NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|171906589|ref|NP_005872|]
View 

branched-chain alpha-ketoacid dehydrogenase kinase isoform a precursor [Homo sapiens]

Protein Classification

PDK/BCKDK family protein kinase( domain architecture ID 13768654)

PDK/BCKDK family protein kinase contains a histidine kinase-like ATPase domain and catalyzes the phosphorylation of protein substrates, such as branched-chain alpha-ketoacid dehydrogenase (BCKD) kinase that catalyzes the phosphorylation and inactivation of the BCKD complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways

CATH:  3.30.565.10|1.20.140.20
EC:  2.7.11.-
Gene Ontology:  GO:0004672|GO:0005524|GO:0006468
PubMed:  10339418|10637609

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 226-401 1.92e-89

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


:

Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 268.05  E-value: 1.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929    1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 306 DVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRisplfghLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929   81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                        170
                 ....*....|....*.
gi 171906589 386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929  154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 4.28e-59

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


:

Pssm-ID: 463093  Cd Length: 158  Bit Score: 189.64  E-value: 4.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589   69 RLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589  149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------DKPDFVGIIC 222
Cdd:pfam10436  80 EKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEE-IQSFLDRFLRSRIGIRLLAEQHIALTEqsnnpsHPPDYVGIID 158
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 226-401 1.92e-89

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 268.05  E-value: 1.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929    1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 306 DVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRisplfghLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929   81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                        170
                 ....*....|....*.
gi 171906589 386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929  154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 4.28e-59

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


Pssm-ID: 463093  Cd Length: 158  Bit Score: 189.64  E-value: 4.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589   69 RLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589  149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------DKPDFVGIIC 222
Cdd:pfam10436  80 EKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEE-IQSFLDRFLRSRIGIRLLAEQHIALTEqsnnpsHPPDYVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 266-401 2.82e-17

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.92  E-value: 2.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589   266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQdpri 345
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 171906589   346 splfghldmhsgaqsgpMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:smart00387  71 -----------------IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 266-401 1.43e-13

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 66.62  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589  266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIaNNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQdpri 345
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKA--------GEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 171906589  346 splfghldmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:pfam02518  69 ------------------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
224-400 2.85e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 64.16  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 224 RLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFI---PMPLDYILPELLKNAMRATMESHldtpynvpDVVI 300
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEK-----GIELELDLPDDLPTVrgdPDRLRQVLLNLLSNAIKYTPEGG--------TVTV 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 301 TIANNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDprisplfghldmhsgaqsgpmHGFGFGLPTSRAYAEYL 380
Cdd:COG0642  248 SVRREGDRVRISVEDTGPGIPPEDLERIFE-PFFRTDPSRRG---------------------GGTGLGLAIVKRIVELH 305

                        170       180
                 ....*....|....*....|
gi 171906589 381 GGSLQLQSLQGIGTDVYLRL 400
Cdd:COG0642  306 GGTIEVESEPGKGTTFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
251-400 4.67e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 51.95  E-value: 4.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 251 RVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHldtpynvpdVVITIANNDVDLIIRISDRGGGIAHKDLDRVmd 330
Cdd:PRK15347 496 RTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG---------IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQI-- 564

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 331 yhFTTaeastqdprisplFGHLDMHSGaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK15347 565 --FTP-------------FYQADTHSQ-------GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVL 612
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 226-401 1.92e-89

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 268.05  E-value: 1.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929    1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 306 DVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRisplfghLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929   81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                        170
                 ....*....|....*.
gi 171906589 386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929  154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 4.28e-59

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


Pssm-ID: 463093  Cd Length: 158  Bit Score: 189.64  E-value: 4.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589   69 RLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589  149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------DKPDFVGIIC 222
Cdd:pfam10436  80 EKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEE-IQSFLDRFLRSRIGIRLLAEQHIALTEqsnnpsHPPDYVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 266-401 2.82e-17

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.92  E-value: 2.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589   266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQdpri 345
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 171906589   346 splfghldmhsgaqsgpMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:smart00387  71 -----------------IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 266-401 1.43e-13

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 66.62  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589  266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIaNNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQdpri 345
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKA--------GEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 171906589  346 splfghldmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:pfam02518  69 ------------------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
224-400 2.85e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 64.16  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 224 RLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFI---PMPLDYILPELLKNAMRATMESHldtpynvpDVVI 300
Cdd:COG0642  181 PVDLAELLEEVVELFRPLAEEK-----GIELELDLPDDLPTVrgdPDRLRQVLLNLLSNAIKYTPEGG--------TVTV 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 301 TIANNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDprisplfghldmhsgaqsgpmHGFGFGLPTSRAYAEYL 380
Cdd:COG0642  248 SVRREGDRVRISVEDTGPGIPPEDLERIFE-PFFRTDPSRRG---------------------GGTGLGLAIVKRIVELH 305

                        170       180
                 ....*....|....*....|
gi 171906589 381 GGSLQLQSLQGIGTDVYLRL 400
Cdd:COG0642  306 GGTIEVESEPGKGTTFTVTL 325
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 272-400 5.34e-08

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 54.47  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 272 ILPELLKNAMRATMESHLDTPYnvpdVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAstqdprisplfgh 351
Cdd:COG3290  285 ILGNLLDNAIEAVEKLPEEERR----VELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLG------------- 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 171906589 352 ldmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG3290  348 ------------EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
223-400 6.02e-08

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 53.37  E-value: 6.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 223 TRLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFIPMP---LDYILPELLKNAMRATMEShldtpynvPDVV 299
Cdd:COG2205   89 EPVDLAELLEEAVEELRPLAEEK-----GIRLELDLPPELPLVYADpelLEQVLANLLDNAIKYSPPG--------GTIT 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 300 ITIANNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDPrisplfghldmhsgaqsgpmhGFGFGLPTSRAYAEY 379
Cdd:COG2205  156 ISARREGDGVRISVSDNGPGIPEEELERIFE-RFYRGDNSRGEG---------------------GTGLGLAIVKRIVEA 213

                        170       180
                 ....*....|....*....|.
gi 171906589 380 LGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG2205  214 HGGTIWVESEPGGGTTFTVTL 234
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 276-400 7.67e-08

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 54.20  E-value: 7.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRAtMESHldtpynvPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEastqdprisplfghldmh 355
Cdd:COG5000  325 LLKNAIEA-IEEG-------GEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP------------------ 378

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 171906589 356 sgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5000  379 --------KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 272-400 2.70e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 48.44  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 272 ILPELLKNAMRATmeshLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprisplfgh 351
Cdd:cd16915    4 IVGNLIDNALDAL----AATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQG------------ 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 171906589 352 ldmhsgaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:cd16915   68 -------------ERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
PRK15347 PRK15347
two component system sensor kinase;
251-400 4.67e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 51.95  E-value: 4.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 251 RVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHldtpynvpdVVITIANNDVDLIIRISDRGGGIAHKDLDRVmd 330
Cdd:PRK15347 496 RTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG---------IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQI-- 564

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 331 yhFTTaeastqdprisplFGHLDMHSGaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK15347 565 --FTP-------------FYQADTHSQ-------GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVL 612
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 276-400 6.15e-06

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 47.87  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRAtMESHLDtpynvPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprisplfghldmh 355
Cdd:COG4191  264 LLINAIDA-MEEGEG-----GRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVG---------------- 321

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 171906589 356 sgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG4191  322 --------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 272-393 1.52e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 43.60  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 272 ILPELLKNAmratmeshLDTPYNVPDVVITIANN--DVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprisplf 349
Cdd:cd16976    4 VLMNLLQNA--------LDAMGKVENPRIRIAARrlGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVG---------- 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 171906589 350 ghldmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIG 393
Cdd:cd16976   66 --------------KGTGLGLSISYGIVEEHGGRLSVANEEGAG 95
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
276-400 4.83e-05

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 45.31  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRATmeshldtpynvPD---VVITIANNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEAStqdprisplfghl 352
Cdd:COG5002  289 LLDNAIKYT-----------PEggtITVSLREEDDQVRISVRDTGIGIPEEDLPRIFE-RFYRVDKS------------- 343

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 171906589 353 dmhsgaQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5002  344 ------RSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 276-400 7.49e-05

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 44.72  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRAtMEshldtpyNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprisplfghldmh 355
Cdd:COG5805  403 LIKNAIEA-MP-------NGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEKGT--------------- 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 171906589 356 sgaqsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5805  460 -----------GLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITL 493
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 272-400 7.98e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 41.71  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 272 ILPELLKNAMRATMESHldtpynvpdVVITIA-----NNDVDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTqdpriS 346
Cdd:cd16922    4 ILLNLLGNAIKFTEEGE---------VTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQARLFE-PFSQADSST-----T 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 171906589 347 PLFGhldmhsgaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:cd16922   69 RKYG--------------GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTL 108
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 276-400 2.84e-04

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 43.04  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRAtMESHldtpynvpdVVITIANNDVD---LIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprisplfghl 352
Cdd:COG5809  387 LLKNAIEA-MPEG---------GNITIETKAEDddkVVISVTDEGCGIPEERLKKLGEPFYTTKEKGT------------ 444

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 171906589 353 dmhsgaqsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5809  445 --------------GLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
PRK13557 PRK13557
histidine kinase; Provisional
 311-398 3.83e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.74  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 311 IRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprisplfghldmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQ 390
Cdd:PRK13557 327 IAVTDTGSGMPPEILARVMDPFFTTKEEG------------------------KGTGLGLSMVYGFAKQSGGAVRIYSEV 382


                 ....*...
gi 171906589 391 GIGTDVYL 398
Cdd:PRK13557 383 GEGTTVRL 390
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 269-388 4.16e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 39.80  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 269 LDYILPELLKNAMRATMESHLdtpynvpdVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEastqdprispl 348
Cdd:cd16947   21 LQRILKNLISNAIKYGSDGKF--------LGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLED----------- 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 171906589 349 fghldmhsgAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQS 388
Cdd:cd16947   82 ---------SRNSAKQGNGLGLTITKRLAESMGGSIYVNS 112
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
229-406 9.69e-04

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.49  E-value: 9.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 229 KIIEKWVDFAR-------------------RLCEHKYGNApRVRINGHVAARFPFIpmpldYILPELLK--------NAM 281
Cdd:PRK11360 440 KVIDQLLEFSRpresqwqpvslnalveevlQLFQTAGVQA-RVDFETELDNELPPI-----WADPELLKqvllniliNAV 513

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 282 RATMEshldtpynvpDVVITIA---NNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprisplfghldmhsga 358
Cdd:PRK11360 514 QAISA----------RGKIRIRtwqYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAKGT------------------ 565

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 171906589 359 qsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGT--DVYLRLRHIDGR 406
Cdd:PRK11360 566 --------GLGLALSQRIINAHGGDIEVESEPGVGTtfTLYLPINPQGNQ 607
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
276-409 1.06e-03

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 40.99  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 276 LLKNAMRATMES---HLDTpYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEastqdprisplfghl 352
Cdd:COG3852  252 LVRNAAEAMPEGgtiTIRT-RVERQVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKE--------------- 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 171906589 353 dmhsgaqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREES 409
Cdd:COG3852  316 -----------KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 273-394 1.08e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 38.15  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 273 LPELLKNAMRATMESHLDTPYNVPDVVITIANNDVD-LIIRISDRGGGIAHKDLDRVMDYHFTTAEAstqdprisplfgh 351
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPADDRaVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------------- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 171906589 352 ldmhsgaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGT 394
Cdd:cd16920   68 -------------GLGMGLSICRSIIEAHGGRLSVESPAGGGA 97
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 269-334 1.27e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 38.04  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171906589 269 LDYILPELLKNAMRATMESHldtpynvpDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFT 334
Cdd:cd16948    6 LSFIIGQIVSNALKYSKQGG--------KIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFT 63
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 266-394 1.32e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 38.17  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 266 PMPLDYILPELLKNAMRAtMESHldtpynvPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdpri 345
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQA-MEGR-------GRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE----- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 171906589 346 splfghldmhsgaqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGT 394
Cdd:cd16943   68 -------------------GTGLGLSLSYRIIQKHGGTIRVASVPGGGT 97
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
258-400 1.56e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 40.54  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 258 VAARFPFIPMPLDYILPELLK---NAMRATMEshldtpynvpDVVITIANNDVD--LIIRISDRGGGIAHKDLDRVMDYH 332
Cdd:PRK10364 335 ANDTLPEIQADPDRLTQVLLNlylNAIQAIGQ----------HGVISVTASESGagVKISVTDSGKGIAADQLEAIFTPY 404

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171906589 333 FTTAeastqdprisplfghldmhsgAQsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK10364 405 FTTK---------------------AE-----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWL 446
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
228-402 2.64e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.05  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 228 KKIIEKWVDFARR---------LCEHKYGNAP--RVRINGHVAARFPFIPMP---------LDYILPELLKNA-----MR 282
Cdd:PRK13837 500 RLIIDQILAFGRKgerntkpfdLSELVTEIAPllRVSLPPGVELDFDQDQEPavvegnpaeLQQVLMNLCSNAaqamdGA 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171906589 283 ATMESHLDTPYNVPDVVI---TIANNDVDLIiRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprisplfghldmhsgaq 359
Cdd:PRK13837 580 GRVDISLSRAKLRAPKVLshgVLPPGRYVLL-RVSDTGAGIDEAVLPHIFEPFFTTRAGGT------------------- 639

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 171906589 360 sgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGT--DVYLRLRH 402
Cdd:PRK13837 640 -------GLGLATVHGIVSAHAGYIDVQSTVGRGTrfDVYLPPSS 677
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH