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Conserved domains on  [gi|27377911|ref|NP_769440|]
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bifunctional serine/threonine kinase and phosphatase [Bradyrhizobium diazoefficiens USDA 110]

Protein Classification

PP2Cc and STKc_PknB_like domain-containing protein (domain architecture ID 10001919)

PP2Cc and STKc_PknB_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
274-537 9.38e-58

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


:

Pssm-ID: 270916  Cd Length: 260  Bit Score: 196.65  E-value: 9.38e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 274 GYRIVREIHGSSRSHIYLAVDAETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATE 353
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 354 FIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGsvrVAGVAEAAPKSA 433
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG---IARALGDSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 434 DEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPY-GAQLAKIRGRSDawKLRYRPAIDAERGIPGWIDGA 512
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHL--QEAPPPPSPLNPDVPPALDAI 235
                       250       260
                ....*....|....*....|....*
gi 27377911 513 LRKALHPDPYKRHEDLSEFVFELRN 537
Cdd:cd14014 236 ILRALAKDPEERPQSAAELLAALRA 260
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
10-251 1.94e-33

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


:

Pssm-ID: 223704  Cd Length: 262  Bit Score: 129.01  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  10 ISIGQHSDRG-RKPVNQDFHGILIPE-EPLLSLkgiaAVLADGISSSTVSQIASESAVKSfLMDYYCTSESWTVKTSARR 87
Cdd:COG0631   8 LKVAGLSDVGtVRKHNEDAFLIKPNEnGNLLLL----FAVADGMGGHAAGEVASKLAVEA-LARLFDETNFNSLNESLEE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  88 VLDATNSWLHAQTRKSQYAYDRDKGYVCTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDH--------RIIVSSE 159
Cdd:COG0631  83 LLKEAILKANEAIAEEGQLNEDVRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHslvnrleqRGIITPE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 160 QTY-------LGRALGINPQLEIDYQTVEIEAGDTFILATDGAYEFVDQRFITSAIAEHaAELDGAAKAIVDEAYRRGSD 232
Cdd:COG0631 163 EARshprrnaLTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNS-ETPQEAADKLIELALEGGGP 241
                       250
                ....*....|....*....
gi 27377911 233 DNITVQILRVDAVPQRDSA 251
Cdd:COG0631 242 DNITVVLVRLNGEGETSRD 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
274-537 9.38e-58

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


Pssm-ID: 270916  Cd Length: 260  Bit Score: 196.65  E-value: 9.38e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 274 GYRIVREIHGSSRSHIYLAVDAETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATE 353
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 354 FIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGsvrVAGVAEAAPKSA 433
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG---IARALGDSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 434 DEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPY-GAQLAKIRGRSDawKLRYRPAIDAERGIPGWIDGA 512
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHL--QEAPPPPSPLNPDVPPALDAI 235
                       250       260
                ....*....|....*....|....*
gi 27377911 513 LRKALHPDPYKRHEDLSEFVFELRN 537
Cdd:cd14014 236 ILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
275-524 1.27e-37

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 140.36  E-value: 1.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    275 YRIVREI-HGSSrSHIYLAVDAETEGPVALKlpSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATE 353
Cdd:smart00220   1 YEILEKLgEGSF-GKVYLARDKKTGKLVAIK--VIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    354 FIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRvagvaEAAPKSA 433
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR-----QLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    434 DEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYGA-----QLAKIRGRSDAWKLRYRPAIDAErgipgw 508
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddqllELFKKIGKPKPPFPPPEWDISPE------ 226
                          250
                   ....*....|....*....
gi 27377911    509 idgA---LRKALHPDPYKR 524
Cdd:smart00220 227 ---AkdlIRKLLVKDPEKR 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
274-538 5.62e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 136.03  E-value: 5.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 274 GYRIVREIHGSSRSHIYLAVDAEtegPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRR-RSYLYVAT 352
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQdEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 353 EFIEGQTLRQWMLDNPRP---DLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGT-AKIIDFGSVRVAG--VA 426
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKgplSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPdpGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 427 EAAPKSADEEILGTVQYTAPEYFLG---EGGSPRSDMFSLAAICYHMLTGHLPYGA--------QLAKIRGRSDAWKLRY 495
Cdd:COG0515 158 TSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGeknssatsQTLKIILELPTPSLAS 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 27377911 496 RPAIDAERGIPGWIDGALRKALHPDPYKRHEDLSEFVFELRNP 538
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAH 280
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
10-251 1.94e-33

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 223704  Cd Length: 262  Bit Score: 129.01  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  10 ISIGQHSDRG-RKPVNQDFHGILIPE-EPLLSLkgiaAVLADGISSSTVSQIASESAVKSfLMDYYCTSESWTVKTSARR 87
Cdd:COG0631   8 LKVAGLSDVGtVRKHNEDAFLIKPNEnGNLLLL----FAVADGMGGHAAGEVASKLAVEA-LARLFDETNFNSLNESLEE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  88 VLDATNSWLHAQTRKSQYAYDRDKGYVCTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDH--------RIIVSSE 159
Cdd:COG0631  83 LLKEAILKANEAIAEEGQLNEDVRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHslvnrleqRGIITPE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 160 QTY-------LGRALGINPQLEIDYQTVEIEAGDTFILATDGAYEFVDQRFITSAIAEHaAELDGAAKAIVDEAYRRGSD 232
Cdd:COG0631 163 EARshprrnaLTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNS-ETPQEAADKLIELALEGGGP 241
                       250
                ....*....|....*....
gi 27377911 233 DNITVQILRVDAVPQRDSA 251
Cdd:COG0631 242 DNITVVLVRLNGEGETSRD 260
Pkinase pfam00069
Protein kinase domain;
275-524 1.18e-32

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 126.56  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   275 YRIVREI-HGSSrSHIYLAVDAETEGPVALKlpSIDLR-DNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVAT 352
Cdd:pfam00069   1 YEVLRKLgSGSF-GTVYKAKHRDTGKIVAIK--KIKKEkIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   353 EFIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRVAGvaeaaPKS 432
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLN-----SGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   433 ADEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYGAQLAKIRGRSDawkLRYRPAIDAERGIPGWIDGA 512
Cdd:pfam00069 153 SLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKI---IDQDFDSPRPSSISEEAKDL 229
                         250
                  ....*....|..
gi 27377911   513 LRKALHPDPYKR 524
Cdd:pfam00069 230 LKKLLKKDPSKR 241
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
10-242 7.49e-29

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 115.89  E-value: 7.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  10 ISIGQHSDRGRKPVNQDFHGILIPeepLLSLKGIAAVLADGISSSTVSQIASESAVKSFLmdYYCTSESWTVKTSARRVL 89
Cdd:cd00143   1 FSAGVSDKGGDRKTNEDAVVIKPN---LNNEDGGLFGVFDGHGGHAAGEFASKLLVEELL--EELEETLTLSEEDIEEAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  90 daTNSWLHAQTRKSQYAYDRDKGYV--CTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDH---------RIIVSS 158
Cdd:cd00143  76 --RKAFLRADEEILEEAQDEPDDARsgTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHkpvneeereRIEKAG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 159 EQTYLG---------RALG-----INPQLEIDYQTVEI-EAGDTFILATDGAYEFVDQRFITSAIAEHAAE--LDGAAKA 221
Cdd:cd00143 154 GRVSNGrvpgvlavtRALGdfdlkPGVSAEPDVTVVKLtEDDDFLILASDGLWDVLSNQEAVDIVRSELAKedLQEAAQE 233
                       250       260
                ....*....|....*....|.
gi 27377911 222 IVDEAYRRGSDDNITVQILRV 242
Cdd:cd00143 234 LVDLALRRGSHDNITVVVVRL 254
pknD PRK13184
serine/threonine-protein kinase; Reviewed
275-576 1.22e-24

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 109.09  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  275 YRIVREIHGSSRSHIYLAVDAETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATEF 354
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  355 IEGQTLRQ-----WMLDNPRPDLE------TVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSvrva 423
Cdd:PRK13184  84 IEGYTLKSllksvWQKESLSKELAektsvgAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA---- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  424 gvaeAAPKSADEE----------------------ILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYgaql 481
Cdd:PRK13184 160 ----AIFKKLEEEdlldidvdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY---- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  482 akirGRSDAWKLRYRPAIDAE------RGIPGWIDGALRKALHPDPYKRHEDLSEFVFELRN---PNPAYLATRTTPLLE 552
Cdd:PRK13184 232 ----RRKKGRKISYRDVILSPievapyREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPhlqGSPEWTVKATLMTKK 307
                        330       340
                 ....*....|....*....|....
gi 27377911  553 RNPllfWKLTTAILACAVITLLAV 576
Cdd:PRK13184 308 KSC---WKFYEPILLSKYFPMLES 328
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
7-240 2.67e-21

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625  Cd Length: 252  Bit Score: 94.36  E-value: 2.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911      7 GLLISIGQHSDRGRKPVNQDFHGILIPEEPLLSLKGIAavlaDGISSSTVSQIASE---SAVKSFLMDYYCTSESWTvkt 83
Cdd:smart00332   6 NLGLRYGLSSMQGVRKPMEDAHVITPDLSDSGGFFGVF----DGHGGSEAAKFLSKnlpEILAEELIKEKDELEDVE--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911     84 sarRVLDATNSWLHAQTRKsqyAYDRDKGyvCTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDHRIIVSSE---- 159
Cdd:smart00332  79 ---EALRKAFLSTDEEILE---ELEALSG--STAVVALISGNKLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDErari 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    160 --------------QTYLGRALG-------INPQLEIdYQTVEIEAGDTFILATDGAYEFV-DQRFITSAIAEHAAELDG 217
Cdd:smart00332 151 eaaggfvingrvngVLALSRAIGdfflkpyVSAEPDV-TVVELTEKDDFLILASDGLWDVLsNQEVVDIVRKHLSKDPKE 229
                          250       260
                   ....*....|....*....|...
gi 27377911    218 AAKAIVDEAYRRGSDDNITVQIL 240
Cdd:smart00332 230 AAKRLIDLALARGSKDNITVVVV 252
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
296-526 2.06e-20

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 95.68  E-value: 2.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    296 ETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRR-SYLYVATEFIEGQTLRQWML-DNPRPDLE 373
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAaDGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    374 TVRgIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGT---AKIIDFG-SVRVAGVAEAAPK--SADEEILGTVQYTAPE 447
Cdd:TIGR03903   81 TGR-LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGiGTLLPGVRDADVAtlTRTTEVLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    448 YFLGEGGSPRSDMFSLAAICYHMLTGHLPY-GAQLAKIrgrsdawklRYRPAIDAERGIPGWIDG-----ALRKALHPDP 521
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTGQRVVqGASVAEI---------LYQQLSPVDVSLPPWIAGhplgqVLRKALNKDP 230

                   ....*
gi 27377911    522 YKRHE 526
Cdd:TIGR03903  231 RQRAA 235
PRK14559 PRK14559
putative protein serine/threonine phosphatase; Provisional
15-250 4.62e-16

putative protein serine/threonine phosphatase; Provisional


Pssm-ID: 237756  Cd Length: 645  Bit Score: 81.26  E-value: 4.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   15 HSDRGR-KPVNQDFHGILIPEEPLLSLKG--IAA----VLADGISSSTVSQIASESAVKSfLMDYYctSESWTVK-TSAR 86
Cdd:PRK14559 380 RTDVGRqRHHNEDYFGINTRIQKLENPHGriVQArglyILCDGMGGHAAGEVASALAVET-LQQYF--QQHWQDElPDEE 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   87 RVLDATNswlhaQTRKSQYAYDRDKGYV------CTLSAMVIKATTAHIFHVGDCRIYRVAGK-ALEQLTDDH----RII 155
Cdd:PRK14559 457 TIREAIY-----LANEAIYDLNQQNARSgsgrmgTTLVMALVQDTQVAVAHVGDSRLYRVTRKgGLEQLTVDHevgqREI 531
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  156 ---VSSEQTY-------LGRALG------INPqleiDYQTVEIEAGDTFILATDGayeFVDQRFITSAIAEH-------A 212
Cdd:PRK14559 532 qrgVEPQIAYarpdayqLTQALGprdnsaIQP----DIQFLEIEEDTLLLLCSDG---LSDNDLLETHWQTHllpllssS 604
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 27377911  213 AELDGAAKAIVDEAYRRGSDDNITVQILRVDAVPQRDS 250
Cdd:PRK14559 605 ANLDQGLNKLIDLANQYNGHDNITAILVRLKVRPQLSL 642
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
15-194 1.30e-08

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 316216  Cd Length: 209  Bit Score: 55.02  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    15 HSDRGrKPvNQDFHGILIPEepllslKGIAAVLADGISSSTVSQIASESAVKSFLMDYYCTSESWTVKTSARRVlDATNS 94
Cdd:pfam13672   5 HIRRG-LP-CQDAFAVWVLD------GGWLIAVADGAGSAKRSDVGARIAVEAAVEALADLLESEEELIEALLR-AILND 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    95 WLhAQTRKSQYAYDRD-KGYVCTLSAMVIKATTAHIFHVGDCRI-YRVAGKALEQLTDDHRIIVSSEQTYLGRAlgiNPQ 172
Cdd:pfam13672  76 WL-ALVKAEALAQDLEpRDYATTLLAAVVTPGGIVFFQIGDGAIvVRDRDGEVQVLSQPDSGEYANETTFLTSE---DAL 151
                         170       180
                  ....*....|....*....|..
gi 27377911   173 LEIDYQTVEIEAGDTFILATDG 194
Cdd:pfam13672 152 DELRIRRLPLEPGDALALMTDG 173
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
274-537 9.38e-58

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


Pssm-ID: 270916  Cd Length: 260  Bit Score: 196.65  E-value: 9.38e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 274 GYRIVREIHGSSRSHIYLAVDAETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATE 353
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 354 FIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGsvrVAGVAEAAPKSA 433
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG---IARALGDSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 434 DEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPY-GAQLAKIRGRSDawKLRYRPAIDAERGIPGWIDGA 512
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHL--QEAPPPPSPLNPDVPPALDAI 235
                       250       260
                ....*....|....*....|....*
gi 27377911 513 LRKALHPDPYKRHEDLSEFVFELRN 537
Cdd:cd14014 236 ILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
275-524 1.27e-37

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 140.36  E-value: 1.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    275 YRIVREI-HGSSrSHIYLAVDAETEGPVALKlpSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATE 353
Cdd:smart00220   1 YEILEKLgEGSF-GKVYLARDKKTGKLVAIK--VIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    354 FIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRvagvaEAAPKSA 433
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR-----QLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911    434 DEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYGA-----QLAKIRGRSDAWKLRYRPAIDAErgipgw 508
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddqllELFKKIGKPKPPFPPPEWDISPE------ 226
                          250
                   ....*....|....*....
gi 27377911    509 idgA---LRKALHPDPYKR 524
Cdd:smart00220 227 ---AkdlIRKLLVKDPEKR 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
274-538 5.62e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 136.03  E-value: 5.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 274 GYRIVREIHGSSRSHIYLAVDAEtegPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRR-RSYLYVAT 352
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRK---LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQdEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 353 EFIEGQTLRQWMLDNPRP---DLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGT-AKIIDFGSVRVAG--VA 426
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKgplSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPdpGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 427 EAAPKSADEEILGTVQYTAPEYFLG---EGGSPRSDMFSLAAICYHMLTGHLPYGA--------QLAKIRGRSDAWKLRY 495
Cdd:COG0515 158 TSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGeknssatsQTLKIILELPTPSLAS 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 27377911 496 RPAIDAERGIPGWIDGALRKALHPDPYKRHEDLSEFVFELRNP 538
Cdd:COG0515 238 PLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAH 280
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
287-470 1.26e-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  Cd Length: 215  Bit Score: 130.85  E-value: 1.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 287 SHIYLAVDAETEGPVALKLpsIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATEFIEGQTLRQWMLD 366
Cdd:cd00180   7 GKVYKARDKETGKKVAVKV--IPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 367 NPRP-DLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRVAGVAEaaPKSADEEILGTVQYTA 445
Cdd:cd00180  85 NKGPlSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD--SLLKTTGGTTPPYYAP 162
                       170       180
                ....*....|....*....|....*
gi 27377911 446 PEYFLGEGGSPRSDMFSLAAICYHM 470
Cdd:cd00180 163 PELLGGRYYGPKVDIWSLGVILYEL 187
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
10-251 1.94e-33

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 223704  Cd Length: 262  Bit Score: 129.01  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  10 ISIGQHSDRG-RKPVNQDFHGILIPE-EPLLSLkgiaAVLADGISSSTVSQIASESAVKSfLMDYYCTSESWTVKTSARR 87
Cdd:COG0631   8 LKVAGLSDVGtVRKHNEDAFLIKPNEnGNLLLL----FAVADGMGGHAAGEVASKLAVEA-LARLFDETNFNSLNESLEE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  88 VLDATNSWLHAQTRKSQYAYDRDKGYVCTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDH--------RIIVSSE 159
Cdd:COG0631  83 LLKEAILKANEAIAEEGQLNEDVRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHslvnrleqRGIITPE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 160 QTY-------LGRALGINPQLEIDYQTVEIEAGDTFILATDGAYEFVDQRFITSAIAEHaAELDGAAKAIVDEAYRRGSD 232
Cdd:COG0631 163 EARshprrnaLTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNS-ETPQEAADKLIELALEGGGP 241
                       250
                ....*....|....*....
gi 27377911 233 DNITVQILRVDAVPQRDSA 251
Cdd:COG0631 242 DNITVVLVRLNGEGETSRD 260
Pkinase pfam00069
Protein kinase domain;
275-524 1.18e-32

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 126.56  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   275 YRIVREI-HGSSrSHIYLAVDAETEGPVALKlpSIDLR-DNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVAT 352
Cdd:pfam00069   1 YEVLRKLgSGSF-GTVYKAKHRDTGKIVAIK--KIKKEkIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   353 EFIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRVAGvaeaaPKS 432
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLN-----SGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911   433 ADEEILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYGAQLAKIRGRSDawkLRYRPAIDAERGIPGWIDGA 512
Cdd:pfam00069 153 SLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKI---IDQDFDSPRPSSISEEAKDL 229
                         250
                  ....*....|..
gi 27377911   513 LRKALHPDPYKR 524
Cdd:pfam00069 230 LKKLLKKDPSKR 241
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
300-524 1.35e-29

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


Pssm-ID: 270901  Cd Length: 245  Bit Score: 117.64  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 300 PVALKLPSIDlRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATEFIEGQTLRQWMLDNPRP-DLETVRGI 378
Cdd:cd13999  18 DVAIKKLKVE-DDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHKKKIPlSWSLRLKI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 379 VEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRVAGVAEAAPKSadeeILGTVQYTAPEYFLGEGGSPRS 458
Cdd:cd13999  97 ALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTG----VVGTPRWMAPEVLRGEPYTEKA 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 459 DMFSLAAICYHMLTGHLPYgaqlAKIRGRSDAWKLRYRPaidAERGIPGWIDGALRKAL----HPDPYKR 524
Cdd:cd13999 173 DVYSFGIVLWELLTGEVPF----KELSPIQIAAAVVQKG---LRPPIPPDCPPELSKLIkrcwNEDPEKR 235
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
10-242 7.49e-29

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 115.89  E-value: 7.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  10 ISIGQHSDRGRKPVNQDFHGILIPeepLLSLKGIAAVLADGISSSTVSQIASESAVKSFLmdYYCTSESWTVKTSARRVL 89
Cdd:cd00143   1 FSAGVSDKGGDRKTNEDAVVIKPN---LNNEDGGLFGVFDGHGGHAAGEFASKLLVEELL--EELEETLTLSEEDIEEAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  90 daTNSWLHAQTRKSQYAYDRDKGYV--CTLSAMVIKATTAHIFHVGDCRIYRVAGKALEQLTDDH---------RIIVSS 158
Cdd:cd00143  76 --RKAFLRADEEILEEAQDEPDDARsgTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHkpvneeereRIEKAG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 159 EQTYLG---------RALG-----INPQLEIDYQTVEI-EAGDTFILATDGAYEFVDQRFITSAIAEHAAE--LDGAAKA 221
Cdd:cd00143 154 GRVSNGrvpgvlavtRALGdfdlkPGVSAEPDVTVVKLtEDDDFLILASDGLWDVLSNQEAVDIVRSELAKedLQEAAQE 233
                       250       260
                ....*....|....*....|.
gi 27377911 222 IVDEAYRRGSDDNITVQILRV 242
Cdd:cd00143 234 LVDLALRRGSHDNITVVVVRL 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
275-524 4.33e-26

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


Pssm-ID: 270905  Cd Length: 252  Bit Score: 107.99  E-value: 4.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 275 YRIVREI-HGSSrSHIYLAVDAETEGPVALKlpSIDLRDNAAYLKRFLMEEwIA--RRIDSPHVLKPMSQSRRRSYLYVA 351
Cdd:cd14003   2 YELGKTLgEGSF-GKVKLARHKLTGEKVAIK--IIDKSKLKEEIEEKIKRE-IEimKLLNHPNIIKLYEVIETENKIYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 352 TEFIEGQTLRQWMLDNPRPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGsvrvagvaeAAPK 431
Cdd:cd14003  78 MEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG---------LSNE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 432 SADEEIL----GTVQYTAPEYFLGEG--GsPRSDMFSLAAICYHMLTGHLPY-GAQLAKIRGRSDAWKLRYRPAIDAE-R 503
Cdd:cd14003 149 FRGGSLLktfcGTPAYAAPEVLLGRKydG-PKADVWSLGVILYAMLTGYLPFdDDNDSKLFRKILKGKYPIPSHLSPDaR 227
                       250       260
                ....*....|....*....|.
gi 27377911 504 GIpgwidgaLRKALHPDPYKR 524
Cdd:cd14003 228 DL-------IRRMLVVDPSKR 241
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
290-524 8.82e-26

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


Pssm-ID: 270783  Cd Length: 258  Bit Score: 107.22  E-value: 8.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 290 YLAVDAETEGPVALKlpSIDL-RDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATEFIEGQTLRQWMLDNP 368
Cdd:cd06606  17 YLALNLDTGELMAVK--EVELsGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLASLLKKFG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 369 RPDLETVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSVRVagVAEAAPKSADEEILGTVQYTAPEY 448
Cdd:cd06606  95 KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKR--LAEIATGEGTKSLRGTPYWMAPEV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911 449 FLGEGGSPRSDMFSLAAICYHMLTGHLPYGAQlakirgrSDAWKLRYRPAIDAER-GIPGWI-DGA---LRKALHPDPYK 523
Cdd:cd06606 173 IRGEGYGRAADIWSLGCTVIEMATGKPPWSEL-------GNPVAALFKIGSSGEPpPIPEHLsEEAkdfLRKCLQRDPKK 245

                .
gi 27377911 524 R 524
Cdd:cd06606 246 R 246
pknD PRK13184
serine/threonine-protein kinase; Reviewed
275-576 1.22e-24

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 109.09  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  275 YRIVREIHGSSRSHIYLAVDAETEGPVALKLPSIDLRDNAAYLKRFLMEEWIARRIDSPHVLKPMSQSRRRSYLYVATEF 354
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  355 IEGQTLRQ-----WMLDNPRPDLE------TVRGIVEQIATGLRAFHRMEMLHQDLRPDNVLIDKTGTAKIIDFGSvrva 423
Cdd:PRK13184  84 IEGYTLKSllksvWQKESLSKELAektsvgAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA---- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  424 gvaeAAPKSADEE----------------------ILGTVQYTAPEYFLGEGGSPRSDMFSLAAICYHMLTGHLPYgaql 481
Cdd:PRK13184 160 ----AIFKKLEEEdlldidvdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY---- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27377911  482 akirGRSDAWKLRYRPAIDAE------RGIPGWIDGALRKALHPDPYKRHEDLSEFVFELRN---PNPAYLATRTTPLLE 552
Cdd:PRK13184 232 ----RRKKGRKISYRDVILSPievapyREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPhlqGSPEWTVKATLMTKK 307
                        330       340
                 ....*....|....*....|....
gi 27377911  553 RNPllfWKLTTAILACAVITLLAV 576
Cdd:PRK13184 308 KSC---WKFYEPILLSKYFPMLES 328