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Conserved domains on  [gi|633578414|gb|KDD50011|]
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hypothetical protein L529_0011 [Bordetella bronchiseptica MBORD901]

Protein Classification

serine/threonine-protein kinase( domain architecture ID 1904506)

serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Bacillus subtilis serine/threonine-protein kinase YabT

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0004674|GO:0005524|GO:0006468
PubMed:  3291115|19614568
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPS1 super family cl43163
Serine/threonine protein kinase [Signal transduction mechanisms];
100-470 6.44e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0515:

Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 76.98  E-value: 6.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 100 GGVPQARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGRAHLL------ALNGAAQGEAALPA--PGYAPFELYV 171
Cdd:COG0515  102 GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIdfgiarALGGATLTQTGTVVgtPGYMAPEQAR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 172 EDPAwprGPWTDIYALSAVAHSLITGRRPPAAPE-----RSVNDGYQPLAQRDLPKYDNDFLRAIDAGLAVRPQARPHTL 246
Cdd:COG0515  182 GEPV---DPRSDVYSLGVTLYELLTGRPPFDGDSpaellRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSA 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 247 EAFVDSLKFPEPEPPAEAMAPQPSEPPPRDEVRDEEPVRQRPAVRSilfAILLALATLGVAVYWWQRLTGTPSGVITSSE 326
Cdd:COG0515  259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA---AAAAAAAAAAAAAAAAAAPAAAAAAAAAAAA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 327 RVTTPGATATPSDSREAEPPAAGTAPPQGGDAGSADTSGAAPPAQAQAGPDAAPAPDVAPEDAATDAQAESEAAATPAPA 406
Cdd:COG0515  336 LAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAA 415
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 633578414 407 VARVTVRINVQPWGEIWINGVRRGVSPPMKELRLAPGRYSVVVRNADLPPYRATLEVKAGQPAR 470
Cdd:COG0515  416 AAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAAL 479
 
Name Accession Description Interval E-value
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
100-470 6.44e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 76.98  E-value: 6.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 100 GGVPQARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGRAHLL------ALNGAAQGEAALPA--PGYAPFELYV 171
Cdd:COG0515  102 GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIdfgiarALGGATLTQTGTVVgtPGYMAPEQAR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 172 EDPAwprGPWTDIYALSAVAHSLITGRRPPAAPE-----RSVNDGYQPLAQRDLPKYDNDFLRAIDAGLAVRPQARPHTL 246
Cdd:COG0515  182 GEPV---DPRSDVYSLGVTLYELLTGRPPFDGDSpaellRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSA 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 247 EAFVDSLKFPEPEPPAEAMAPQPSEPPPRDEVRDEEPVRQRPAVRSilfAILLALATLGVAVYWWQRLTGTPSGVITSSE 326
Cdd:COG0515  259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA---AAAAAAAAAAAAAAAAAAPAAAAAAAAAAAA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 327 RVTTPGATATPSDSREAEPPAAGTAPPQGGDAGSADTSGAAPPAQAQAGPDAAPAPDVAPEDAATDAQAESEAAATPAPA 406
Cdd:COG0515  336 LAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAA 415
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 633578414 407 VARVTVRINVQPWGEIWINGVRRGVSPPMKELRLAPGRYSVVVRNADLPPYRATLEVKAGQPAR 470
Cdd:COG0515  416 AAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAAL 479
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
100-254 1.13e-10

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 61.83  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 100 GGVPQARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGR--------AHLLALNGAAQGEAALPAPGYAPFELYV 171
Cdd:cd14014   95 GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRvkltdfgiARALGDSGLTQTGSVLGTPAYMAPEQAR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 172 EDPAwprGPWTDIYALSAVAHSLITGRRPPAAPE------RSVNDGYQPLAQRDlPKYDNDFLRAIDAGLAVRPQARPHT 245
Cdd:cd14014  175 GGPV---DPRSDIYSLGVVLYELLTGRPPFDGDSpaavlaKHLQEAPPPPSPLN-PDVPPALDAIILRALAKDPEERPQS 250

                 ....*....
gi 633578414 246 LEAFVDSLK 254
Cdd:cd14014  251 AAELLAALR 259
 
Name Accession Description Interval E-value
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
100-470 6.44e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 76.98  E-value: 6.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 100 GGVPQARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGRAHLL------ALNGAAQGEAALPA--PGYAPFELYV 171
Cdd:COG0515  102 GPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIdfgiarALGGATLTQTGTVVgtPGYMAPEQAR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 172 EDPAwprGPWTDIYALSAVAHSLITGRRPPAAPE-----RSVNDGYQPLAQRDLPKYDNDFLRAIDAGLAVRPQARPHTL 246
Cdd:COG0515  182 GEPV---DPRSDVYSLGVTLYELLTGRPPFDGDSpaellRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSA 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 247 EAFVDSLKFPEPEPPAEAMAPQPSEPPPRDEVRDEEPVRQRPAVRSilfAILLALATLGVAVYWWQRLTGTPSGVITSSE 326
Cdd:COG0515  259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA---AAAAAAAAAAAAAAAAAAPAAAAAAAAAAAA 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 327 RVTTPGATATPSDSREAEPPAAGTAPPQGGDAGSADTSGAAPPAQAQAGPDAAPAPDVAPEDAATDAQAESEAAATPAPA 406
Cdd:COG0515  336 LAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAA 415
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 633578414 407 VARVTVRINVQPWGEIWINGVRRGVSPPMKELRLAPGRYSVVVRNADLPPYRATLEVKAGQPAR 470
Cdd:COG0515  416 AAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAAL 479
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
100-254 1.13e-10

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 61.83  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 100 GGVPQARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGR--------AHLLALNGAAQGEAALPAPGYAPFELYV 171
Cdd:cd14014   95 GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRvkltdfgiARALGDSGLTQTGSVLGTPAYMAPEQAR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 172 EDPAwprGPWTDIYALSAVAHSLITGRRPPAAPE------RSVNDGYQPLAQRDlPKYDNDFLRAIDAGLAVRPQARPHT 245
Cdd:cd14014  175 GGPV---DPRSDIYSLGVVLYELLTGRPPFDGDSpaavlaKHLQEAPPPPSPLN-PDVPPALDAIILRALAKDPEERPQS 250

                 ....*....
gi 633578414 246 LEAFVDSLK 254
Cdd:cd14014  251 AAELLAALR 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
104-251 2.51e-06

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 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: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 48.79  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 104 QARIKRLLGELVPQLASVHEQGHICGDITVDSVGLDESGRAHLLALNGAAQGEAALPA------PGY-AP--FELYVEDP 174
Cdd:cd05578   99 EETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLAtstsgtKPYmAPevFMRAGYSF 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633578414 175 AwprgpwTDIYALSAVAHSLITGRRPPAAPERSVNDGY---QPLAQRDLPKYDN-DFLRAIDAGLAVRPQARPHTLEAFV 250
Cdd:cd05578  179 A------VDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIrakFETASVLYPAGWSeEAIDLINKLLERDPQKRLGDLSDLK 252

                 .
gi 633578414 251 D 251
Cdd:cd05578  253 N 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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