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Conserved domains on  [gi|32476927|ref|NP_869921|]
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serine/threonine-protein kinase [Rhodopirellula baltica SH 1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
383-675 4.04e-91

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: 299.50  E-value: 4.04e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLtpDDQLPFYA 462
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGE--DDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHhldrtaseraKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAK 542
Cdd:cd14014   79 MEYVEGGSLADLLRER----------GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  543 RIGDEEpdqsqkrdvegksddsgfdQTRAGTRLGSPGYMAPEQASGRISDhgAHTDIYGLGATLYELIAGDLPFKASSTA 622
Cdd:cd14014  149 ALGDSG-------------------LTQTGSVLGTPAYMAPEQARGGPVD--PRSDIYSLGVVLYELLTGRPPFDGDSPA 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32476927  623 SLMEAIQHQSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQN 675
Cdd:cd14014  208 AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
WD40 COG2319
WD40 repeat [General function prediction only];
1092-1341 1.69e-06

WD40 repeat [General function prediction only];


:

Pssm-ID: 225201  Cd Length: 466  Bit Score: 52.40  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1092 VAIGTYEDFIVNYVGNTVSISNWRDN-----RDSVSFPTNSQVRsvCWASAGRIIVSGHEDGTVRVHHPFSNAYEEAVVE 1166
Cdd:COG2319  204 LAFSPDGGLLIASGSSDGTIRLWDLStgkllRSTLSGHSDSVVS--SFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLS 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1167 R---TVTNPAIDSGQRYLACLNSDKKLGLLDLRSYEWVTQ-DLCTTTGLVQSLKFNSDSEWIMV----DDESGLFVVNCR 1238
Cdd:COG2319  282 GhssSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKLLSSlTLKGHEGPVSSLSFSPDGSLLVSggsdDGTIRLWDLRTG 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1239 DGKRKVELGNSKSASEFSADGTLVVTKADERVVELYDLQQMHSIDTVGLDLNSVLdtvRCDMDTlRYLLLSSEGKTQQLR 1318
Cdd:COG2319  362 KPLKTLEGHSNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGHTSRVT---SLDFSP-DGKSLASGSSDNTIR 437
                        250       260
                 ....*....|....*....|...
gi 32476927 1319 VIDVSDGRIINEISIKTSISGKG 1341
Cdd:COG2319  438 LWDLKTSLKSVSFSPDGKVLASK 460
WD40 COG2319
WD40 repeat [General function prediction only];
837-1199 5.34e-04

WD40 repeat [General function prediction only];


:

Pssm-ID: 225201  Cd Length: 466  Bit Score: 44.69  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  837 LARFKSPILQVSSSQDGTKIAVL-QDNSRIVFVIDPKSMTVN--GSFECESVVQRVLMNAAGTHLLIAVE--DGKVLYQA 911
Cdd:COG2319   61 LRGHEDSITSIAFSPDGELLLSGsSDGTIKLWDLDNGEKLIKslEGLHDSSVSKLALSSPDGNSILLASSslDGTVKLWD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  912 LSDP-KDRTALLDTPSDCTQLQFG-ARDSIAYVGTLDGLLK-YDLRSGRLLAR-CKTEFRCDAIVPSKDGNVLYISGRQD 987
Cdd:COG2319  141 LSTPgKLIRTLEGHSESVTSLAFSpDGKLLASGSSLDGTIKlWDLRTGKPLSTlAGHTDPVSSLAFSPDGGLLIASGSSD 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  988 R--IDW---GGLKLVGTIKGNgLSLQANLAAKRGFYLERVDAERFIVEKTMINDGALSWPLATDTTGDLILYLQPAENRM 1062
Cdd:COG2319  221 GtiRLWdlsTGKLLRSTLSGH-SDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLSVAFSPDGKLL 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1063 VLNIAD--VAHPPIELMQLGDPLF------------VNPSFPPVAIGTYEDfivnyvgNTVSISNWRDNRDSVSFPTNSQ 1128
Cdd:COG2319  300 ASGSSDgtVRLWDLETGKLLSSLTlkghegpvsslsFSPDGSLLVSGGSDD-------GTIRLWDLRTGKPLKTLEGHSN 372
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32476927 1129 VRSVCWASAGRIIVSGHEDGTVRVHHP--FSNAYEEAVVERTVTNPAIDSGQRYLACLNSDKKLGLLDLRSYE 1199
Cdd:COG2319  373 VLSVSFSPDGRVVSSGSTDGTVRLWDLstGSLLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSL 445
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1620-1808 4.66e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 223533  Cd Length: 291  Bit Score: 40.98  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1620 DSWRWWGTIANRLFEEQRYADSLDAsLNVLVSLGKEKEESDNYVVtlaniAKCQSKLGEFQKARTCLTNALAARDSIgwt 1699
Cdd:COG0457   93 NLAEALLNLGLLLEALGKYEEALEL-LEKALALDPDPDLAEALLA-----LGALYELGDYEEALELYEKALELDPEL--- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1700 DLRVQLLFELATIDADAGQPEEFFENAEAFLEKTAPRKLELWssystlsIRLAREYRLKGRHDKAVVVVGKILDDVKSGA 1779
Cdd:COG0457  164 NELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEAL-------LNLGLLYLKLGKYEEALEYYEKALELDPDNA 236
                        170       180
                 ....*....|....*....|....*....
gi 32476927 1780 gglsdKKLLEILLCLHAGKDFANLIDVYQ 1808
Cdd:COG0457  237 -----EALYNLALLLLELGRYEEALEALE 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
383-675 4.04e-91

