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Conserved domains on  [gi|116622381|ref|YP_824537|]
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serine/threonine protein kinase [Candidatus Solibacter usitatus Ellin6076]

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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 ...
9-268 2.45e-70

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: 228.62  E-value: 2.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLI--PNAGDRSTRMTIEAERR-GAAIQqelHdldPRMVEIYEYGDADGY 84
Cdd:cd14014    1 RYRLVRLLGRgGMGEVYRARDTLLGRPVAIKVLrpELAEDEEFRERFLREARaLARLS---H---PNIVRVYDVGEDDGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  85 FFVAMQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRA 164
Cdd:cd14014   75 PYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAH--RAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 165 NCNATDHEF-GSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRL--EVLIRSRRPPRALGPGCPPGL 241
Cdd:cd14014  153 SGLTQTGSVlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVlaKHLQEAPPPPSPLNPDVPPAL 232
                        250       260
                 ....*....|....*....|....*..
gi 116622381 242 RAVVMKALAPDSRQRYPSAVEFHADLQ 268
Cdd:cd14014  233 DAIILRALAKDPEERPQSAAELLAALR 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
10-266 1.33e-49

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.10  E-value: 1.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381    10 YEIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTIEAERRgaaIQQELHDldPRMVEIYEYGDADGYFFVA 88
Cdd:smart00220   1 YEILEKLGEgSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIK---ILKKLKH--PNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381    89 MQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRANCNA 168
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLH--SKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   169 TDhEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRR--LEVLIRSRRPPRALGPGCPPGLRAVVM 246
Cdd:smart00220 154 TT-FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLelFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                          250       260
                   ....*....|....*....|
gi 116622381   247 KALAPDSRQRyPSAVEFHAD 266
Cdd:smart00220 233 KLLVKDPEKR-LTAEEALQH 251
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
9-268 2.45e-70

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: 228.62  E-value: 2.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLI--PNAGDRSTRMTIEAERR-GAAIQqelHdldPRMVEIYEYGDADGY 84
Cdd:cd14014    1 RYRLVRLLGRgGMGEVYRARDTLLGRPVAIKVLrpELAEDEEFRERFLREARaLARLS---H---PNIVRVYDVGEDDGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  85 FFVAMQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRA 164
Cdd:cd14014   75 PYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAH--RAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 165 NCNATDHEF-GSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRL--EVLIRSRRPPRALGPGCPPGL 241
Cdd:cd14014  153 SGLTQTGSVlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVlaKHLQEAPPPPSPLNPDVPPAL 232
                        250       260
                 ....*....|....*....|....*..
gi 116622381 242 RAVVMKALAPDSRQRYPSAVEFHADLQ 268
Cdd:cd14014  233 DAIILRALAKDPEERPQSAAELLAALR 259
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
56-161 2.53e-06

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 47.28  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  56 RRGAAIQQELHDLDPRMVEIYEYgDADGYFFVaMQYVEGRTVADLLAlERVIDPCRaavialEICEQLMKFHgwESGVVH 135
Cdd:COG3642   47 RREARILAKAREAGVPVPIVYDV-DPDNGLIV-MEYIEGELLKDALE-EARPDLLR------EVGRLVGKLH--KAGIVH 115
                         90       100
                 ....*....|....*....|....*.
gi 116622381 136 GDIKPSNIHLGcSETVRLLDFGIAKT 161
Cdd:COG3642  116 GDLTTSNIILS-GGRIYFIDFGLGEF 140
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
89-160 4.61e-06

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


Pssm-ID: 234331  Cd Length: 199  Bit Score: 46.44  E-value: 4.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116622381   89 MQYVEGRTVADLLAlERVIDPCRaavialEICEQLMKFHgwESGVVHGDIKPSNIHLGcSETVRLLDFGIAK 160
Cdd:TIGR03724  76 MEYIEGKPLKDVIE-EGNDELLR------EIGRLVGKLH--KAGIVHGDLTTSNIIVR-DDKLYLIDFGLGK 137
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
89-160 2.08e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 44.51  E-value: 2.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116622381  89 MQYVEGRTVADLLalERVIDPCRAavIALEICEQLMKFHgwESGVVHGDIKPSNIHLGcSETVRLLDFGIAK 160
Cdd:PRK14879  78 MEYIEGEPLKDLI--NSNGMEELE--LSREIGRLVGKLH--SAGIIHGDLTTSNMILS-GGKIYLIDFGLAE 142
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
173-239 9.95e-04

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 38.92  E-value: 9.95e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116622381   173 FGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAED--TRRLEVLIrSRRPPRALGPGCPP 239
Cdd:smart00750  65 RPDPYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERelSAILEILL-NGMPADDPRDRSNL 132
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
130-210 2.52e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 38.78  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 130 ESGVVHGDIKPSNIHLGCSETVRLLDFGIA-------KTLRANCNATDHEFGSPSYCSPERLTRSEVNPQSDLWALGatl 202
Cdd:PHA02882 144 EHGISHGDIKPENIMVDGNNRGYIIDYGIAshfiihgKHIEYSKEQKDLHRGTLYYAGLDAHNGACVTRRGDLESLG--- 220
                         90
                 ....*....|
gi 116622381 203 YEML--AGVP 210
Cdd:PHA02882 221 YCMLkwAGIK 230
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
10-266 1.33e-49

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.10  E-value: 1.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381    10 YEIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTIEAERRgaaIQQELHDldPRMVEIYEYGDADGYFFVA 88
Cdd:smart00220   1 YEILEKLGEgSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIK---ILKKLKH--PNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381    89 MQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRANCNA 168
Cdd:smart00220  76 MEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLH--SKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   169 TDhEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRR--LEVLIRSRRPPRALGPGCPPGLRAVVM 246
Cdd:smart00220 154 TT-FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLelFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                          250       260
                   ....*....|....*....|
gi 116622381   247 KALAPDSRQRyPSAVEFHAD 266
Cdd:smart00220 233 KLLVKDPEKR-LTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
10-268 4.83e-39

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 146.81  E-value: 4.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  10 YEIIRRLGK-SMTEVYLARDTveeRKVALKLIPNAgDRSTRMTIEAERRGAAIQQELHDlDPRMVEIYEYGDADGYFFVA 88
Cdd:COG0515    2 YRILRKLGEgSFGEVYLARDR---KLVALKVLAKK-LESKSKEVERFLREIQILASLNH-PPNIVKLYDFFQDEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  89 MQYVEGRTVADLLAL---ERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSET-VRLLDFGIAKTLRA 164
Cdd:COG0515   77 MEYVDGGSLEDLLKKigrKGPLSESEALFILAQILSALEYLH--SKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 165 NCNATDHEF------GSPSYCSPERLTRSE---VNPQSDLWALGATLYEMLAGVPPYQAED----TRRLEVLIRSRRPPR 231
Cdd:COG0515  155 PGSTSSIPAlpstsvGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKnssaTSQTLKIILELPTPS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 116622381 232 ALGP-------GCPPGLRAVVMKALAPDSRQRYPSAVEFHADLQ 268
Cdd:COG0515  235 LASPlspsnpeLISKAASDLLKKLLAKDPKNRLSSSSDLSHDLL 278
Pkinase pfam00069
Protein kinase domain;
10-262 1.03e-35

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 133.91  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   10 YEIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRST-RMTIEAErrgAAIQQEL-HdldPRMVEIYEYGDADGYFF 86
Cdd:pfam00069   1 YELLRKLGSgSFGTVYKAKHKGTGKIVAVKILKKRSEKSKkDQTARRE---IRILRRLsH---PNIVRLIDAFEDKDHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   87 VAMQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRANC 166
Cdd:pfam00069  75 LVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLH--SNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  167 NATDHEFGSPSYCSPERL-TRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPRALGP-----GCPPG 240
Cdd:pfam00069 153 SSLTTFVGTPEYMAPEVLlGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDepksdSGSEE 232
                         250       260
                  ....*....|....*....|..
gi 116622381  241 LRAVVMKALAPDSRQRyPSAVE 262
Cdd:pfam00069 233 AKDLIKKCLNKDPSKR-PTAEE 253
pknD PRK13184
serine/threonine-protein kinase; Reviewed
7-294 1.89e-33

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 134.51  E-value: 1.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   7 IGRYEIIRRLGKS-MTEVYLARDTVEERKVALKLIpnagdrsTRMTIEAER------RGAAIQQELhdLDPRMVEIYE-Y 78
Cdd:PRK13184   1 MQRYDIIRLIGKGgMGEVYLAYDPVCSRRVALKKI-------REDLSENPLlkkrflREAKIAADL--IHPGIVPVYSiC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  79 GDADGYFFVaMQYVEGRTVADLLALERVIDPCRAAV-----------IALEICEQLMKFHgwESGVVHGDIKPSNIHLGC 147
Cdd:PRK13184  72 SDGDPVYYT-MPYIEGYTLKSLLKSVWQKESLSKELaektsvgaflsIFHKICATIEYVH--SKGVLHRDLKPDNILLGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 148 SETVRLLDFGIAKT----------LRANCNATDHE--------FGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGV 209
Cdd:PRK13184 149 FGEVVILDWGAAIFkkleeedlldIDVDERNICYSsmtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 210 PPYQAEDTRRLeVLIRSRRPPRALGP--GCPPGLRAVVMKALAPDSRQRYPSAVEFHADLQLFLERKPtraeterrsKWN 287
Cdd:PRK13184 229 FPYRRKKGRKI-SYRDVILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP---------EWT 298

                 ....*..
gi 116622381 288 PAATLEA 294
Cdd:PRK13184 299 VKATLMT 305
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
34-260 1.08e-18

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 89.13  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381    34 KVALKLIPNAGDRSTRMTIEAERRGAAIQQELHdldPRMVEIYEYGDA-DGYFFVAMQYVEGRTVADLLALERVIDPCRA 112
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYH---PNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   113 AVIALEICEQLMKFHgwESGVVHGDIKPSNIHL---GCSETVRLLDFGIAKTL-------RANCNATDHEFGSPSYCSPE 182
Cdd:TIGR03903   82 GRLMLQVLDALACAH--NQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLpgvrdadVATLTRTTEVLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   183 RLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRrlEVLIRSRRPPRALGPGCPPGLR--AVVMKALAPDSRQRYPSA 260
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVA--EILYQQLSPVDVSLPPWIAGHPlgQVLRKALNKDPRQRAASA 237
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
130-212 1.44e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 64.45  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 130 ESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLrancnaTDHEF---GSPSYCSPERLTRSEVNPQSDLWALGATLYEML 206
Cdd:PTZ00263 136 SKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV------PDRTFtlcGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFI 209

                 ....*.
gi 116622381 207 AGVPPY 212
Cdd:PTZ00263 210 AGYPPF 215
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
11-212 3.45e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 60.61  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  11 EIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTIEAErrgAAIqqeLHDLD-PRMVEIYEYGDADGYFFVA 88
Cdd:PLN00034  77 ERVNRIGSgAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICRE---IEI---LRDVNhPNVVKCHDMFDHNGEIQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  89 MQY-----VEGRTVADLLALervidpcraAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLR 163
Cdd:PLN00034 151 LEFmdggsLEGTHIADEQFL---------ADVARQILSGIAYLH--RRHIVHRDIKPSNLLINSAKNVKIADFGVSRILA 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116622381 164 ANCNATDHEFGSPSYCSPERLTrSEVNP------QSDLWALGATLYEMLAGVPPY 212
Cdd:PLN00034 220 QTMDPCNSSVGTIAYMSPERIN-TDLNHgaydgyAGDIWSLGVSILEFYLGRFPF 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
89-222 1.27e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 54.86  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  89 MQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHGWEsgVVHGDIKPSNI-HLGCSETVRLLDFGIAKTLrancn 167
Cdd:PHA03390  88 MDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHN--IIHNDIKLENVlYDRAKDRIYLCDYGLCKII----- 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116622381 168 atdhefGSPS-------YCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEV 222
Cdd:PHA03390 161 ------GTPScydgtldYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDL 216
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
9-268 2.45e-70

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: 228.62  E-value: 2.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLI--PNAGDRSTRMTIEAERR-GAAIQqelHdldPRMVEIYEYGDADGY 84
Cdd:cd14014    1 RYRLVRLLGRgGMGEVYRARDTLLGRPVAIKVLrpELAEDEEFRERFLREARaLARLS---H---PNIVRVYDVGEDDGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  85 FFVAMQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRA 164
Cdd:cd14014   75 PYIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAH--RAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 165 NCNATDHEF-GSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRL--EVLIRSRRPPRALGPGCPPGL 241
Cdd:cd14014  153 SGLTQTGSVlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVlaKHLQEAPPPPSPLNPDVPPAL 232
                        250       260
                 ....*....|....*....|....*..
gi 116622381 242 RAVVMKALAPDSRQRYPSAVEFHADLQ 268
Cdd:cd14014  233 DAIILRALAKDPEERPQSAAELLAALR 259
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
10-260 7.14e-35

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: 131.56  E-value: 7.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  10 YEIIRRLGK-SMTEVYLARDTVEERKVALKLIPnagdrstrmtIEAERRGAAIQQE---LHDLD-PRMVEIYEYGDADGY 84
Cdd:cd05122    2 FEILEKIGKgGFGVVYKARHKKTGQIVAIKKIN----------LESKEKKESILNEiaiLKKCKhPNIVKYYGSYLKKDE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  85 FFVAMQYVEGRTVADLL-ALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLr 163
Cdd:cd05122   72 LWIVMEFCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLH--SHGIIHRDIKAANILLTSDGEVKLIDFGLSAQL- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 164 ANCNATDHEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPRALGP-GCPPGLR 242
Cdd:cd05122  149 SDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPkKWSKEFK 228
                        250
                 ....*....|....*...
gi 116622381 243 AVVMKALAPDSRQRyPSA 260
Cdd:cd05122  229 DFLKKCLQKDPEKR-PTA 245
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
16-205 2.35e-34

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: 128.93  E-value: 2.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  16 LGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTIEAErrgAAIQQELHDldPRMVEIYEYGDADGYFFVAMQYVEG 94
Cdd:cd00180    1 LGKgSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLRE---IEILKKLNH--PNIVKLYDVFETENFLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  95 RTVADLLA-LERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRANCNATDHEF 173
Cdd:cd00180   76 GSLKDLLKeNKGPLSEEEALSILRQLLSALEYLH--SNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTG 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 116622381 174 GSPS--YCSPERLTRSEVNPQSDLWALGATLYEM 205
Cdd:cd00180  154 GTTPpyYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
9-257 3.47e-30

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: 118.39  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLIpnagDRSTRMTIEAERrgaaIQQELHDLD----PRMVEIYEYGDADG 83
Cdd:cd14003    1 NYELGKTLGEgSFGKVKLARHKLTGEKVAIKII----DKSKLKEEIEEK----IKREIEIMKllnhPNIIKLYEVIETEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  84 YFFVAMQYVEGRTVADLLALERVIDPCRAA------VIALEICEQLmkfhgwesGVVHGDIKPSNIHLGCSETVRLLDFG 157
Cdd:cd14003   73 KIYLVMEYASGGELFDYIVNNGRLSEDEARrffqqlISAVDYCHSN--------GIVHRDLKLENILLDKNGNLKIIDFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 158 IAKTLRANCNAtdHEF-GSPSYCSPERLTRSEVN-PQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRS---RRPPRA 232
Cdd:cd14003  145 LSNEFRGGSLL--KTFcGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKgkyPIPSHL 222
                        250       260
                 ....*....|....*....|....*
gi 116622381 233 lgpgcPPGLRAVVMKALAPDSRQRY 257
Cdd:cd14003  223 -----SPDARDLIRRMLVVDPSKRI 242
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
9-262 1.05e-29

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 117.18  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLIPnagdrSTRMTiEAERRGAaiQQE---LHDLD-PRMVEIYEYGDADG 83
Cdd:cd08215    1 KYEKIRVIGKgSFGSAYLVRRKSDGKLYVLKEID-----LSNMS-EKEREEA--LNEvklLSKLKhPNIVKYYESFEENG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  84 YFFVAMQYVEGRTVADLLAL----------ERVIDpcraavIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRL 153
Cdd:cd08215   73 KLCIVMEYADGGDLAQKIKKqkkkgqpfpeEQILD------WFVQICLALKYLH--SRKILHRDLKTQNIFLTKDGVVKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 154 LDFGIAKTLRANCNATDHEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPrAL 233
Cdd:cd08215  145 GDFGISKVLESTTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYP-PI 223
                        250       260
                 ....*....|....*....|....*....
gi 116622381 234 GPGCPPGLRAVVMKALAPDSRQRyPSAVE 262
Cdd:cd08215  224 PSQYSSELRDLVNSMLQKDPEKR-PSANE 251
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
9-226 9.54e-29

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: 114.50  E-value: 9.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTieaerrgaAIQQE---LHDLD-PRMVEIYEYGDADG 83
Cdd:cd05117    1 KYELGKVLGRgSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEE--------MLRREieiLKRLDhPNIVKLYEVFEDDK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  84 YFFVAMQYVEGrtvADLLalERVIDPCR-----AAVIALEICEQLMKFHgwESGVVHGDIKPSNIhLGCSE----TVRLL 154
Cdd:cd05117   73 NLYLVMELCTG---GELF--DRIVKKGSfsereAAKIMKQILSAVAYLH--SQGIVHRDLKPENI-LLASKdpdsPIKII 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116622381 155 DFGIAKTLRANCNATDhEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRS 226
Cdd:cd05117  145 DFGLAKIFEEGEKLKT-VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK 215
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
9-262 4.11e-27

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-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: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 110.41  E-value: 4.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381   9 RYEIIRRLGK-SMTEVYLARDTVEERKVALKLIpnagDRStrmtiEAERRGAAIQQE---LHDLDPRMVEIYeYGDA-DG 83
Cdd:cd06609    2 LFTLLERIGKgSFGEVYKGIDKRTNQVVAIKVI----DLE-----EAEDEIEDIQQEiqfLSQCDSPYITKY-YGSFlKG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  84 Y-FFVAMQYVEGRTVADLLaLERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTL 162
Cdd:cd06609   72 SkLWIIMEYCGGGSVLDLL-KPGPLDETYIAFILREVLLGLEYLH--SEGKIHRDIKAANILLSEEGDVKLADFGVSGQL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 163 RANCNATDHEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPRALGPGCPPGLR 242
Cdd:cd06609  149 TSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNKFSKPFK 228
                        250       260
                 ....*....|....*....|
gi 116622381 243 AVVMKALAPDSRQRyPSAVE 262
Cdd:cd06609  229 DFVELCLNKDPKER-PSAKE 247
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
10-262 4.40e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK 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: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 109.61  E-value: 4.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  10 YEIIRRLGK-SMTEVYLARDTVEERKVALKlipnagdrstRMTIEAERRGAAIQ-----QELHDldPRMVEIYEYGDADG 83
Cdd:cd06614    2 YKNLEKIGEgASGEVYKATDRATGKEVAIK----------KMRLRKQNKELIINeilimKECKH--PNIVDYYDSYLVGD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  84 YFFVAMQYVEGRTVADLLALERVI-DPCRAAVIALEICEQLMKFHGweSGVVHGDIKPSNIHLGCSETVRLLDFGIAKTL 162
Cdd:cd06614   70 ELWVVMEYMDGGSLTDIITQNPVRmNESQIAYVCREVLQGLEYLHS--QNVIHRDIKSDNILLSKDGSVKLADFGFAAQL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 163 RANCNATDHEFGSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPRALGP-GCPPGL 241
Cdd:cd06614  148 TKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPeKWSPEF 227
                        250       260
                 ....*....|....*....|.
gi 116622381 242 RAVVMKALAPDSRQRyPSAVE 262
Cdd:cd06614  228 KDFLNKCLVKDPEKR-PSAEE 247
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
11-262 1.29e-26

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 108.45  E-value: 1.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  11 EIIRRLGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRMTIEAERRgaaiqqELHDLD-PRMVEIYEYGDADGYFFVA 88
Cdd:cd06623    4 ERVKVLGQgSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELK------TLRSCEsPYVVKCYGAFYKEGEISIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  89 MQYVEGRTVADLLALERVIDPCRAAVIALEICEQLMKFHGwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTL---RAN 165
Cdd:cd06623   78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHT-KRHIIHRDIKPSNLLINSKGEVKIADFGISKVLentLDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 166 CNatdhEF-GSPSYCSPERLtRSEVNP-QSDLWALGATLYEMLAGVPPYQAEDTRRLEVLIR---SRRPPRALGPGCPPG 240
Cdd:cd06623  157 CN----TFvGTVTYMSPERI-QGESYSyAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQaicDGPPPSLPAEEFSPE 231
                        250       260
                 ....*....|....*....|..
gi 116622381 241 LRAVVMKALAPDSRQRyPSAVE 262
Cdd:cd06623  232 FRDFISACLQKDPKKR-PSAAE 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
23-256 1.78e-26

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: 108.41  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  23 VYLARDTVEERKVALK------LIPNAGDRSTRMTIEAE----RRGAAIQQELHDldPRMVEIYE--YGDADGYFFVAMQ 90
Cdd:cd14008    9 VKLALDTETGQLYAIKifnksrLRKRREGKNDRGKIKNAlddvRREIAIMKKLDH--PNIVRLYEviDDPESDKLYLVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  91 YVEGRTVADLLALERV--IDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLRANCNA 168
Cdd:cd14008   87 YCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLH--ENGIVHRDIKPENLLLTADGTVKISDFGVSEMFEDGNDT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381 169 TDHEFGSPSYCSPErLTRSEVNPQS----DLWALGATLYEMLAGVPPYQAEDTRRLEVLIRSRRPPRALGPGCPPGLRAV 244
Cdd:cd14008  165 LQKTAGTPAFLAPE-LCDGDSKTYSgkaaDIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPELSPELKDL 243
                        250
                 ....*....|..
gi 116622381 245 VMKALAPDSRQR 256
Cdd:cd14008  244 LRRMLEKDPEKR 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
16-217 9.37e-25

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: 102.98  E-value: 9.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  16 LGK-SMTEVYLARDTVEERKVALKLIPNAGDRSTRM--TIEAERRgaaIQQELHDldPRMVEIYEYGDADGYFFVAMQYV 92
Cdd:cd05123    1 LGKgSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEveHTLNERN---ILERVNH--PFIVKLHYAFQTEEKLYLVLDYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116622381  93 EGRTVADLLALERVIDPCRAAVIALEICEQLMKFHgwESGVVHGDIKPSNIHLGCSETVRLLDFGIAKTLrANCNATDHE 172
Cdd:cd05123   76 PGGELFSHLSKEGRFPEERARFYAAEIVLALEYLH--SLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL-SSDGDRTYT 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 116622381 173 F-GSPSYCSPERLTRSEVNPQSDLWALGATLYEMLAGVPPYQAEDT 217
Cdd:cd05123  153 FcGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENR 198