Cdd:PRK14879  76 IVMEYIEGEPLKDLINSNGM----EELELSREIGRLVGKLHS--AGIIHGDLTTSNMILSGG--KIYLIDFGLA 141
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
109-188 3.45e-07

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 49.20  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 109 EDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKlvkvinyLHsfEHQIIHRDLKPENILFTSnlTDIKLLDFGIAS 188
Cdd:COG3642  71 PDNGLIVMEYIEGELLKDALEEARPDLLREVGRLVGK-------LH--KAGIVHGDLTTSNIILSG--GRIYFIDFGLGE 139
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
114-187 1.03e-06

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 47.59  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507987   114 IVMEYVDGPSLREMLNQKGYfsvqevvYYFTKLVKVINYLHsfEHQIIHRDLKPENILFTSNltDIKLLDFGIA 187
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIEENGD-------ELAREIGRLVGKLH--KAGIVHGDLTTSNIIVRDD--KVYLIDFGLG 136
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
80-298 4.43e-42

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 149.22  E-value: 4.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987     80 RVSHKNLVQTFDVvsprlsvlsenqvIVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:smart00220  53 KLKHPNIVRLYDV-------------FEDEDKLYLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHS--KG 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987    160 IIHRDLKPENILFTSNlTDIKLLDFGIASAVIRNAEKTevltdenSLFGTVSYMTPEVLEstvnkegkriRKPPTVQYDI 239
Cdd:smart00220 118 IVHRDLKPENILLDED-GHVKLADFGLARQLDPGEKLT-------TFVGTPEYMAPEVLL----------GKGYGKAVDI 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987    240 YSLGVILFEMLVGRVPFNksiDPKKERETIQKARNFDVPLMGNlRSDVPVSLENIVFKC 298
Cdd:smart00220 180 WSLGVILYELLTGKPPFP---GDDQLLELFKKIGKPKPPFPPP-EWDISPEAKDLIRKL 234
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
14-352 1.60e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 142.96  E-value: 1.60e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHvqefgplqkrqftRLVLKVVQRTDKINDNNWKKFLDGTITTTRVSHKNLVQTFDvv 93
Cdd:COG0515   1 SYRILRKLGEGSF-GEVYLARDRK-------------LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLY-- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsenQVIVLEDTVMIVMEYVDGPSLREMLN---QKGYFSVQEVVYYFTKLVKVINYLHsfEHQIIHRDLKPENI 170
Cdd:COG0515  65 ----------DFFQDEGSLYLVMEYVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLH--SKGIIHRDIKPENI 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 171 LFTSNLTDIKLLDFGIASAVIRNAEKTEVLTDENSLFGTVSYMTPEVLESTVNkegkrirKPPTVQYDIYSLGVILFEML 250
Cdd:COG0515 133 LLDRDGRVVKLIDFGLAKLLPDPGSTSSIPALPSTSVGTPGYMAPEVLLGLSL-------AYASSSSDIWSLGITLYELL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 251 VGRVPFNKSIDPKKERETIQKARNFDVPLMGN-----LRSDVPVSLENIVFKCTAVKRENSKWMYSDTKQLLADLAQWQT 325
Cdd:COG0515 206 TGLPPFEGEKNSSATSQTLKIILELPTPSLASplspsNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKE 285
                       330       340
                ....*....|....*....|....*..
gi 13507987 326 EQTLIKPVHERILEGQNEMRELMVSNY 352
Cdd:COG0515 286 SDLSDLLKPDDSAPLRLSLPPSLEALI 312
Pkinase pfam00069
Protein kinase domain;
80-256 5.22e-36