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: 299.50  E-value: 4.04e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLtpDDQLPFYA 462
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGE--DDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHhldrtaseraKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAK 542
Cdd:cd14014   79 MEYVEGGSLADLLRER----------GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  543 RIGDEEpdqsqkrdvegksddsgfdQTRAGTRLGSPGYMAPEQASGRISDhgAHTDIYGLGATLYELIAGDLPFKASSTA 622
Cdd:cd14014  149 ALGDSG-------------------LTQTGSVLGTPAYMAPEQARGGPVD--PRSDIYSLGVVLYELLTGRPPFDGDSPA 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32476927  623 SLMEAIQHQSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQN 675
Cdd:cd14014  208 AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
pknD PRK13184
serine/threonine-protein kinase; Reviewed
383-703 6.72e-52

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 199.61  E-value: 6.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELglTPDDQLPFYA 462
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI--CSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   463 MRFVGHKTLHDAIRH-HHLDRTASERAKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLA 541
Cdd:PRK13184   81 MPYIEGYTLKSLLKSvWQKESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   542 KRIGDEEPDQSqkrDVEGKSDDSGFDQ-TRAGTRLGSPGYMAPEQASGriSDHGAHTDIYGLGATLYELIAGDLPFKASS 620
Cdd:PRK13184  161 IFKKLEEEDLL---DIDVDERNICYSSmTIPGKIVGTPDYMAPERLLG--VPASESTDIYALGVILYQMLTLSFPYRRKK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   621 TASLMEAiQHQSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQNWLADEP----IAVLPdnllrasqra 696
Cdd:PRK13184  236 GRKISYR-DVILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSPewtvKATLM---------- 304

                  ....*..
gi 32476927   697 IRKRPSW 703
Cdd:PRK13184  305 TKKKSCW 311
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
392-671 2.81e-45

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 167.71  E-value: 2.81e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     392 TGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPmaIERFLREARITGRLQHPNIIPVYELGLTPDDqlpFY-AMRFVGHKT 470
Cdd:smart00220    9 EGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDK---LYlVMEYCEGGD 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     471 LHDAIRHHhldRTASERAKKVHFRELLQsfvsvckAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIGDEEpd 550
Cdd:smart00220   84 LFDLLKKR---GRLSEDEARFYLRQILS-------ALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     551 qsqkrdvegksddsgfdqtRAGTRLGSPGYMAPEQASGRisDHGAHTDIYGLGATLYELIAGDLPFKASSTASLMEAIQH 630
Cdd:smart00220  152 -------------------KLTTFVGTPEYMAPEVLLGK--GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG 210
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 32476927     631 QSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALAD 671
Cdd:smart00220  211 KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
384-741 5.10e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 159.14  E-value: 5.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  384 YRLTRTHQTGGLGVVSVAEDtvlNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHP-NIIPVYELGltPDDQLPFYA 462
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFF--QDEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHHLDRTASERAKKVHFRELlqsfvsvCKAVAYAHSEGIMHRDIKPANIMLG-DYGEVILLDWGLA 541
Cdd:COG0515   77 MEYVDGGSLEDLLKKIGRKGPLSESEALFILAQI-------LSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  542 KRIGDEepdqsqkrdvegksDDSGFDQTRAGTRLGSPGYMAPEQASGRISDH-GAHTDIYGLGATLYELIAGDLPFKASS 620
Cdd:COG0515  150 KLLPDP--------------GSTSSIPALPSTSVGTPGYMAPEVLLGLSLAYaSSSSDIWSLGITLYELLTGLPPFEGEK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  621 ----TASLMEAIQHQSIPSIA-----ESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQNWLADEPIAVLPDNLLR 691
Cdd:COG0515  216 nssaTSQTLKIILELPTPSLAsplspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPD 295
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 32476927  692 ASQRAIRKRPSWVSGTIAALAVGVLTVTTGLFFVNKEKNLKNESLTRESE 741
Cdd:COG0515  296 DSAPLRLSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSP 345
Pkinase pfam00069
Protein kinase domain;
393-672 5.85e-39

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 149.29  E-value: 5.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    393 GGLGVVSVAEDTVLNRNVAIKQLKgNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLTPDDqlpFY-AMRFVGHKTL 471
Cdd:pfam00069   10 GSFGTVYKAKHRDTGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN---LYlVLEYVEGGSL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    472 HDAIRHHhldRTASERAKKVHFRELLQsfvsvckAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIgdeepdq 551
Cdd:pfam00069   86 FDLLSEK---GAFSEREAKFIMKQILE-------GLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    552 sqkrdvegkSDDSGFDqtragTRLGSPGYMAPEQASGRisDHGAHTDIYGLGATLYELIAGDLPFKASSTASLMEAIQHQ 631
Cdd:pfam00069  149 ---------NSGSSLT-----SFVGTPWYMAPEVLRGN--PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQ 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 32476927    632 SIPSiaESNKQVPAALVAICGKAMEKLPADRYASAEALADD 672
Cdd:pfam00069  213 DFDS--PRPSSISEEAKDLLKKLLKKDPSKRLTATEALQHP 251
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
410-720 1.04e-22

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: 106.47  E-value: 1.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    410 VAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLTPDDQLpFYAMRFVGHKTLHDAIRhhhlDRTASERAK 489
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLL-FAVFEYVPGRTLREVLA----ADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    490 KVHFreLLQsfvsVCKAVAYAHSEGIMHRDIKPANIML---GDYGEVILLDWGLAKRI-GDEEPDQSQkrdvegksddsg 565
Cdd:TIGR03903   81 TGRL--MLQ----VLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLpGVRDADVAT------------ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    566 fdQTRAGTRLGSPGYMAPEQASGRISDhgAHTDIYGLGATLYELIAGDLPFKASSTAslmEAIQHQ------SIPSIAES 639
Cdd:TIGR03903  143 --LTRTTEVLGTPTYCAPEQLRGEPVT--PNSDLYAWGLIFLECLTGQRVVQGASVA---EILYQQlspvdvSLPPWIAG 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    640 NKqvpaaLVAICGKAMEKLPADRYASAEALADDIQNWLADEPIAVLPDNlLRASQRAIrKRPSWVSGTIAALAVGVLTVT 719
Cdd:TIGR03903  216 HP-----LGQVLRKALNKDPRQRAASAPALAERFRALELCALVGILRMG-EGAGREAI-AAPLVASGTLDGETGERRQLT 288

                   .
gi 32476927    720 T 720
Cdd:TIGR03903  289 A 289
WD40 COG2319
WD40 repeat [General function prediction only];
1092-1341 1.69e-06

WD40 repeat [General function prediction only];


Pssm-ID: 225201  Cd Length: 466  Bit Score: 52.40  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1092 VAIGTYEDFIVNYVGNTVSISNWRDN-----RDSVSFPTNSQVRsvCWASAGRIIVSGHEDGTVRVHHPFSNAYEEAVVE 1166
Cdd:COG2319  204 LAFSPDGGLLIASGSSDGTIRLWDLStgkllRSTLSGHSDSVVS--SFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLS 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1167 R---TVTNPAIDSGQRYLACLNSDKKLGLLDLRSYEWVTQ-DLCTTTGLVQSLKFNSDSEWIMV----DDESGLFVVNCR 1238
Cdd:COG2319  282 GhssSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKLLSSlTLKGHEGPVSSLSFSPDGSLLVSggsdDGTIRLWDLRTG 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1239 DGKRKVELGNSKSASEFSADGTLVVTKADERVVELYDLQQMHSIDTVGLDLNSVLdtvRCDMDTlRYLLLSSEGKTQQLR 1318
Cdd:COG2319  362 KPLKTLEGHSNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGHTSRVT---SLDFSP-DGKSLASGSSDNTIR 437
                        250       260
                 ....*....|....*....|...
gi 32476927 1319 VIDVSDGRIINEISIKTSISGKG 1341
Cdd:COG2319  438 LWDLKTSLKSVSFSPDGKVLASK 460
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1107-1332 3.77e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121  Cd Length: 289  Bit Score: 47.71  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1107 NTVSISNWRDNRDSVSFPT-NSQVRSVCWASAGRIIVSGHEDGTVRVHHpFSNAYEEAVV---ERTVTNPAIDSGQRYLA 1182
Cdd:cd00200   73 KTIRLWDLETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWD-VETGKCLTTLrghTDWVNSVAFSPDGTFVA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1183 CLNSDKKLGLLDLRsyewvtqdlctTTGLVQSLKFNSDSewimvddesglfvVNCrdgkrkvelgnsksaSEFSADGTLV 1262
Cdd:cd00200  152 SSSQDGTIKLWDLR-----------TGKCVATLTGHTGE-------------VNS---------------VAFSPDGEKL 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1263 VTKADERVVELYDLQQMHSIDTVGLDLNSVLDtvrCDMDTLRYLLLSSeGKTQQLRVIDVSDGRIINEIS 1332
Cdd:cd00200  193 LSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS---VAFSPDGYLLASG-SEDGTIRVWDLRTGECVQTLS 258
WD40 COG2319
WD40 repeat [General function prediction only];
837-1199 5.34e-04

WD40 repeat [General function prediction only];


Pssm-ID: 225201  Cd Length: 466  Bit Score: 44.69  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  837 LARFKSPILQVSSSQDGTKIAVL-QDNSRIVFVIDPKSMTVN--GSFECESVVQRVLMNAAGTHLLIAVE--DGKVLYQA 911
Cdd:COG2319   61 LRGHEDSITSIAFSPDGELLLSGsSDGTIKLWDLDNGEKLIKslEGLHDSSVSKLALSSPDGNSILLASSslDGTVKLWD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  912 LSDP-KDRTALLDTPSDCTQLQFG-ARDSIAYVGTLDGLLK-YDLRSGRLLAR-CKTEFRCDAIVPSKDGNVLYISGRQD 987
Cdd:COG2319  141 LSTPgKLIRTLEGHSESVTSLAFSpDGKLLASGSSLDGTIKlWDLRTGKPLSTlAGHTDPVSSLAFSPDGGLLIASGSSD 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  988 R--IDW---GGLKLVGTIKGNgLSLQANLAAKRGFYLERVDAERFIVEKTMINDGALSWPLATDTTGDLILYLQPAENRM 1062
Cdd:COG2319  221 GtiRLWdlsTGKLLRSTLSGH-SDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLSVAFSPDGKLL 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1063 VLNIAD--VAHPPIELMQLGDPLF------------VNPSFPPVAIGTYEDfivnyvgNTVSISNWRDNRDSVSFPTNSQ 1128
Cdd:COG2319  300 ASGSSDgtVRLWDLETGKLLSSLTlkghegpvsslsFSPDGSLLVSGGSDD-------GTIRLWDLRTGKPLKTLEGHSN 372
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32476927 1129 VRSVCWASAGRIIVSGHEDGTVRVHHP--FSNAYEEAVVERTVTNPAIDSGQRYLACLNSDKKLGLLDLRSYE 1199
Cdd:COG2319  373 VLSVSFSPDGRVVSSGSTDGTVRLWDLstGSLLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSL 445
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1620-1808 4.66e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533  Cd Length: 291  Bit Score: 40.98  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1620 DSWRWWGTIANRLFEEQRYADSLDAsLNVLVSLGKEKEESDNYVVtlaniAKCQSKLGEFQKARTCLTNALAARDSIgwt 1699
Cdd:COG0457   93 NLAEALLNLGLLLEALGKYEEALEL-LEKALALDPDPDLAEALLA-----LGALYELGDYEEALELYEKALELDPEL--- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927 1700 DLRVQLLFELATIDADAGQPEEFFENAEAFLEKTAPRKLELWssystlsIRLAREYRLKGRHDKAVVVVGKILDDVKSGA 1779
Cdd:COG0457  164 NELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEAL-------LNLGLLYLKLGKYEEALEYYEKALELDPDNA 236
                        170       180
                 ....*....|....*....|....*....
gi 32476927 1780 gglsdKKLLEILLCLHAGKDFANLIDVYQ 1808
Cdd:COG0457  237 -----EALYNLALLLLELGRYEEALEALE 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
383-675 4.04e-91

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: 299.50  E-value: 4.04e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLtpDDQLPFYA 462
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGE--DDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHhldrtaseraKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAK 542
Cdd:cd14014   79 MEYVEGGSLADLLRER----------GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  543 RIGDEEpdqsqkrdvegksddsgfdQTRAGTRLGSPGYMAPEQASGRISDhgAHTDIYGLGATLYELIAGDLPFKASSTA 622
Cdd:cd14014  149 ALGDSG-------------------LTQTGSVLGTPAYMAPEQARGGPVD--PRSDIYSLGVVLYELLTGRPPFDGDSPA 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32476927  623 SLMEAIQHQSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQN 675
Cdd:cd14014  208 AVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
pknD PRK13184
serine/threonine-protein kinase; Reviewed
383-703 6.72e-52

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 199.61  E-value: 6.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHPNIIPVYELglTPDDQLPFYA 462
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI--CSDGDPVYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   463 MRFVGHKTLHDAIRH-HHLDRTASERAKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLA 541
Cdd:PRK13184   81 MPYIEGYTLKSLLKSvWQKESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   542 KRIGDEEPDQSqkrDVEGKSDDSGFDQ-TRAGTRLGSPGYMAPEQASGriSDHGAHTDIYGLGATLYELIAGDLPFKASS 620
Cdd:PRK13184  161 IFKKLEEEDLL---DIDVDERNICYSSmTIPGKIVGTPDYMAPERLLG--VPASESTDIYALGVILYQMLTLSFPYRRKK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927   621 TASLMEAiQHQSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQNWLADEP----IAVLPdnllrasqra 696
Cdd:PRK13184  236 GRKISYR-DVILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSPewtvKATLM---------- 304

                  ....*..
gi 32476927   697 IRKRPSW 703
Cdd:PRK13184  305 TKKKSCW 311
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
392-671 2.81e-45

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 167.71  E-value: 2.81e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     392 TGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPmaIERFLREARITGRLQHPNIIPVYELGLTPDDqlpFY-AMRFVGHKT 470
Cdd:smart00220    9 EGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDK---LYlVMEYCEGGD 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     471 LHDAIRHHhldRTASERAKKVHFRELLQsfvsvckAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIGDEEpd 550
Cdd:smart00220   84 LFDLLKKR---GRLSEDEARFYLRQILS-------ALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927     551 qsqkrdvegksddsgfdqtRAGTRLGSPGYMAPEQASGRisDHGAHTDIYGLGATLYELIAGDLPFKASSTASLMEAIQH 630
Cdd:smart00220  152 -------------------KLTTFVGTPEYMAPEVLLGK--GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG 210
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 32476927     631 QSIPSIAESNKQVPAALVAICGKAMEKLPADRYASAEALAD 671
Cdd:smart00220  211 KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
384-741 5.10e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 159.14  E-value: 5.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  384 YRLTRTHQTGGLGVVSVAEDtvlNRNVAIKQLKGNRAIDPMAIERFLREARITGRLQHP-NIIPVYELGltPDDQLPFYA 462
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFF--QDEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHHLDRTASERAKKVHFRELlqsfvsvCKAVAYAHSEGIMHRDIKPANIMLG-DYGEVILLDWGLA 541
Cdd:COG0515   77 MEYVDGGSLEDLLKKIGRKGPLSESEALFILAQI-------LSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  542 KRIGDEepdqsqkrdvegksDDSGFDQTRAGTRLGSPGYMAPEQASGRISDH-GAHTDIYGLGATLYELIAGDLPFKASS 620
Cdd:COG0515  150 KLLPDP--------------GSTSSIPALPSTSVGTPGYMAPEVLLGLSLAYaSSSSDIWSLGITLYELLTGLPPFEGEK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  621 ----TASLMEAIQHQSIPSIA-----ESNKQVPAALVAICGKAMEKLPADRYASAEALADDIQNWLADEPIAVLPDNLLR 691
Cdd:COG0515  216 nssaTSQTLKIILELPTPSLAsplspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPD 295
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 32476927  692 ASQRAIRKRPSWVSGTIAALAVGVLTVTTGLFFVNKEKNLKNESLTRESE 741
Cdd:COG0515  296 DSAPLRLSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSP 345
Pkinase pfam00069
Protein kinase domain;
393-672 5.85e-39

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 149.29  E-value: 5.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    393 GGLGVVSVAEDTVLNRNVAIKQLKgNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLTPDDqlpFY-AMRFVGHKTL 471
Cdd:pfam00069   10 GSFGTVYKAKHRDTGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN---LYlVLEYVEGGSL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    472 HDAIRHHhldRTASERAKKVHFRELLQsfvsvckAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIgdeepdq 551
Cdd:pfam00069   86 FDLLSEK---GAFSEREAKFIMKQILE-------GLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQL------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927    552 sqkrdvegkSDDSGFDqtragTRLGSPGYMAPEQASGRisDHGAHTDIYGLGATLYELIAGDLPFKASSTASLMEAIQHQ 631
Cdd:pfam00069  149 ---------NSGSSLT-----SFVGTPWYMAPEVLRGN--PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQ 212
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 32476927    632 SIPSiaESNKQVPAALVAICGKAMEKLPADRYASAEALADD 672
Cdd:pfam00069  213 DFDS--PRPSSISEEAKDLLKKLLKKDPSKRLTATEALQHP 251
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
393-609 2.67e-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: 134.32  E-value: 2.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  393 GGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPmaIERFLREARITGRLQHPNIIPVYELGLTPDdqlPFY-AMRFVGHKTL 471
Cdd:cd00180    4 GSFGKVYKARDKETGKKVAVKVIPKEKLKKL--LEELLREIEILKKLNHPNIVKLYDVFETEN---FLYlVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  472 HDAIRhhhldrtasERAKKVHFRELLQSFVSVCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIGDEEpdq 551
Cdd:cd00180   79 KDLLK---------ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD--- 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32476927  552 sqkrdvegksddsgfDQTRAGTRLGSPGYMAPEQASGRisDHGAHTDIYGLGATLYEL 609
Cdd:cd00180  147 ---------------SLLKTTGGTTPPYYAPPELLGGR--YYGPKVDIWSLGVILYEL 187
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
383-620 1.32e-32

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: 130.72  E-value: 1.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKGNRAIDPMaIERFLREARITGRLQHPNIIPVYELGLTPDDQlpFYA 462
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEI-EEKIKREIEIMKLLNHPNIIKLYEVIETENKI--YLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  463 MRFVGHKTLHDAIRHHhlDRTASERAKKVhFRELlqsfvsvCKAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAK 542
Cdd:cd14003   78 MEYASGGELFDYIVNN--GRLSEDEARRF-FQQL-------ISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32476927  543 RIGDEEpdqsqkrdvegksddsgfdqtRAGTRLGSPGYMAPEQASGRISDhGAHTDIYGLGATLYELIAGDLPFKASS 620
Cdd:cd14003  148 EFRGGS---------------------LLKTFCGTPAYAAPEVLLGRKYD-GPKADVWSLGVILYAMLTGYLPFDDDN 203
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
393-669 9.72e-32

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692  Cd Length: 254  Bit Score: 128.09  E-value: 9.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  393 GGLGVVSVAEDTVLNRNVAIKQLKGNRAIDpmaIERFLREARITGRLQHPNIIPVYELGLTPDDqlPFYAMRFVGHKTLH 472
Cdd:cd05122   11 GGFGVVYKARHKKTGQIVAIKKINLESKEK---KESILNEIAILKKCKHPNIVKYYGSYLKKDE--LWIVMEFCSGGSLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  473 DAIRHHHldRTASERAKKVHFRELLQsfvsvckAVAYAHSEGIMHRDIKPANIMLGDYGEVILLDWGLAKRIGDEEPDQs 552
Cdd:cd05122   86 DLLKNTN--KTLTEQQIAYVCKEVLK-------GLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRN- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  553 qkrdvegksddsgfdqtragTRLGSPGYMAPEQASGriSDHGAHTDIYGLGATLYELIAGDLPFKASSTASLMEAIQHQS 632
Cdd:cd05122  156 --------------------TFVGTPYWMAPEVIQG--KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNG 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 32476927  633 IPSIaESNKQVPAALVAICGKAMEKLPADRyASAEAL 669
Cdd:cd05122  214 PPGL-RNPKKWSKEFKDFLKKCLQKDPEKR-PTAEQL 248
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
383-629 2.03e-30

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687  Cd Length: 258  Bit Score: 124.51  E-value: 2.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32476927  383 RYRLTRTHQTGGLGVVSVAEDTVLNRNVAIKQLKgNRAIDPMAIERFLREARITGRLQHPNIIPVYELGLTPDDqlpFY- 461
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIID-KKKLKSEDE