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Conserved domains on  [gi|116625318|ref|YP_827474|]
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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 ...
11-266 9.57e-89

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: 283.71  E-value: 9.57e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  11 PYEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDPVSRARFEQEARAVAALNHPNIVAVYDVGE----GYFVSE 86
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEddgrPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  87 LVDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARirptkaasALDQ 161
Cdd:cd14014   81 YVEGGSLadllrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR--------ALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 162 TVTAHTeaGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPP---ELPDTVPP 238
Cdd:cd14014  153 SGLTQT--GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPppsPLNPDVPP 230
                        250       260
                 ....*....|....*....|....*...
gi 116625318 239 MLRDIVTRCLEKEPGQRFQSAKDLEFAL 266
Cdd:cd14014  231 ALDAIILRALAKDPEERPQSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-262 1.62e-55

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 191.97  E-value: 1.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318    12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEvaRDPVSRARFEQEARAVAALNHPNIVAVYDVGEG----YFVSEL 87
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDedklYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318    88 VDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARIrptkaasaldqt 162
Cdd:smart00220  79 CEGGDLfdllkKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ------------ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   163 VTAHTEAGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPPELP---DTVPPM 239
Cdd:smart00220 147 LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPppeWDISPE 226
                          250       260
                   ....*....|....*....|...
gi 116625318   240 LRDIVTRCLEKEPGQRFqSAKDL 262
Cdd:smart00220 227 AKDLIRKLLVKDPEKRL-TAEEA 248
SGL pfam08450
SMP-30/Gluconolaconase/LRE-like region; This family describes a region that is found in ...
375-587 2.99e-05

SMP-30/Gluconolaconase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


:

Pssm-ID: 254808 [Multi-domain]  Cd Length: 245  Bit Score: 44.93  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  375 EQVSWSADGTRLYFdrlTDVPRG-VYSVPKLGGKEQLLLEDASNpEALA---DGSLLVtrlnaARKHQIFRFWTDSGRVE 450
Cdd:pfam08450   3 EGPVWDEEEGALYW---VDILGGrIHRLDPATGKETVWDLPGPV-GAIAlrdDGRLIV-----ALKRGLALLDLDTGELT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  451 alpVLLKMVGDRSIVRaFPDGK-----SAVAyGTPAN---AAGSSPALYRIEIGSGAVRLLDP-GPPEGaevggLAVTRD 521
Cdd:pfam08450  74 ---TLADLEPDEPLNR-FNDGKvdpdgRFWF-GTMGFdiaPGGEPGALYRLDPDGKVERVLDGiTISNG-----LAWSPD 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116625318  522 GKRVLFATSRRSAYTVKSIPADGNGPSPEVLLLTGAAYslDAGPDGSIyLDQ-------WHRASTLLRFSASG 587
Cdd:pfam08450 144 GKTLYFADSPTRRIWAFDYDADGGLISNRRVFADFKDG--DGEPDGMA-VDAegnvwvaRWGGGKVVRYDPDG 213
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-266 9.57e-89

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: 283.71  E-value: 9.57e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  11 PYEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDPVSRARFEQEARAVAALNHPNIVAVYDVGE----GYFVSE 86
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEddgrPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  87 LVDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARirptkaasALDQ 161
Cdd:cd14014   81 YVEGGSLadllrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR--------ALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 162 TVTAHTeaGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPP---ELPDTVPP 238
Cdd:cd14014  153 SGLTQT--GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPppsPLNPDVPP 230
                        250       260
                 ....*....|....*....|....*...
gi 116625318 239 MLRDIVTRCLEKEPGQRFQSAKDLEFAL 266
Cdd:cd14014  231 ALDAIILRALAKDPEERPQSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-262 1.62e-55

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 191.97  E-value: 1.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318    12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEvaRDPVSRARFEQEARAVAALNHPNIVAVYDVGEG----YFVSEL 87
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDedklYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318    88 VDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARIrptkaasaldqt 162
Cdd:smart00220  79 CEGGDLfdllkKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ------------ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   163 VTAHTEAGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPPELP---DTVPPM 239
Cdd:smart00220 147 LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPppeWDISPE 226
                          250       260
                   ....*....|....*....|...
gi 116625318   240 LRDIVTRCLEKEPGQRFqSAKDL 262
Cdd:smart00220 227 AKDLIRKLLVKDPEKRL-TAEEA 248
Pkinase pfam00069
Protein kinase domain;
12-262 2.36e-45

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 163.96  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDPVSRARFeQEARAVAALNHPNIVAVYDV----GEGYFVSEL 87
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQTAR-REIRILRRLSHPNIVRLIDAfedkDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   88 VDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARIRPTKaasaldqt 162
Cdd:pfam00069  80 CEGGDLfdylsRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKS-------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  163 vtaHTEAGTVVGTVSYMSPEQVR-GLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILR--QDPPELP----DT 235
Cdd:pfam00069 152 ---SSSLTTFVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRilGPPLEFDepksDS 228
                         250       260
                  ....*....|....*....|....*..
gi 116625318  236 VPPMLRDIVTRCLEKEPGQRFqSAKDL 262
Cdd:pfam00069 229 GSEEAKDLIKKCLNKDPSKRP-TAEEI 254
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
12-267 3.14e-45

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: 167.23  E-value: 3.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  12 YEIVAPLGAGGMGEVYRAHDSRlgrDVALKILPAEVARDPVSRARFEQEARAVAALNHP-NIVAVYDVGEG----YFVSE 86
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDegslYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  87 LVDGESLR--------GAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDG-RAKILDFGLArirptKAAS 157
Cdd:COG0515   79 YVDGGSLEdllkkigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLA-----KLLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 158 ALDQTVTAHTEAGTVVGTVSYMSPEQVRGLE---VDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILR-------- 226
Cdd:COG0515  154 DPGSTSSIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptp 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 116625318 227 ----QDPPELPDTVPPMLRDIVTRCLEKEPGQRFQSAKDLEFALL 267
Cdd:COG0515  234 slasPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLL 278
pknD PRK13184
serine/threonine-protein kinase; Reviewed
9-266 2.97e-35

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 142.99  E-value: 2.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   9 LGPYEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDPVSRARFEQEARAVAALNHPNIVAVYDV-GEG---YFV 84
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSIcSDGdpvYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  85 SELVDGESLRG------AKFSLRKTLDIAAQIAS----------GIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLA 148
Cdd:PRK13184  81 MPYIEGYTLKSllksvwQKESLSKELAEKTSVGAflsifhkicaTIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 149 RIRPTK----AASALDQTVTAH---TEAGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTM 221
Cdd:PRK13184 161 IFKKLEeedlLDIDVDERNICYssmTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIS 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 116625318 222 QAILRQDPPELPD--TVPPMLRDIVTRCLEKEPGQRFQSAKDLEFAL 266
Cdd:PRK13184 241 YRDVILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
13-263 4.46e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 110.30  E-value: 4.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  13 EIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEvARDPVSRarfeQEARAVAAL---NHPNIVAVYDV----GEGYFVS 85
Cdd:PLN00034  77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN-HEDTVRR----QICREIEILrdvNHPNVVKCHDMfdhnGEIQVLL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  86 ELVDGESLRGAKFSLRKTL-DIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARIrptkaasaLDQTVT 164
Cdd:PLN00034 152 EFMDGGSLEGTHIADEQFLaDVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRI--------LAQTMD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 165 AhteAGTVVGTVSYMSPEQV-----RGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVD---TMQAILRQDPPELPDTV 236
Cdd:PLN00034 224 P---CNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDwasLMCAICMSQPPEAPATA 300
                        250       260
                 ....*....|....*....|....*..
gi 116625318 237 PPMLRDIVTRCLEKEPGQRFQSAKDLE 263
Cdd:PLN00034 301 SREFRHFISCCLQREPAKRWSAMQLLQ 327
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
35-262 1.39e-25

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: 112.63  E-value: 1.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318    35 GRDVALKILPAEVARDPVSRARFEQEARAVAALNHPNIVAVYDVGEG-----YFVSELVDGESLR------GAkFSLRKT 103
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAppgllFAVFEYVPGRTLRevlaadGA-LPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   104 LDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDG---RAKILDFGLARIRPtKAASALDQTVTAHTEagtVVGTVSYMS 180
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLP-GVRDADVATLTRTTE---VLGTPTYCA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318   181 PEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPPELPDTVPPM-LRDIVTRCLEKEPGQRFQSA 259
Cdd:TIGR03903  158 PEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPWIAGHpLGQVLRKALNKDPRQRAASA 237

                   ...
gi 116625318   260 KDL 262
Cdd:TIGR03903  238 PAL 240
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
123-262 2.17e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 88.00  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 123 VHRDLKPGNILVTHDGRAKILDFGLarirpTKAASAldqtvTAHTEAG-TVVGTVSYMSPEQVRGLEVDHRSDIFSFGIM 201
Cdd:PTZ00283 165 IHRDIKSANILLCSNGLVKLGDFGF-----SKMYAA-----TVSDDVGrTFCGTPYYVAPEIWRRKPYSKKADMFSLGVL 234
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116625318 202 LHGMLGGSRTFHGETTVDTMQAIL--RQDPpeLPDTVPPMLRDIVTRCLEKEPGQRFQSAKDL 262
Cdd:PTZ00283 235 LYELLTLKRPFDGENMEEVMHKTLagRYDP--LPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
Protein_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
331-412 2.70e-08

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274305 [Multi-domain]  Cd Length: 417  Bit Score: 55.74  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  331 PRLSPDGQTLAFTPFVSGVTQVAVMTPASGDIAVLthaTAEGSVEQVSWSADGTRLYFDRLTDvPRGVYSVPKLGGKEQL 410
Cdd:TIGR02800 327 PSWSPDGDLIAFVHREGGGFNIAVMDLDGGGERVL---TDTGLDESPSFAPNGRMILYATTRG-GRGVLGLVSTDGRFRA 402

                  ..
gi 116625318  411 LL 412
Cdd:TIGR02800 403 RL 404
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
123-249 3.95e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 51.01  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 123 VHRDLKPGNILVT-HDGRAKILDFGLARIRPTKaaSALDqtvtahteagtvvGTVSYMSPEQVRGLEVDHRSDIFSFGIM 201
Cdd:PHA03390 131 IHNDIKLENVLYDrAKDRIYLCDYGLCKIIGTP--SCYD-------------GTLDYFSPEKIKGHNYDVSFDWWAVGVL 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116625318 202 LHGMLGGSRTF---HGET-TVDTMQAILRQDPPELPDtVPPMLRDIVTRCLE 249
Cdd:PHA03390 196 TYELLTGKHPFkedEDEElDLESLLKRQQKKLPFIKN-VSKNANDFVQSMLK 246
tolB PRK04922
translocation protein TolB; Provisional
329-530 1.64e-06

translocation protein TolB; Provisional


Pssm-ID: 179892 [Multi-domain]  Cd Length: 433  Bit Score: 50.05  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 329 SCPRLSPDGQTLAFTPFVSGVTQVAVMTPASGDIAVLTHATAEGSveQVSWSADGTRLYF--DRltdvprgvysvpklGG 406
Cdd:PRK04922 251 GAPSFSPDGRRLALTLSRDGNPEIYVMDLGSRQLTRLTNHFGIDT--EPTWAPDGKSIYFtsDR--------------GG 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 407 KEQLLLEDASNPEAladgsllvTRLnaarkhqifrfwTDSGRVEALPVLLkmvgdrsivrafPDGKS-AVAYGTpanaaG 485
Cdd:PRK04922 315 RPQIYRVAASGGSA--------ERL------------TFQGNYNARASVS------------PDGKKiAMVHGS-----G 357
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 116625318 486 SSpalYRI---EIGSGAVRLLDPGP--------PEGAEVggLAVTRDGKR-VLFATS 530
Cdd:PRK04922 358 GQ---YRIavmDLSTGSVRTLTPGSldespsfaPNGSMV--LYATREGGRgVLAAVS 409
TolB COG0823
Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and ...
331-428 3.35e-06

Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and secretion]


Pssm-ID: 223893 [Multi-domain]  Cd Length: 425  Bit Score: 48.99  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 331 PRLSPDGQTLAFTPFVSGVTQVAVMTPASGDIAVLTHATAEGSVEqvSWSADGTRLYF--DRlTDVPRgVYSVPKLGGKE 408
Cdd:COG0823  243 PAFSPDGSKLAFSSSRDGSPDIYLMDLDGKNLPRLTNGFGINTSP--SWSPDGSKIVFtsDR-GGRPQ-IYLYDLEGSQV 318
                         90       100
                 ....*....|....*....|...
gi 116625318 409 QLLLEDA---SNPEALADGSLLV 428
Cdd:COG0823  319 TRLTFSGggnSNPVWSPDGDKIV 341
SGL pfam08450
SMP-30/Gluconolaconase/LRE-like region; This family describes a region that is found in ...
375-587 2.99e-05

SMP-30/Gluconolaconase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 254808 [Multi-domain]  Cd Length: 245  Bit Score: 44.93  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  375 EQVSWSADGTRLYFdrlTDVPRG-VYSVPKLGGKEQLLLEDASNpEALA---DGSLLVtrlnaARKHQIFRFWTDSGRVE 450
Cdd:pfam08450   3 EGPVWDEEEGALYW---VDILGGrIHRLDPATGKETVWDLPGPV-GAIAlrdDGRLIV-----ALKRGLALLDLDTGELT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  451 alpVLLKMVGDRSIVRaFPDGK-----SAVAyGTPAN---AAGSSPALYRIEIGSGAVRLLDP-GPPEGaevggLAVTRD 521
Cdd:pfam08450  74 ---TLADLEPDEPLNR-FNDGKvdpdgRFWF-GTMGFdiaPGGEPGALYRLDPDGKVERVLDGiTISNG-----LAWSPD 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116625318  522 GKRVLFATSRRSAYTVKSIPADGNGPSPEVLLLTGAAYslDAGPDGSIyLDQ-------WHRASTLLRFSASG 587
Cdd:pfam08450 144 GKTLYFADSPTRRIWAFDYDADGGLISNRRVFADFKDG--DGEPDGMA-VDAegnvwvaRWGGGKVVRYDPDG 213
TolB COG0823
Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and ...
331-530 8.69e-04

Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and secretion]


Pssm-ID: 223893 [Multi-domain]  Cd Length: 425  Bit Score: 41.28  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 331 PRLSPDGQTLAFTPFVSGVT-QVAVMTPASGDIAVLthATAEGSVEQVSWSADGTRLYFDRLTDVPRGVYSVPKLGGKEQ 409
Cdd:COG0823  198 PAWSPDGKKLAYVSFELGGCpRIYYLDLNTGKRPVI--LNFNGNNGAPAFSPDGSKLAFSSSRDGSPDIYLMDLDGKNLP 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 410 LLLED---ASNPEALADGSLLVTRLNAARKHQIFRFWTDSGRVEAlpvLLKMVGDRSIVRAFPDGKSAVayGTPANAAGS 486
Cdd:COG0823  276 RLTNGfgiNTSPSWSPDGSKIVFTSDRGGRPQIYLYDLEGSQVTR---LTFSGGGNSNPVWSPDGDKIV--FESSSGGQW 350
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116625318 487 SPALYRIEIGSGaVRLLDPG----PPEGAEVGGLAV---TRDGKRVLFATS 530
Cdd:COG0823  351 DIDKNDLASGGK-IRILTSTylneSPSWAPNGRMIMfssGQGGGSVLSLVS 400
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-266 9.57e-89

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: 283.71  E-value: 9.57e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  11 PYEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDPVSRARFEQEARAVAALNHPNIVAVYDVGE----GYFVSE 86
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEddgrPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  87 LVDGESL-----RGAKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARirptkaasALDQ 161
Cdd:cd14014   81 YVEGGSLadllrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR--------ALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 162 TVTAHTeaGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPP---ELPDTVPP 238
Cdd:cd14014  153 SGLTQT--GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPppsPLNPDVPP 230
                        250       260
                 ....*....|....*....|....*...
gi 116625318 239 MLRDIVTRCLEKEPGQRFQSAKDLEFAL 266
Cdd:cd14014  231 ALDAIILRALAKDPEERPQSAAELLAAL 258
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-255 3.29e-43

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 157.70  E-value: 3.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  18 LGAGGMGEVYRAhdSRLGRDVALKILPAEVARDPVSRArFEQEARAVAALNHPNIV----AVYDVGEGYFVSELVDGESL 93
Cdd:cd13999    1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEDDNDELLKE-FRREVSILSKLRHPNIVqfigACLSPPPLCIVTEYMPGGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  94 RGA------KFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLARIrptkaasaLDQTVTAHT 167
Cdd:cd13999   78 YDLlhkkkiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRI--------KNSTTEKMT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 168 eagTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTV-DTMQAILRQDPPELPDTVPPMLRDIVTR 246
Cdd:cd13999  150 ---GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIqIAAAVVQKGLRPPIPPDCPPELSKLIKR 226

                 ....*....
gi 116625318 247 CLEKEPGQR 255
Cdd:cd13999  227 CWNEDPEKR 235
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-262 1.22e-40

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: 150.43  E-value: 1.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDpvsRARFEQEARAVAALNHPNIVAVYDV----GEGYFVSEL 87
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEK---KESILNEIAILKKCKHPNIVKYYGSylkkDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  88 VDGESLRGAKFSLRKTLD------IAAQIASGIAAAHAAGIVHRDLKPGNILVTHDGRAKILDFGLA-RIRPTKAASald 160
Cdd:cd05122   79 CSGGSLKDLLKNTNKTLTeqqiayVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSaQLSDGKTRN--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 161 qtvtahteagTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQDPPELPDTV--PP 238
Cdd:cd05122  156 ----------TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKkwSK 225
                        250       260
                 ....*....|....*....|....
gi 116625318 239 MLRDIVTRCLEKEPGQRfQSAKDL 262
Cdd:cd05122  226 EFKDFLKKCLQKDPEKR-PTAEQL 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
13-262 2.13e-40

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: 150.05  E-value: 2.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  13 EIVAPLGAGGMGEVYRAHDSRLGRDVALKILPaeVARDPVSRARFEQEARAVAALNHPNIV----AVYDVGEGYFVSELV 88
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCESPYVVkcygAFYKEGEISIVLEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  89 DGESLRGA-----KFSLRKTLDIAAQIASGIAAA-HAAGIVHRDLKPGNILVTHDGRAKILDFGLARIrptkaasaLDQT 162
Cdd:cd06623   82 DGGSLADLlkkvgKIPEPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKV--------LENT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 163 VtahTEAGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTF---HGETTVDTMQAILRQDPPELPDT-VPP 238
Cdd:cd06623  154 L---DQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFlppGQPSFFELMQAICDGPPPSLPAEeFSP 230
                        250       260
                 ....*....|....*....|....
gi 116625318 239 MLRDIVTRCLEKEPGQRfQSAKDL 262
Cdd:cd06623  231 EFRDFISACLQKDPKKR-PSAAEL 253
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-262 1.45e-39

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: 147.62  E-value: 1.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEVARDpVSRARFEQEARAVAALNHPNIVAVYDVGEG----YFVSEL 87
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKS-EDEEMLRREIEILKRLDHPNIVKLYEVFEDdknlYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318  88 VDGESL------RGaKFSLRKTLDIAAQIASGIAAAHAAGIVHRDLKPGNILVT---HDGRAKILDFGLARIRPTKaasa 158
Cdd:cd05117   81 CTGGELfdrivkKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKIFEEG---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116625318 159 ldqtvtahTEAGTVVGTVSYMSPEQVRGLEVDHRSDIFSFGIMLHGMLGGSRTFHGETTVDTMQAILRQD---PPELPDT 235
Cdd:cd05117  156 --------EKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKysfDSPEWKN 227
                        250       260
                 ....*....|....*....|....*..
gi 116625318 236 VPPMLRDIVTRCLEKEPGQRFqSAKDL 262
Cdd:cd05117  228 VSEEAKDLIKRLLVVDPKKRL-TAAEA 253
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
12-262 1.14e-37

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: 142.22  E-value: 1.14e-37
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gi 116625318  12 YEIVAPLGAGGMGEVYRAHDSRLGRDVALKILPAEvARDPVSRARFEQEARAVAA