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 132.72  E-value: 5.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987    80 RVSHKNLVQTFDVVSPrlsvlsenqvivlEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:pfam00069  54 KLNHPNIVRLYDVFED-------------KDHLYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHS--NG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987   160 IIHRDLKPENILFTSNLtDIKLLDFGIASAVIRNAEKTevltdenSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDI 239
Cdd:pfam00069 119 IVHRDLKPENILIDEDG-NLKITDFGLAKQLSSGSKLT-------TFVGTPWYMAPEVLRG----------NPYGPKVDV 180
                         170
                  ....*....|....*..
gi 13507987   240 YSLGVILFEMLVGRVPF 256
Cdd:pfam00069 181 WSLGCILYELLTGKPPF 197
pknD PRK13184
serine/threonine-protein kinase; Reviewed
14-363 4.75e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 94.07  E-value: 4.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987   14 KYRIEKLINRGGMNSyLFLAsnlhvqeFGPLQKRqftRLVLKVVqRTDKINDNNWKK-FLDGTITTTRVSHKNLVqtfdv 92
Cdd:PRK13184   3 RYDIIRLIGKGGMGE-VYLA-------YDPVCSR---RVALKKI-REDLSENPLLKKrFLREAKIAADLIHPGIV----- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987   93 vsPRLSVLSENqvivleDTVMIVMEYVDGPSLREMLN---QKGYF--------SVQEVVYYFTKLVKVINYLHSfeHQII 161
Cdd:PRK13184  66 --PVYSICSDG------DPVYYTMPYIEGYTLKSLLKsvwQKESLskelaektSVGAFLSIFHKICATIEYVHS--KGVL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  162 HRDLKPENILFtSNLTDIKLLDFGiaSAVIRNAEKTEVLT----DENSLF----------GTVSYMTPEVLESTvnkegk 227
Cdd:PRK13184 136 HRDLKPDNILL-GLFGEVVILDWG--AAIFKKLEEEDLLDidvdERNICYssmtipgkivGTPDYMAPERLLGV------ 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  228 rirkPPTVQYDIYSLGVILFEMLVGRVPFNKsidpKKERETIQKARNFDVPLMGNLRsDVPVSLENIVFKCTAVkreNSK 307
Cdd:PRK13184 207 ----PASESTDIYALGVILYQMLTLSFPYRR----KKGRKISYRDVILSPIEVAPYR-EIPPFLSQIAMKALAV---DPA 274
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987  308 WMYSDTKQLLADLAQWqteqtlikpvheriLEGQNEMRE---LMVSNYLPWYLRKGVLI 363
Cdd:PRK13184 275 ERYSSVQELKQDLEPH--------------LQGSPEWTVkatLMTKKKSCWKFYEPILL 319
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
51-254 9.43e-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 [Multi-domain]  Cd Length: 1266  Bit Score: 84.13  E-value: 9.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987     51 RLVLKVVqRTDKIND-NNWKKFLDGTITTTRVSHKNLVQTFDV-VSPrlsvlsenqvivlEDTVMIVMEYVDGPSLREML 128
Cdd:TIGR03903    5 EVAIKLL-RTDAPEEeHQRARFRRETALCARLYHPNIVALLDSgEAP-------------PGLLFAVFEYVPGRTLREVL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987    129 NQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSnlTDI----KLLDFGIaSAVIRNAEKTEV--LTD 202
Cdd:TIGR03903   71 AADGALPAGETGRLMLQVLDALACAHN--QGIVHRDLKPQNIMVSQ--TGVrphaKVLDFGI-GTLLPGVRDADVatLTR 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13507987    203 ENSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDIYSLGVILFEMLVGRV 254
Cdd:TIGR03903  146 TTEVLGTPTYCAPEQLRG----------EPVTPNSDLYAWGLIFLECLTGQR 187
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
14-322 2.01e-64

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 208.59  E-value: 2.01e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHvqefgpLQKRqftrLVLKVVQRTDKINDNNWKKFLDGTITTTRVSHKNLVQTFDVV 93
Cdd:cd14014   1 RYRLVRLLGRGGM-GEVYRARDTL------LGRP----VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsenqviVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFT 173
Cdd:cd14014  70 -------------EDDGRPYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHR--AGIVHRDIKPANILLT 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 174 SNLTdIKLLDFGIASAVirnaeKTEVLTDENSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDIYSLGVILFEMLVGR 253
Cdd:cd14014 135 EDGR-VKLTDFGIARAL-----GDSGLTQTGSVLGTPAYMAPEQARG----------GPVDPRSDIYSLGVVLYELLTGR 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507987 254 VPFNKSIDPkkerETIQKARNFDVPLMGNLRSDVPVSLENIVFKCTAVKRENSkwmYSDTKQLLADLAQ 322
Cdd:cd14014 199 PPFDGDSPA----AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEER---PQSAAELLAALRA 260
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
14-278 2.42e-38

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 139.19  E-value: 2.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHVQEFgplqkrqftrLVLKVVQRtDKINDNNWKKFLDGTITTTRVSHKNLVQTFDVV 93
Cdd:cd14003   1 NYELGKTLGEGSF-GKVKLARHKLTGEK----------VAIKIIDK-SKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVI 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvLSENQVIvledtvmIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFT 173
Cdd:cd14003  69 ------ETENKIY-------LVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHS--NGIVHRDLKLENILLD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 174 SNLtDIKLLDFGiASAVIRNAEKTevltdeNSLFGTVSYMTPEVLESTvNKEGKRIrkpptvqyDIYSLGVILFEMLVGR 253
Cdd:cd14003 134 KNG-NLKIIDFG-LSNEFRGGSLL------KTFCGTPAYAAPEVLLGR-KYDGPKA--------DVWSLGVILYAMLTGY 196
                       250       260
                ....*....|....*....|....*
gi 13507987 254 VPFNKSIDPKKERETIQKarNFDVP 278
Cdd:cd14003 197 LPFDDDNDSKLFRKILKG--KYPIP 219
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
80-276 1.03e-34

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 129.52  E-value: 1.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  80 RVSHKNLVQTFDVVsprlsvlsENqvivlEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:cd05117  55 RLDHPNIVKLYEVF--------ED-----DKNLYLVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHS--QG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 160 IIHRDLKPENILFTSNLTD--IKLLDFGIASAVirnaEKTEVLTDensLFGTVSYMTPEVLestvnkEGKRIRKPptvqY 237
Cdd:cd05117 120 IVHRDLKPENILLASKDPDspIKIIDFGLAKIF----EEGEKLKT---VCGTPYYVAPEVL------KGKGYGKK----C 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 13507987 238 DIYSLGVILFEMLVGRVPFNKSiDPKKERETIQKAR-NFD 276
Cdd:cd05117 183 DIWSLGVILYILLCGYPPFYGE-TEQELFEKILKGKySFD 221
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
109-277 9.79e-31

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 117.96  E-value: 9.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 109 EDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNLtDIKLLDFGIAS 188
Cdd:cd14007  72 KKRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHS--KNIIHRDIKPENILLGSNG-ELKLADFGWSV 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 189 AVIRNAEKTevltdensLFGTVSYMTPEVLEstvnkegkriRKPPTVQYDIYSLGVILFEMLVGRVPFnksiDPKKERET 268
Cdd:cd14007 149 HAPSNRRKT--------FCGTLDYLPPEMVE----------GKEYDYKVDIWSLGVLCYELLVGKPPF----ESKSHQET 206

                ....*....
gi 13507987 269 IQKARNFDV 277
Cdd:cd14007 207 YKRIQNVDI 215
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
115-256 1.20e-30

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 117.62  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 115 VMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSnltD--IKLLDFGIASAVIR 192
Cdd:cd05123  71 VLDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHS--LGIIYRDLKPENILLDS---DghIKLTDFGLAKELSS 145
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507987 193 NAEKTevltdeNSLFGTVSYMTPEVLEstvnkegkriRKPPTVQYDIYSLGVILFEMLVGRVPF 256
Cdd:cd05123 146 DGDRT------YTFCGTPEYLAPEVLL----------GKGYGKAVDWWSLGVLLYEMLTGKPPF 193
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
81-263 4.37e-30

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 116.15  E-value: 4.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  81 VSHKNLVQTFDvvsprlSVLsenqvivLEDTVMIVMEYVDGPSLREMLNQKGY-FSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:cd05122  54 CKHPNIVKYYG------SYL-------KKDELWIVMEFCSGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHS--HG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 160 IIHRDLKPENILFTSNlTDIKLLDFGIASAVIRNaektevlTDENSLFGTVSYMTPEVLEstvnkegkriRKPPTVQYDI 239
Cdd:cd05122 119 IIHRDIKAANILLTSD-GEVKLIDFGLSAQLSDG-------KTRNTFVGTPYWMAPEVIQ----------GKPYGFKADI 180
                       170       180
                ....*....|....*....|....
gi 13507987 240 YSLGVILFEMLVGRVPFNKSIDPK 263
Cdd:cd05122 181 WSLGITAIEMAEGKPPYSELPPMK 204
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
109-278 5.60e-30

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 116.55  E-value: 5.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 109 EDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNLTdIKLLDFGIAS 188
Cdd:cd05579  65 KKNLYLVMEYLPGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHS--HGIIHRDLKPDNILIDANGH-LKLTDFGLSK 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 189 A---------VIRNAEKTEVLTDENSLFGTVSYMTPEVLESTvnKEGKRIrkpptvqyDIYSLGVILFEMLVGRVPFNKS 259
Cdd:cd05579 142 VglvrrqiklSIQKKSNGAPEKEDRRIVGTPDYLAPEILLGQ--GHGKTV--------DWWSLGVILYEFLVGIPPFHAE 211
                       170
                ....*....|....*....
gi 13507987 260 idpkKERETIQKARNFDVP 278
Cdd:cd05579 212 ----TPEEIFQNILNGKIE 226
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
50-249 1.03e-29

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 114.29  E-value: 1.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  50 TRLVLKVVqrtDKINDNNWKKFLDGTITT-TRVSHKNLVQTFDVVSprlsvlsenqvivLEDTVMIVMEYVDGPSLREML 128
Cdd:cd00180  19 KKVAVKVI---PKEKLKKLLEELLREIEIlKKLNHPNIVKLYDVFE-------------TENFLYLVMEYCEGGSLKDLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 129 NQK-GYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNLTdIKLLDFGIAsaviRNAEKTEVLTDENSLF 207
Cdd:cd00180  83 KENkGPLSEEEALSILRQLLSALEYLHS--NGIIHRDLKPENILLDSDGT-VKLADFGLA----KDLDSDDSLLKTTGGT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13507987 208 GTVSYMTPEVLEstvnkegkriRKPPTVQYDIYSLGVILFEM 249
Cdd:cd00180 156 TPPYYAPPELLG----------GRYYGPKVDIWSLGVILYEL 187
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
109-292 5.39e-29

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 115.07  E-value: 5.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 109 EDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSFEHqiIHRDLKPENILFTSNlTDIKLLDFGIAS 188
Cdd:cd05573  73 EDHLYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGF--IHRDIKPDNILLDAD-GHIKLADFGLCT 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 189 AVIRNAEKTEVLTDE-----------------------NSLFGTVSYMTPEVLestvnkegkrIRKPPTVQYDIYSLGVI 245
Cdd:cd05573 150 KMNKSGDRESYLNDSvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVL----------RGTGYGPECDWWSLGVI 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13507987 246 LFEMLVGRVPFNKSidpkKERETIQKARNFDVPLMgnLRSDVPVSLE 292
Cdd:cd05573 220 LYEMLYGFPPFYSD----SLVETYSKIMNWKESLV--FPDDPDVSPE 260
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
82-276 1.91e-28

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 112.78  E-value: 1.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  82 SHKNLVQTFDVVSPRLSVlsenqvivledtvMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQII 161
Cdd:cd14092  57 GHPNIVKLHEVFQDELHT-------------YLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHS--KGVV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 162 HRDLKPENILFTSNLTD--IKLLDFGIASAvirnaeKTEVLTDENSLFgTVSYMTPEVLESTVNKEGKrirkppTVQYDI 239
Cdd:cd14092 122 HRDLKPENLLFTDEDDDaeIKIVDFGFARL------KPENQPLKTPCF-TLPYAAPEVLKQALSTQGY------DESCDL 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 13507987 240 YSLGVILFEMLVGRVPFNKSIDPKKERETIQKAR----NFD 276
Cdd:cd14092 189 WSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKsgdfSFD 229
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
46-309 4.05e-28

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 110.86  E-value: 4.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  46 KRQFTRLVLKVVQRTDKINDNN--WKKFLDGTITTTRVSHKNLVQTFDVVsprlsvlsenqvIVLEDTVMIVMEYVDGPS 123
Cdd:cd13994  17 PRSGVLYAVKEYRRRDDESKRKdyVKRLTSEYIISSKLHHPNIVKVLDLC------------QDLHGKWCLVMEYCPGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 124 LREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNLTdIKLLDFGIASAVIRNAEKTEVltDE 203
Cdd:cd13994  85 LFTLIEKADSLSLEEKDCFFKQILRGVAYLHS--HGIAHRDLKPENILLDEDGV-LKLTDFGTAEVFGMPAEKESP--MS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 204 NSLFGTVSYMTPEVLEStvnkegkrirkpptVQY-----DIYSLGVILFEMLVGRVPFNKSIDPKKERETIQKARNFDVP 278
Cdd:cd13994 160 AGLCGSEPYMAPEVFTS--------------GSYdgravDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNG 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13507987 279 LMGNLRSDVPVSLENIVFK---------CTAVKRENSKWM 309
Cdd:cd13994 226 PYEPIENLLPSECRRLIYRmlhpdpekrITIDEALNDPWV 265
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
109-257 4.13e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 110.63  E-value: 4.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 109 EDTVMIVMEYVDGPSLREMLNQ----KGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFTSNLTdIKLLDF 184
Cdd:cd08215  71 NGKLCIVMEYADGGDLAQKIKKqkkkGQPFPEEQILDWFVQICLALKYLHS--RKILHRDLKTQNIFLTKDGV-VKLGDF 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507987 185 GIASAVIRNAEKTevltdeNSLFGTVSYMTPEVLEStvnkegkrirKPPTVQYDIYSLGVILFEMLVGRVPFN 257
Cdd:cd08215 148 GISKVLESTTDLA------KTVVGTPYYLSPELCEN----------KPYNYKSDIWALGCVLYELCTLKHPFE 204
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
80-298 1.59e-27

