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Conserved domains on  [gi|22536502|ref|NP_687353|]
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serine/threonine protein kinase [Streptococcus agalactiae 2603V/R]

Protein Classification

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 ...
11-271 1.29e-121

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: 365.76  E-value: 1.29e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDLILDNEeVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRP-VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 22536502 251 TAKKLTDRYKTTYEMGRDLST 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
PASTA super family cl02768
PASTA domain. This domain is found at the C-termini of several Penicillin-binding proteins ...
355-581 7.14e-34

PASTA domain. This domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


The actual alignment was detected with superfamily member COG2815:

Pssm-ID: 322077  Cd Length: 303  Bit Score: 132.15  E-value: 7.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 355 VVGIIVFAYKIL-VSPTTIRVPDVSNKTVAQAKMTLENSGLKVGaIRNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYI 433
Cdd:COG2815   8 LVVAGVLLATFFpVSPDKVKVPNVAGLDEEDAKAELQKAGLEVG-VRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 434 ATPNKSFTLGNYKEHNYKDILKDLQGKGVKKSLIKvKRKINNDYTTGTILAQSLPEGTSFNPDGNKKLTLTVAVnDPMIM 513
Cdd:COG2815  87 STGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKIT-QEEVSDEVPAGTVISQSPSAGTEVKPGETVKLTVSKGP-ETITV 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22536502 514 PDVTGMTVGEVIETLTDLGLDadnlvfyqmqngvYQTVVTPPSSSK---IASQDPYYGGEVglRRGDKVKL 581
Cdd:COG2815 165 PDLVGMTYDEASSNLKAAGLT-------------VNSKEYVSSDRPegeVISQSPPAGTTV--NVGSKIEI 220
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-271 1.29e-121

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: 365.76  E-value: 1.29e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDLILDNEeVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRP-VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 22536502 251 TAKKLTDRYKTTYEMGRDLST 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-259 6.00e-74

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 241.28  E-value: 6.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     12 YRILKSIGRGGMADVYLARDlILDNEEVAIKVLRTNYQTDQiaVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-KKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     92 YVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLtqTNS 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    172 MLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKAT 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235

                   ....*...
gi 22536502    252 AKKLTDRY 259
Cdd:smart00220 236 VKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-339 2.81e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 206.13  E-value: 2.81e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  12 YRILKSIGRGGMADVYLARDlildNEEVAIKVLRTNYQTDQIAVARFQREARAMAELTHP-NIVAIRDIGEEDGQQFLVM 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD----RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDN---APLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGT-VKVTDFGIAVAFAETSL 166
Cdd:COG0515  78 EYVDGGSLEDLLKKIgrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 167 TQ-----TNSMLGSVHYLSPEQARGS---KATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQK---------PL 229
Cdd:COG0515 158 TSsipalPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIilelptpslAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 230 PSILAENKSVPQALENIVIKATAKKLTDRYKTTYEMGRDLSTALSSTRHREPKLVFND---TESTKTLPKVTSTVSSLTT 306
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDdsaPLRLSLPPSLEALISSLNS 317
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 22536502 307 EQLLRNQKQAKT----TEKITPDSASNDKTKSKKKAS 339
Cdd:COG0515 318 LAISGSDLKLDDsnfsKELAPNGVSSSPHNSSSLLLS 354
Pkinase pfam00069
Protein kinase domain;
12-236 7.96e-58

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 197.82  E-value: 7.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    12 YRILKSIGRGGMADVYLARDlILDNEEVAIKVLRTNYQTDQIAvARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVME 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKH-RDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    92 YVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFaeTSLTQTNS 171
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL--NSGSSLTS 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22536502   172 MLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVT----IALQHFQKPLPSILAEN 236
Cdd:pfam00069 157 FVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEiyekIIDQDFDSPRPSSISEE 225
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
38-258 9.33e-49

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: 185.05  E-value: 9.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     38 EVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGE-EDGQQFLVMEYVDGFDLKKYIQDNAPLSNNEVVRI 116
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    117 MNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGT---VKVTDFGIAV------AFAETSLTQTNSMLGSVHYLSPEQARGS 187
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTllpgvrDADVATLTRTTEVLGTPTYCAPEQLRGE 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22536502    188 KATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQkPLPSilaenkSVPQALE-----NIVIKATAKKLTDR 258
Cdd:TIGR03903  165 PVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLS-PVDV------SLPPWIAghplgQVLRKALNKDPRQR 233
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-269 1.10e-44

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 171.49  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502   10 GRYRILKSIGRGGMADVYLARDLILdNEEVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLV 89
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVC-SRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502   90 MEYVDGFDLKKYIQD-------NAPLSNNEVV----RIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIA 158
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  159 VA-------FAETSLTQTNSM----------LGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIA 221
Cdd:PRK13184 161 IFkkleeedLLDIDVDERNICyssmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIS 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 22536502  222 LQHfQKPLPSILAENKSVPQALENIVIKATAKKLTDRYKTTYEMGRDL 269
Cdd:PRK13184 241 YRD-VILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
355-581 7.14e-34

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225372  Cd Length: 303  Bit Score: 132.15  E-value: 7.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 355 VVGIIVFAYKIL-VSPTTIRVPDVSNKTVAQAKMTLENSGLKVGaIRNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYI 433
Cdd:COG2815   8 LVVAGVLLATFFpVSPDKVKVPNVAGLDEEDAKAELQKAGLEVG-VRERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 434 ATPNKSFTLGNYKEHNYKDILKDLQGKGVKKSLIKvKRKINNDYTTGTILAQSLPEGTSFNPDGNKKLTLTVAVnDPMIM 513
Cdd:COG2815  87 STGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKIT-QEEVSDEVPAGTVISQSPSAGTEVKPGETVKLTVSKGP-ETITV 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22536502 514 PDVTGMTVGEVIETLTDLGLDadnlvfyqmqngvYQTVVTPPSSSK---IASQDPYYGGEVglRRGDKVKL 581
Cdd:COG2815 165 PDLVGMTYDEASSNLKAAGLT-------------VNSKEYVSSDRPegeVISQSPPAGTTV--NVGSKIEI 220
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
374-434 1.34e-15

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 73.33  E-value: 1.34e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22536502 374 VPDVSNKTVAQAKMTLENSGLKVGAIRNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYIA 434
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA smart00740
PASTA domain;
368-435 5.46e-13

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 66.17  E-value: 5.46e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22536502    368 SPTTIRVPDVSNKTVAQAKMTLENSGLKVGAIrNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYIAT 435
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVV-EEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
372-435 2.91e-12

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 309063  Cd Length: 63  Bit Score: 63.80  E-value: 2.91e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22536502   372 IRVPDVSNKTVAQAKMTLENSGLKVGaIRNIESDSVSEGLVVKTDPAAGRSRREGAKVNLYIAT 435
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVG-TVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-271 1.29e-121

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: 365.76  E-value: 1.29e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDLILDNEeVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRP-VAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 22536502 251 TAKKLTDRYKTTYEMGRDLST 271
Cdd:cd14014 240 LAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-259 6.00e-74

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 241.28  E-value: 6.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     12 YRILKSIGRGGMADVYLARDlILDNEEVAIKVLRTNYQTDQiaVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-KKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     92 YVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLtqTNS 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    172 MLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQKPLPSILAENKSVPQALENIVIKAT 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235

                   ....*...
gi 22536502    252 AKKLTDRY 259
Cdd:smart00220 236 VKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-339 2.81e-59

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 206.13  E-value: 2.81e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  12 YRILKSIGRGGMADVYLARDlildNEEVAIKVLRTNYQTDQIAVARFQREARAMAELTHP-NIVAIRDIGEEDGQQFLVM 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD----RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDN---APLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGT-VKVTDFGIAVAFAETSL 166
Cdd:COG0515  78 EYVDGGSLEDLLKKIgrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 167 TQ-----TNSMLGSVHYLSPEQARGS---KATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQK---------PL 229
Cdd:COG0515 158 TSsipalPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIilelptpslAS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502 230 PSILAENKSVPQALENIVIKATAKKLTDRYKTTYEMGRDLSTALSSTRHREPKLVFND---TESTKTLPKVTSTVSSLTT 306
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDdsaPLRLSLPPSLEALISSLNS 317
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 22536502 307 EQLLRNQKQAKT----TEKITPDSASNDKTKSKKKAS 339
Cdd:COG0515 318 LAISGSDLKLDDsnfsKELAPNGVSSSPHNSSSLLLS 354
Pkinase pfam00069
Protein kinase domain;
12-236 7.96e-58

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 197.82  E-value: 7.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    12 YRILKSIGRGGMADVYLARDlILDNEEVAIKVLRTNYQTDQIAvARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVME 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKH-RDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    92 YVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFaeTSLTQTNS 171
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL--NSGSSLTS 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22536502   172 MLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVT----IALQHFQKPLPSILAEN 236
Cdd:pfam00069 157 FVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEiyekIIDQDFDSPRPSSISEE 225
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
11-216 9.20e-55

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: 189.27  E-value: 9.20e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDlILDNEEVAIKVLRtNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVM 90
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARH-KLTGEKVAIKIID-KSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTn 170
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKT- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 22536502 171 sMLGSVHYLSPEQARGSK-ATVQSDIYAMGIMLFEMLTGHIPYDGDS 216
Cdd:cd14003 158 -FCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDN 203
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-205 2.70e-54

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: 186.71  E-value: 2.70e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  18 IGRGGMADVYLARDLIlDNEEVAIKVLrtNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVMEYVDGFD 97
Cdd:cd00180   1 LGKGSFGKVYKARDKE-TGKKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  98 LKKYIQDN-APLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAE-TSLTQTNSMLGS 175
Cdd:cd00180  78 LKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSdDSLLKTTGGTTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 22536502 176 VHYLSPEQARGSKATVQSDIYAMGIMLFEM 205
Cdd:cd00180 158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-216 1.35e-50

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: 178.04  E-value: 1.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDlILDNEEVAIKVLRTNYQTDQiAVARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVM 90
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRR-KSDGKLYVLKEIDLSNMSEK-EREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  91 EYVDGFDLKKYI----QDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFaETSL 166
Cdd:cd08215  79 EYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL-ESTT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 22536502 167 TQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDS 216
Cdd:cd08215 158 DLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANN 207
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-249 1.79e-50

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: 177.34  E-value: 1.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  18 IGRGGMADVYLARdliLDNEEVAIKVLRTNYQTDQIAVArFQREARAMAELTHPNIVAIRDIGEEDGQQFLVMEYVDGFD 97
Cdd:cd13999   1 IGSGSFGEVYKGK---WRGTDVAIKKLKVEDDNDELLKE-FRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  98 LKKYIQDNA-PLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQTnSMLGSV 176
Cdd:cd13999  77 LYDLLHKKKiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMT-GVVGTP 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22536502 177 HYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQ-HFQKPLPSILaenKSVPQALENIVIK 249
Cdd:cd13999 156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAvVQKGLRPPIP---PDCPPELSKLIKR 226
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-220 5.31e-50

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: 176.13  E-value: 5.31e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  11 RYRILKSIGRGGMADVYLARDlILDNEEVAIKVL-RTNYQTDQIAvaRFQREARAMAELTHPNIVAIRDIGEEDGQQFLV 89
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVH-KKTGEEYAVKIIdKKKLKSEDEE--MLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  90 MEYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKK---GTVKVTDFGIAVAFAETSL 166
Cdd:cd05117  78 MELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKIIDFGLAKIFEEGEK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 22536502 167 TQTnsMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTI 220
Cdd:cd05117 158 LKT--VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQEL 209
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-212 6.44e-49

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: 173.16  E-value: 6.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  12 YRILKSIGRGGMADVYLARDLiLDNEEVAIKVLRTNYQTDQiavARFQREARAMAELTHPNIVAIRDIGEEDGQQFLVME 91
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHK-KTGQIVAIKKINLESKEKK---ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  92 YVDGFDLKKYIQD-NAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETslTQTN 170
Cdd:cd05122  78 FCSGGSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDG--KTRN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22536502 171 SMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLTGHIPY 212
Cdd:cd05122 156 TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY 197
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
38-258 9.33e-49

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: 185.05  E-value: 9.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     38 EVAIKVLRTNYQTDQIAVARFQREARAMAELTHPNIVAIRDIGE-EDGQQFLVMEYVDGFDLKKYIQDNAPLSNNEVVRI 116
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502    117 MNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGT---VKVTDFGIAV------AFAETSLTQTNSMLGSVHYLSPEQARGS 187
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTllpgvrDADVATLTRTTEVLGTPTYCAPEQLRGE 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22536502    188 KATVQSDIYAMGIMLFEMLTGHIPYDGDSAVTIALQHFQkPLPSilaenkSVPQALE-----NIVIKATAKKLTDR 258
Cdd:TIGR03903  165 PVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLS-PVDV------SLPPWIAghplgQVLRKALNKDPRQR 233
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
10-216 2.13e-46

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983  Cd Length: 255  Bit Score: 165.89  E-value: 2.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  10 GRYRILKSIGRGGMADVYLARDLIlDNEEVAIKVL-RTNYQTDQIAvARFQREARAMAELTHPNIVAIRDIGEEDGQQFL 88
Cdd:cd14081   1 GPYRLGKTLGKGQTGLVKLAKHCV-TGQKVAIKIVnKEKLSKESVL-MKVEREIAIMKLIEHPNVLKLYDVYENKKYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502  89 VMEYVDGFDLKKYIQDNAPLSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAvafaetSLTQ 168
Cdd:cd14081  79 VLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA------SLQP 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 22536502 169 TNSML----GSVHYLSPE-----QARGSKAtvqsDIYAMGIMLFEMLTGHIPYDGDS 216
Cdd:cd14081 153 EGSLLetscGSPHYACPEvikgeKYDGRKA----DIWSCGVILYALLVGALPFDDDN 205
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
13-221 7.14e-45

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


Pssm-ID: 197581  Cd Length: 257  Bit Score: 161.54  E-value: 7.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     13 RILKSIGRGGMADVYLAR-DLILDN--EEVAIKVLRTNYQTDQIAvaRFQREARAMAELTHPNIVAIRDIGEEDGQQFLV 89
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKkkVEVAVKTLKEDASEQQIE--EFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22536502     90 MEYVDGFDLKKYIQDNAP-LSNNEVVRIMNEVLSAMSLAHQKGIVHRDLKPQNILLTKKGTVKVTDFGIAVAFAETSLTQ 168
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYR 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 22536502    169 TNSMLGSVHYLSPEQARGSKATVQSDIYAMGIMLFEMLT-GHIPYDGDSAVTIA 221