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Conserved domains on  [gi|21223194|ref|NP_628973|]
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Ser/Thr protein kinase [Streptomyces coelicolor A3(2)]

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
18-302 3.28e-35

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14014:

Pssm-ID: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 131.55  E-value: 3.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  18 PWEVREPVASGAFATVYEAVrdasagpDRTLDdgeqpRRAALKFLPTGTRTPRQLhhlRDLAEREVQLlrrlrsprlirm 97
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR-------DTLLG-----RPVAIKVLRPELAEDEEF---RERFLREARA------------ 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  98 ydTLTVDDP------DHPELDGATVLVLERAEG-SLDAVLArtpapESGP-------ALLAQICEGLHQLHRAGWVHGDL 163
Cdd:cd14014  54 --LARLSHPnivrvyDVGEDDGRPYIVMEYVEGgSLADLLR-----ERGPlpprealRILAQIADALAAAHRAGIVHRDI 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 164 KPANVLLMADGSARLADFNMAAELEGTHAYTPAFA--TPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFP 241
Cdd:cd14014 127 KPANILLTEDGRVKLTDFGIARALGDSGLTQTGSVlgTPAYMAPEQA------RGGPVDPRSDIYSLGVVLYELLTGRPP 200
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223194 242 LPGGTSEArSDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTTDTATLLRRVEE 302
Cdd:cd14014 201 FDGDSPAA-VLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
389-446 2.67e-13

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 279773  Cd Length: 57  Bit Score: 64.83  E-value: 2.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 21223194   389 GSQVRELQCLLRYLHGItaVGEVDGDFGPMTQGAVVTFQERAGLDADGIVGPATWRAL 446
Cdd:pfam01471   2 GEDVKELQRYLNRLGYY--PGPVDGVFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Pkinase pfam00069
Protein kinase domain;
19-291 1.05e-30

Protein kinase domain;


:

Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 118.47  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    19 WEVREPVASGAFATVYEAVRdasagpdrtLDDGEQprrAALKFLPTGTRTPRQLHHLRdlaeREVQLLRRLRSPRLIRMY 98
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKH---------RDTGKI---VAVKKIKKEKIKKKKDKNVL----REIKILKKLNHPNIVRLY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    99 DTLTvdDPDHpeldgaTVLVLERAE-GSLDAVL-ARTPAPES-GPALLAQICEGLHQLHRAGWVHGDLKPANVLLMADGS 175
Cdd:pfam00069  65 DVFE--DKDH------LYLVLEYVEgGSLFDLLsEKGAFSEReAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194   176 ARLADFNMAAELEGTHAYTPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLPGGTSEARSDAAM 255
Cdd:pfam00069 137 LKITDFGLAKQLSSGSKLTTFVGTPWYMAPEVL------RGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDTLYELII 210
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 21223194   256 RytRGREELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:pfam00069 211 D--QLDLSSPRPSSISEEAKDLLKKLLKKDPSKRLT 244
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
18-302 3.28e-35

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: 131.55  E-value: 3.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  18 PWEVREPVASGAFATVYEAVrdasagpDRTLDdgeqpRRAALKFLPTGTRTPRQLhhlRDLAEREVQLlrrlrsprlirm 97
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR-------DTLLG-----RPVAIKVLRPELAEDEEF---RERFLREARA------------ 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  98 ydTLTVDDP------DHPELDGATVLVLERAEG-SLDAVLArtpapESGP-------ALLAQICEGLHQLHRAGWVHGDL 163
Cdd:cd14014  54 --LARLSHPnivrvyDVGEDDGRPYIVMEYVEGgSLADLLR-----ERGPlpprealRILAQIADALAAAHRAGIVHRDI 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 164 KPANVLLMADGSARLADFNMAAELEGTHAYTPAFA--TPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFP 241
Cdd:cd14014 127 KPANILLTEDGRVKLTDFGIARALGDSGLTQTGSVlgTPAYMAPEQA------RGGPVDPRSDIYSLGVVLYELLTGRPP 200
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223194 242 LPGGTSEArSDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTTDTATLLRRVEE 302
Cdd:cd14014 201 FDGDSPAA-VLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
389-446 2.67e-13

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 279773  Cd Length: 57  Bit Score: 64.83  E-value: 2.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 21223194   389 GSQVRELQCLLRYLHGItaVGEVDGDFGPMTQGAVVTFQERAGLDADGIVGPATWRAL 446
Cdd:pfam01471   2 GEDVKELQRYLNRLGYY--PGPVDGVFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
117-176 8.96e-06

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 283861  Cd Length: 207  Bit Score: 45.06  E-value: 8.96e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223194   117 LVLERAEG--SLDAVLAR--TPAPESGPALLAQICEGLHQLHRAGWVHGDLKPANVLLMADGSA 176
Cdd:pfam06293  94 LLTERLEGaqDLADWLADwaVPSGELRRALWEAVGRLIAQMHRAGVNHGDLYAHHILLQQEGDE 157
PRK12274 PRK12274
serine/threonine protein kinase; Provisional
106-184 6.67e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 237032  Cd Length: 218  Bit Score: 39.89  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  106 PDHPELDGATVLVLERAEGSLDAVLARtpAPESGPALLAQICEGLHQLHRAGWVHGDL-KPANVLLMADGSARLADFNMA 184
Cdd:PRK12274  62 PRTPRLLHWDGRHLDRSYLAGAAMYQR--PPRGDLAYFRAARRLLQQLHRCGVAHNDLaKEANWLVQEDGSPAVIDFQLA 139
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
115-184 1.37e-03

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 38.73  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194   115 TVLVLERAEGsldaVLARTPAPESGPALLAQICEGLHQLHRAGWVHGDLKPANVLLmADGSARLADFNMA 184
Cdd:TIGR03724  72 KTIVMEYIEG----KPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIV-RDDKVYLIDFGLG 136
Pkinase pfam00069
Protein kinase domain;
19-291 1.05e-30

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 118.47  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    19 WEVREPVASGAFATVYEAVRdasagpdrtLDDGEQprrAALKFLPTGTRTPRQLHHLRdlaeREVQLLRRLRSPRLIRMY 98
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKH---------RDTGKI---VAVKKIKKEKIKKKKDKNVL----REIKILKKLNHPNIVRLY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    99 DTLTvdDPDHpeldgaTVLVLERAE-GSLDAVL-ARTPAPES-GPALLAQICEGLHQLHRAGWVHGDLKPANVLLMADGS 175
Cdd:pfam00069  65 DVFE--DKDH------LYLVLEYVEgGSLFDLLsEKGAFSEReAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194   176 ARLADFNMAAELEGTHAYTPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLPGGTSEARSDAAM 255
Cdd:pfam00069 137 LKITDFGLAKQLSSGSKLTTFVGTPWYMAPEVL------RGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDTLYELII 210
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 21223194   256 RytRGREELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:pfam00069 211 D--QLDLSSPRPSSISEEAKDLLKKLLKKDPSKRLT 244
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
19-291 9.66e-30

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 115.70  E-value: 9.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194     19 WEVREPVASGAFATVYEAVRdasagpdrtLDDGeqpRRAALKFLPtgtrtPRQLHHLRDLAEREVQllrrlrsprlirMY 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD---------KKTG---KLVAIKVIK-----KKKIKKDRERILREIK------------IL 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194     99 DTLtvddpDHP---------ELDGATVLVLERAE-GSLDAVLARTPA-PESGPA-LLAQICEGLHQLHRAGWVHGDLKPA 166
Cdd:smart00220  52 KKL-----KHPnivrlydvfEDEDKLYLVMEYCEgGDLFDLLKKRGRlSEDEARfYLRQILSALEYLHSKGIVHRDLKPE 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    167 NVLLMADGSARLADFNMAAELEGTHAYTPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLPGGT 246
Cdd:smart00220 127 NILLDEDGHVKLADFGLARQLDPGEKLTTFVGTPEYMAPEVL------LGKGYGKAVDIWSLGVILYELLTGKPPFPGDD 200
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 21223194    247 SEarsDAAMRYTRGR--EELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:smart00220 201 QL---LELFKKIGKPkpPFPPPEWDISPEAKDLIRKLLVKDPEKRLT 244
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-298 3.70e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 93.65  E-value: 3.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  19 WEVREPVASGAFATVYEAVRdasagpdrtlddgeqPRRAALKFLPTGTRTPRQLHhlrDLAEREVQLLRR-LRSPRLIRM 97
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---------------RKLVALKVLAKKLESKSKEV---ERFLREIQILASlNHPPNIVKL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  98 YDTLTVDDPDhpeldgatVLVLERAEG-SLDAVLARTPAPESGP-----ALLAQICEGLHQLHRAGWVHGDLKPANVLLM 171
Cdd:COG0515  64 YDFFQDEGSL--------YLVMEYVDGgSLEDLLKKIGRKGPLSesealFILAQILSALEYLHSKGIIHRDIKPENILLD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 172 ADGS-ARLADFNMAAEL-------EGTHAYTPAFATPDYTPPELLWpevDERGTRIRPSADVWAFGVLAHVVLTGAFPLP 243
Cdd:COG0515 136 RDGRvVKLIDFGLAKLLpdpgstsSIPALPSTSVGTPGYMAPEVLL---GLSLAYASSSSDIWSLGITLYELLTGLPPFE 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21223194 244 GGTSEARSDAAMRYTR--------GREELRLSPALPDTWRDILRDCLAPTHAERTTDTATLLR 298
Cdd:COG0515 213 GEKNSSATSQTLKIILelptpslaSPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSH 275
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
382-446 2.72e-12

spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]


Pssm-ID: 213747 [Multi-domain]  Cd Length: 200  Bit Score: 64.70  E-value: 2.72e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21223194   382 TIARGDGGSQVRELQCLLRYLHGITavGEVDGDFGPMTQGAVVTFQERAGLDADGIVGPATWRAL 446
Cdd:TIGR02869   5 TYQRGATGSDVIEIQRRLKYWGYYN--GKVDGVFGWGTYWAVRNFQSKNGLTVDGIVGPKTKAAL 67
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
386-447 1.32e-11

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225943 [Multi-domain]  Cd Length: 185  Bit Score: 62.35  E-value: 1.32e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21223194 386 GDGGSQVRELQCLLRYLHGiTAVGEVDGDFGPMTQGAVVTFQERAGLDADGIVGPATWRALR 447
Cdd:COG3409 124 GLGGGDVATLQQPLPLLGY-RSGIRVDGIFGPQTEAAVKAFQRQYGLTVDGIVGPQTWAALR 184
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
117-250 2.48e-10

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 60.16  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  117 LVLERAEGSLDAVL-ARTPAPESG-PALLAQICEGLHQLHRAGWVHGDLKPANVLLMADGSARLADFNMA---------- 184
Cdd:PTZ00024  97 LVMDIMASDLKKVVdRKIRLTESQvKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLArrygyppysd 176
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223194  185 -----AELEGTHAYTPAFATPDYTPPELLWPevderGTRIRPSADVWAFGVLAHVVLTGAfPLPGGTSEAR 250
Cdd:PTZ00024 177 tlskdETMQRREEMTSKVVTLWYRAPELLMG-----AEKYHFAVDMWSVGCIFAELLTGK-PLFPGENEID 241
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
112-246 8.62e-09

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: 56.39  E-value: 8.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    112 DGATVLVLERAEG-SLDAVLART---PAPESGpALLAQICEGLHQLHRAGWVHGDLKPANVLLMADG---SARLADFNMA 184
Cdd:TIGR03903   51 PGLLFAVFEYVPGrTLREVLAADgalPAGETG-RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIG 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194    185 AELEGTHAY--------TPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLPGGT 246
Cdd:TIGR03903  130 TLLPGVRDAdvatltrtTEVLGTPTYCAPEQL------RGEPVTPNSDLYAWGLIFLECLTGQRVVQGAS 193
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
18-302 3.28e-35

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: 131.55  E-value: 3.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  18 PWEVREPVASGAFATVYEAVrdasagpDRTLDdgeqpRRAALKFLPTGTRTPRQLhhlRDLAEREVQLlrrlrsprlirm 97
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR-------DTLLG-----RPVAIKVLRPELAEDEEF---RERFLREARA------------ 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  98 ydTLTVDDP------DHPELDGATVLVLERAEG-SLDAVLArtpapESGP-------ALLAQICEGLHQLHRAGWVHGDL 163
Cdd:cd14014  54 --LARLSHPnivrvyDVGEDDGRPYIVMEYVEGgSLADLLR-----ERGPlpprealRILAQIADALAAAHRAGIVHRDI 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 164 KPANVLLMADGSARLADFNMAAELEGTHAYTPAFA--TPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFP 241
Cdd:cd14014 127 KPANILLTEDGRVKLTDFGIARALGDSGLTQTGSVlgTPAYMAPEQA------RGGPVDPRSDIYSLGVVLYELLTGRPP 200
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223194 242 LPGGTSEArSDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTTDTATLLRRVEE 302
Cdd:cd14014 201 FDGDSPAA-VLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
27-231 1.34e-23

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: 97.73  E-value: 1.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  27 SGAFATVYEAVrdasagpdrtldDGEQPRRAALKFLPtgtrtPRQLHHLRDLAEREVQllrrlrsprlirMYDTLtvddp 106
Cdd:cd00180   3 KGSFGKVYKAR------------DKETGKKVAVKVIP-----KEKLKKLLEELLREIE------------ILKKL----- 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 107 DHP---------ELDGATVLVLERAE-GSLDAVLARTPAPESGPA---LLAQICEGLHQLHRAGWVHGDLKPANVLLMAD 173
Cdd:cd00180  49 NHPnivklydvfETENFLYLVMEYCEgGSLKDLLKENKGPLSEEEalsILRQLLSALEYLHSNGIIHRDLKPENILLDSD 128
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223194 174 GSARLADFNMAAELEGTH---AYTPAFATPDYTPPELLWPEVDErgtrirPSADVWAFGVL 231
Cdd:cd00180 129 GTVKLADFGLAKDLDSDDsllKTTGGTTPPYYAPPELLGGRYYG------PKVDIWSLGVI 183
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
19-298 1.56e-21

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 92.58  E-value: 1.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  19 WEVREPVASGAFATVYEAVrdasagpdrTLDDGEqprRAALKFLPTGTRTPRQLHHLrdlaEREVQllrrlrsprlirMY 98
Cdd:cd06606   2 WKKGELLGKGSFGSVYLAL---------NLDTGE---LMAVKEVELSGDSEEELEAL----EREIR------------IL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  99 DTLtvddpDHP--------ELDGATV-LVLERA-EGSLDAVLARTPA-PESGPALLA-QICEGLHQLHRAGWVHGDLKPA 166
Cdd:cd06606  54 SSL-----KHPnivrylgtERTENTLnIFLEYVpGGSLASLLKKFGKlPEPVVRKYTrQILEGLEYLHSNGIVHRDIKGA 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 167 NVLLMADGSARLADFNMAAELEG--THAYTPAFA-TPDYTPPELLwpevdeRGTRIRPSADVWAFGVLahVV--LTGAFP 241
Cdd:cd06606 129 NILVDSDGVVKLADFGCAKRLAEiaTGEGTKSLRgTPYWMAPEVI------RGEGYGRAADIWSLGCT--VIemATGKPP 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21223194 242 LPGGTSEArsDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTTdTATLLR 298
Cdd:cd06606 201 WSELGNPV--AALFKIGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRPT-ADELLQ 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
104-291 1.88e-20

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 89.53  E-value: 1.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 104 DDPDHPELdgatVLVLERAEGSldaVLARTPAPESGPAL--------LAQICEGLHQLHRAGWVHGDLKPANVLLMADGS 175
Cdd:cd14008  74 DDPESDKL----YLVLEYCEGG---PVMELDSGDRVPPLpeetarkyFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 176 ARLADFNMAAELEGTHAY------TPAFatpdyTPPELLWPevdERGTRIRPSADVWAFGVLAHVVLTGAFPLpGGTSEa 249
Cdd:cd14008 147 VKISDFGVSEMFEDGNDTlqktagTPAF-----LAPELCDG---DSKTYSGKAADIWALGVTLYCLVFGRLPF-NGDNI- 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21223194 250 rSDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:cd14008 217 -LELYEAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRIT 257
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
18-291 1.47e-19

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: 86.80  E-value: 1.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  18 PWEVREPVASGAFATVYEAvrdasagpdRTLDDGEQprrAALKFLPTGTRTPRQLHHLRdlaeREVQLLRRLrsprlirm 97
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLA---------RHKLTGEK---VAIKIIDKSKLKEEIEEKIK----REIEIMKLL-------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  98 ydtltvddpDHP---------ELDGATVLVLERAEG--SLDAVLARTPAPES-GPALLAQICEGLHQLHRAGWVHGDLKP 165
Cdd:cd14003  57 ---------NHPniiklyeviETENKIYLVMEYASGgeLFDYIVNNGRLSEDeARRFFQQLISAVDYCHSNGIVHRDLKL 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 166 ANVLLMADGSARLADFNMAAE-LEGTHAYTPAfATPDYTPPELLwpevdERGTRIRPSADVWAFGVLAHVVLTGAFPLpg 244
Cdd:cd14003 128 ENILLDKNGNLKIIDFGLSNEfRGGSLLKTFC-GTPAYAAPEVL-----LGRKYDGPKADVWSLGVILYAMLTGYLPF-- 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21223194 245 gtsEARSDAAMRYTRGREELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:cd14003 200 ---DDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRIT 243
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
19-291 7.24e-19

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: 84.95  E-value: 7.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  19 WEVREPVASGAFATVYEAvRDASAGpdrtlddgeqpRRAALKFLPTgtRTPRQLHHLRdlaeREVQLLRRLRSPRLIRMY 98
Cdd:cd05122   2 FEILEKIGKGGFGVVYKA-RHKKTG-----------QIVAIKKINL--ESKEKKESIL----NEIAILKKCKHPNIVKYY 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  99 DTLTVDDpdhpELdgatVLVLERAE-GSLDAVLARTPAPESgPALLAQIC----EGLHQLHRAGWVHGDLKPANVLLMAD 173
Cdd:cd05122  64 GSYLKKD----EL----WIVMEFCSgGSLKDLLKNTNKTLT-EQQIAYVCkevlKGLEYLHSHGIIHRDIKAANILLTSD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 174 GSARLADFNMAAELEGTHAYTPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLpggtSEARSDA 253
Cdd:cd05122 135 GEVKLIDFGLSAQLSDGKTRNTFVGTPYWMAPEVI------QGKPYGFKADIWSLGITAIEMAEGKPPY----SELPPMK 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21223194 254 AMRYTR--GREELRLSPALPDTWRDILRDCLAPTHAERTT 291
Cdd:cd05122 205 ALFLIAtnGPPGLRNPKKWSKEFKDFLKKCLQKDPEKRPT 244
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
144-241 5.64e-18

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 82.18  E-value: 5.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 144 AQICEGLHQLHRAGWVHGDLKPANVLLMADGSARLADFNMAAELEGTHAYTPAFA-TPDYTPPELLwpevdeRGTRIRPS 222
Cdd:cd05123 100 AEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCgTPEYLAPEVL------LGKGYGKA 173
                        90
                ....*....|....*....
gi 21223194 223 ADVWAFGVLAHVVLTGAFP 241
Cdd:cd05123 174 VDWWSLGVLLYEMLTGKPP 192
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-291 9.39e-18

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 81.51  E-value: 9.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  20 EVREPVASGAFATVYEAvRDASAGpdrtlddgeqpRRAALKFLPTGTRTPRQlhhlrdlAEREVQllrrlrsprlirMYD 99
Cdd:cd05118   2 EVLRKIGEGAFGTVWLA-RDKVTG-----------EKVAIKKIKNDFRHPKA-------ALREIK------------LLK 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 100 TLTvDDPDHPEL-----------DGATVLVLERAEGSLDAVLARTPAPESGPAL---LAQICEGLHQLHRAGWVHGDLKP 165
Cdd:cd05118  51 HLN-DVEGHPNIvklldvfehrgGNHLCLVFELMGMNLYELIKDYPRGLPLDLIksyLYQLLQALDFLHSNGIIHRDLKP 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 166 ANVLLMADGSA-RLADFNMaAELEGTHAYTPAFATPDYTPPELLWpevdeRGTRIRPSADVWAFGVLAHVVLTGaFPLPG 244
Cdd:cd05118 130 ENILINLELGQlKLADFGL-ARSFTSPPYTPYVATRWYRAPEVLL-----GAKPYGSSIDIWSLGCILAELLTG-RPLFP 202
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21223194 245 GTSEARSDAAMRYTRGREELrlspalpdtwRDILRDCLAPTHAERTT 291
Cdd:cd05118 203 GDSEVDQLAKIVRLLGTPEA----------LDLLSKMLKYDPAKRIT 239
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
143-275 1.38e-17

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 81.22  E-value: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 143 LAQICEGLHQLHRAGWVHGDLKPANVLLMaDGSAR---LADFNMAAELeGTHAYTPAFATPdYTPPELLwPEVDERGTRI 219
Cdd:cd13987  97 AAQLASALDFMHSKNLVHRDIKPENVLLF-DKDCRrvkLCDFGLTRRV-GSTVKRVSGTIP-YTAPEVC-EAKKNEGFVV 172
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21223194 220 RPSADVWAFGVLAHVVLTGAFPLpggtsEARSDAAMRYTR-GREELRLSPALPDTWR 275
Cdd:cd13987 173 DPSIDVWAFGVLLFCCLTGNFPW-----EKADSDDQFYEEfVRWQKRKNTAVPSQWR 224
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
145-291 2.14e-17

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 80.51  E-value: 2.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 145 QICEGLHQLHRAGWVHGDLKPANVLLMADGSARLADFNMAAELEGTHAYTpAFATPDYTPPElLWpevdeRGTRIRPSAD 224
Cdd:cd08530 111 QMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKT-QIGTPLYAAPE-VW-----KGRPYDYKSD 183
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21223194 225 VWAFGVLAHVVLTGAFPLpggtsEARSDAAMRYT--RGReelrlSPALPDTWRD----ILRDCLAPTHAERTT 291
Cdd:cd08530 184 IWSLGCLLYEMATFRPPF-----EARTMQELRYKvcRGK-----FPPIPPVYSQdlqqIIRSLLQVNPKKRPS 246
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
26-244 6.33e-17

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 78.85  E-value: 6.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  26 ASGAFATVYEAVRDASagpDRTLddgeqprraALKFLPTGTRTprqlhhlRDLAEREVQLLRRLRSPRLIRMYDTLtvDD 105
Cdd:cd14006   2 GRGRFGVVKRCIEKAT---GREF---------AAKFIPKRDKK-------KEAVLREISILNQLQHPRIIQLHEAY--ES 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 106 PdhPELdgatVLVLERAEGS--LDAVLARTPAPESGPA-LLAQICEGLHQLHRAGWVHGDLKPANVLL--MADGSARLAD 180
Cdd:cd14006  61 P--TEL----VLILELCSGGelLDRLAERGSLSEEEVRtYMRQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKIID 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21223194 181 FNMAAELE-GTHAYTPaFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLPG 244
Cdd:cd14006 135 FGLARKLNpGEELKEI-FGTPEFVAPEIV------NGEPVSLATDMWSIGVLTYVLLSGLSPFLG 192
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
116-244 8.36e-17

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 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: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 78.82  E-value: 8.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 116 VLVLERAEGS--LDAVLA-RTPA--PESGPALLAQICEGLHQLHRAGWVHGDLKPANVLLMAD---GSARLADFNMAAEL 187
Cdd:cd14197  85 ILVLEYAAGGeiFNQCVAdREEAfkEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRIL 164
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21223194 188 EGTHAYTPAFATPDYTPPELLWPEvdergtRIRPSADVWAFGVLAHVVLTGAFPLPG 244
Cdd:cd14197 165 KNSEELREIMGTPEYVAPEILSYE------PISTATDMWSIGVLAYVMLTGISPFLG 215
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-248 1.16e-16

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: 78.29  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  19 WEVREPVASGAFATVYEAVRDASagpdrtlddgeqPRRAALKFLPTGTRTPRQLHHLRdlaeREVQllrrlrsprlirmy 98
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKT------------GEEYAVKIIDKKKLKSEDEEMLR----REIE-------------- 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  99 dtlTVDDPDHP---------ELDGATVLVLERAEGS--LDAVLARTPAPESGPA-LLAQICEGLHQLHRAGWVHGDLKPA 166
Cdd:cd05117  52 ---ILKRLDHPnivklyevfEDDKNLYLVMELCTGGelFDRIVKKGSFSEREAAkIMKQILSAVAYLHSQGIVHRDLKPE 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 167 NVLLM---ADGSARLADFNMAAELEGTHAYTPAFATPDYTPPELLwpevdeRGTRIRPSADVWAFGVLAHVVLTGAFPLP 243
Cdd:cd05117 129 NILLAskdPDSPIKIIDFGLAKIFEEGEKLKTVCGTPYYVAPEVL------KGKGYGKKCDIWSLGVILYILLCGYPPFY 202

                ....*
gi 21223194 244 GGTSE 248
Cdd:cd05117 203 GETEQ 207
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
19-249 1.80e-16

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 77.90  E-value: 1.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  19 WEVREPVASGAFATVYEAVrDASAGPDRTLDDGEQPRRAALKFLPTG----TRTPRQLHHlrdlaEREVQLLrrlrsprl 94
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAV-EVETGKMRAIKQIVKRKVAGNDKNLQLfqreINILKSLEH-----PGIVRLI-------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194  95 irmydtltvddpDHPELDGATVLVLERAEGS--LDAVLARTPAPE-SGPALLAQICEGLHQLHRAGWVHGDLKPANVLLM 171
Cdd:cd14098  68 ------------DWYEDDQHIYLVMEYVEGGdlMDFIMAWGAIPEqHARELTKQILEAMAYTHSMGITHRDLKPENILIT 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223194 172 ADGS--ARLADFNMaAELEGTHAYTPAF-ATPDYTPPELLwpevDERGTRIRPS----ADVWAFGVLAHVVLTGAFPLPG 244