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 108.78  E-value: 1.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  80 RVSHKNLVQTFDVV--SPRLsvlsenqvivledtvMIVMEYVDGPSLREML-NQKGYFSVQEVVYYFTKLVKVINYLHSf 156
Cdd:cd13999  46 KLRHPNIVQFIGAClsPPPL---------------CIVTEYMPGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHS- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 157 eHQIIHRDLKPENILFTSNLTdIKLLDFGIASAVirnAEKTEVLTDENslfGTVSYMTPEVLEStvnkegkrirKPPTVQ 236
Cdd:cd13999 110 -PPIIHRDLKSLNILLDENFT-VKIADFGLSRIK---NSTTEKMTGVV---GTPRWMAPEVLRG----------EPYTEK 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507987 237 YDIYSLGVILFEMLVGRVPFnksidpkKERETIQKA-RNFDVPLMGNLRSDVPVSLENIVFKC 298
Cdd:cd13999 172 ADVYSFGIVLWELLTGEVPF-------KELSPIQIAaAVVQKGLRPPIPPDCPPELSKLIKRC 227
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
15-292 1.62e-27

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 109.19  E-value: 1.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  15 YRIEKLINRGgmnSYlflASNLHVQEFGPLQKRqftRLVLKVVQRTdKINDNNWKKFLDGTITT-TRVSHKNLVQTFDVv 93
Cdd:cd14080   2 YRLGKTIGEG---SY---SKVKLAEYTKSGLKE---KVACKIIDKK-KAPKDFLEKFLPRELEIlRKLRHPNIIQVYSI- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsenqvIVLEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSFEhqIIHRDLKPENILFT 173
Cdd:cd14080  71 ------------FERGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLD--IAHRDLKCENILLD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 174 SNLTdIKLLDFGIAsaviRNAEKTEVLTDENSLFGTVSYMTPEVLESTvnkegkrirkP--PTVqYDIYSLGVILFEMLV 251
Cdd:cd14080 137 SNNN-VKLSDFGFA----RLCPDDDGDVLSKTFCGSAAYAAPEILQGI----------PydPKK-YDIWSLGVILYIMLC 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 13507987 252 GRVPFNKSiDPKKEREtIQKARNFDVPlmgnlRSDVPVSLE 292
Cdd:cd14080 201 GSMPFDDS-NIKKMLK-DQQNRKVRFP-----SSVKKLSPE 234
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
80-256 2.67e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 108.38  E-value: 2.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  80 RVSHKNLVQTFDvvsprlsvlSENQvivlEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQ 159
Cdd:cd06606  55 SLKHPNIVRYLG---------TERT----ENTLNIFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHS--NG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987 160 IIHRDLKPENILFTSNLTdIKLLDFGIAsaviRNAEKTEVLTDENSLFGTVSYMTPEVlestVNKEGkrirkpPTVQYDI 239
Cdd:cd06606 120 IVHRDIKGANILVDSDGV-VKLADFGCA----KRLAEIATGEGTKSLRGTPYWMAPEV----IRGEG------YGRAADI 184
                       170
                ....*....|....*..
gi 13507987 240 YSLGVILFEMLVGRVPF 256
Cdd:cd06606 185 WSLGCTVIEMATGKPPW 201
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
14-292 2.71e-27

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 108.41  E-value: 2.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  14 KYRIEKLINRGGMnSYLFLASNLHVQEfgplqkrqftRLVLKVVQRTDKINDNNWKKFLDGTITTTRVSHKNLVQTFDVV 93
Cdd:cd14099   2 RYRRGKFLGKGGF-AKCYEVTDMSTGK----------VYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507987  94 sprlsvlsENqvivlEDTVMIVMEYVDGPSLREMLNQKGYFSVQEVVYYFTKLVKVINYLHSfeHQIIHRDLKPENILFT 173
Cdd:cd14099  71 --------ED-----EENVYILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVK