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Conserved domains on  [gi|6753164|ref|NP_033869|]
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branched-chain alpha-ketoacid dehydrogenase kinase precursor [Mus musculus]

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

Graphical summary

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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 1.26e-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: 268.44  E-value: 1.26e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  306 DIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRinplfghLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929  81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                       170
                ....*....|....*.
gi 6753164  386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929 154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 6.16e-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: 189.25  E-value: 6.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164     69 RLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164    149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------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 1.26e-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: 268.44  E-value: 1.26e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  306 DIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRinplfghLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929  81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                       170
                ....*....|....*.
gi 6753164  386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929 154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 6.16e-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: 189.25  E-value: 6.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164     69 RLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164    149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------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 4.36e-17

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.53  E-value: 4.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164     266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQdpri 345
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753164     346 nplfghldmhsggqsgpMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:smart00387  71 -----------------IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 266-401 2.01e-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: 66.24  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164    266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDiDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQdpri 345
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKA--------GEITVTLSEGG-ELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753164    346 nplfghldmhsggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:pfam02518  69 ------------------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
224-400 3.32e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 64.16  E-value: 3.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  224 RLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFI---PMPLDYILPELLKNAMRATMESHldtpynvpDVVI 300
Cdd:COG0642 181 PVDLAELLEEVVELFRPLAEEK-----GIELELDLPDDLPTVrgdPDRLRQVLLNLLSNAIKYTPEGG--------TVTV 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  301 TIANNDIDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDprinplfghldmhsggqsgpmHGFGFGLPTSRAYAEYL 380
Cdd:COG0642 248 SVRREGDRVRISVEDTGPGIPPEDLERIFE-PFFRTDPSRRG---------------------GGTGLGLAIVKRIVELH 305

                       170       180
                ....*....|....*....|
gi 6753164  381 GGSLQLQSLQGIGTDVYLRL 400
Cdd:COG0642 306 GGTIEVESEPGKGTTFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
251-400 2.99e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 52.72  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   251 RVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHldtpynvpdVVITIANNDIDLIIRISDRGGGIAHKDLDRVmd 330
Cdd:PRK15347 496 RTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG---------IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQI-- 564

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   331 yhFTTaeastqdprinplFGHLDMHSGGQsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK15347 565 --FTP-------------FYQADTHSQGT-------GLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVL 612
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 226-401 1.26e-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: 268.44  E-value: 1.26e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  226 SPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANN 305
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIKVTVAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  306 DIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRinplfghLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQ 385
Cdd:cd16929  81 DEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDF-------SDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLD 153

                       170
                ....*....|....*.
gi 6753164  386 LQSLQGIGTDVYLRLR 401
Cdd:cd16929 154 LQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 69-222 6.16e-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: 189.25  E-value: 6.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164     69 RLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQaDE 148
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILE-DN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164    149 AQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKlVRYFLDKTLTSRLGIRMLATHHLALHE------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 4.36e-17

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.53  E-value: 4.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164     266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQdpri 345
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753164     346 nplfghldmhsggqsgpMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:smart00387  71 -----------------IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 266-401 2.01e-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: 66.24  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164    266 PMPLDYILPELLKNAMRATMEShldtpynvPDVVITIANNDiDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQdpri 345
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKA--------GEITVTLSEGG-ELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6753164    346 nplfghldmhsggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLR 401
Cdd:pfam02518  69 ------------------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
224-400 3.32e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 64.16  E-value: 3.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  224 RLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFI---PMPLDYILPELLKNAMRATMESHldtpynvpDVVI 300
Cdd:COG0642 181 PVDLAELLEEVVELFRPLAEEK-----GIELELDLPDDLPTVrgdPDRLRQVLLNLLSNAIKYTPEGG--------TVTV 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  301 TIANNDIDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDprinplfghldmhsggqsgpmHGFGFGLPTSRAYAEYL 380
Cdd:COG0642 248 SVRREGDRVRISVEDTGPGIPPEDLERIFE-PFFRTDPSRRG---------------------GGTGLGLAIVKRIVELH 305

                       170       180
                ....*....|....*....|
gi 6753164  381 GGSLQLQSLQGIGTDVYLRL 400
Cdd:COG0642 306 GGTIEVESEPGKGTTFTVTL 325
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 272-400 4.47e-08

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 54.85  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  272 ILPELLKNAMRATMESHLDTPYnvpdVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAstqdprinplfgh 351
Cdd:COG3290 285 ILGNLLDNAIEAVEKLPEEERR----VELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLG------------- 347

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6753164  352 ldmhsggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG3290 348 ------------EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 276-400 7.15e-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: 7.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRAtMESHldtpynvPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEastqdprinplfghldmh 355
Cdd:COG5000 325 LLKNAIEA-IEEG-------GEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP------------------ 378

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6753164  356 sggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5000 379 --------KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
223-400 8.80e-08

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 52.60  E-value: 8.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  223 TRLSPKKIIEKWVDFARRLCEHKygnapRVRINGHVAARFPFIPMP---LDYILPELLKNAMRATMEShldtpynvPDVV 299
Cdd:COG2205  89 EPVDLAELLEEAVEELRPLAEEK-----GIRLELDLPPELPLVYADpelLEQVLANLLDNAIKYSPPG--------GTIT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  300 ITIANNDIDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQDPrinplfghldmhsggqsgpmhGFGFGLPTSRAYAEY 379
Cdd:COG2205 156 ISARREGDGVRISVSDNGPGIPEEELERIFE-RFYRGDNSRGEG---------------------GTGLGLAIVKRIVEA 213

                       170       180
                ....*....|....*....|.
gi 6753164  380 LGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG2205 214 HGGTIWVESEPGGGTTFTVTL 234
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 272-400 2.75e-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: 2.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  272 ILPELLKNAMRATmeshLDTPYNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprinplfgh 351
Cdd:cd16915   4 IVGNLIDNALDAL----AATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQG------------ 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6753164  352 ldmhsggqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:cd16915  68 -------------ERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
PRK15347 PRK15347
two component system sensor kinase;
251-400 2.99e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 52.72  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   251 RVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHldtpynvpdVVITIANNDIDLIIRISDRGGGIAHKDLDRVmd 330
Cdd:PRK15347 496 RTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG---------IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQI-- 564

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   331 yhFTTaeastqdprinplFGHLDMHSGGQsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK15347 565 --FTP-------------FYQADTHSQGT-------GLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVL 612
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 276-400 2.72e-06

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 49.03  E-value: 2.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRAtMESHLDtpynvPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprinplfghldmh 355
Cdd:COG4191 264 LLINAIDA-MEEGEG-----GRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVG---------------- 321

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6753164  356 sggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 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 1.23e-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: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  272 ILPELLKNAmratmeshLDTPYNVPDVVITIANN--DIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAStqdprinplf 349
Cdd:cd16976   4 VLMNLLQNA--------LDAMGKVENPRIRIAARrlGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVG---------- 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6753164  350 ghldmhsggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIG 393
Cdd:cd16976  66 --------------KGTGLGLSISYGIVEEHGGRLSVANEEGAG 95
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
276-400 5.86e-05

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 44.93  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRATmeshldtpynvPD---VVITIANNDIDLIIRISDRGGGIAHKDLDRVMDyHFTTAEAStqdprinplfghl 352
Cdd:COG5002 289 LLDNAIKYT-----------PEggtITVSLREEDDQVRISVRDTGIGIPEEDLPRIFE-RFYRVDKS------------- 343

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 6753164  353 dmhsggQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5002 344 ------RSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 272-400 7.60e-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: 7.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  272 ILPELLKNAMRATMESHldtpynvpdVVITIA-----NNDIDLIIRISDRGGGIAHKDLDRVMDyHFTTAEASTQdprin 346
Cdd:cd16922   4 ILLNLLGNAIKFTEEGE---------VTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQARLFE-PFSQADSSTT----- 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6753164  347 plfghldmhsgGQSGpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:cd16922  69 -----------RKYG---GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTL 108
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 276-400 1.04e-04

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: 44.34  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRAtMEshldtpyNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprinplfghldmh 355
Cdd:COG5805 403 LIKNAIEA-MP-------NGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEKGT--------------- 459

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6753164  356 sggqsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5805 460 -----------GLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITL 493
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
228-402 2.88e-04

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 43.13  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   228 KKIIEKWVDFARR---------LCEHKYGNAP--RVRINGHVAARFPFIPMP---------LDYILPELLKNA-----MR 282
Cdd:PRK13837 500 RLIIDQILAFGRKgerntkpfdLSELVTEIAPllRVSLPPGVELDFDQDQEPavvegnpaeLQQVLMNLCSNAaqamdGA 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   283 ATMESHLDTPYNVPDVVI---TIANNDIDLIiRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprinplfghldmhsggq 359
Cdd:PRK13837 580 GRVDISLSRAKLRAPKVLshgVLPPGRYVLL-RVSDTGAGIDEAVLPHIFEPFFTTRAGGT------------------- 639

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6753164   360 sgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGT--DVYLRLRH 402
Cdd:PRK13837 640 -------GLGLATVHGIVSAHAGYIDVQSTVGRGTrfDVYLPPSS 677
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 276-400 4.32e-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: 42.27  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRAtMESHldtpynvpdVVITIANNDID---LIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprinplfghl 352
Cdd:COG5809 387 LLKNAIEA-MPEG---------GNITIETKAEDddkVVISVTDEGCGIPEERLKKLGEPFYTTKEKGT------------ 444

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 6753164  353 dmhsggqsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:COG5809 445 --------------GLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 269-388 6.18e-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: 39.42  E-value: 6.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  269 LDYILPELLKNAMRATMESHLdtpynvpdVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEAstqdprinpl 348
Cdd:cd16947  21 LQRILKNLISNAIKYGSDGKF--------LGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDS---------- 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6753164  349 fghldmhsggQSGPMHGFGFGLPTSRAYAEYLGGSLQLQS 388
Cdd:cd16947  83 ----------RNSAKQGNGLGLTITKRLAESMGGSIYVNS 112
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
229-406 8.96e-04

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.49  E-value: 8.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   229 KIIEKWVDFAR-------------------RLCEHKYGNApRVRINGHVAARFPFIpmpldYILPELLK--------NAM 281
Cdd:PRK11360 440 KVIDQLLEFSRpresqwqpvslnalveevlQLFQTAGVQA-RVDFETELDNELPPI-----WADPELLKqvllniliNAV 513

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   282 RATMEshldtpynvpDVVITIA---NNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdprinplfghldmhsgg 358
Cdd:PRK11360 514 QAISA----------RGKIRIRtwqYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAKGT------------------ 565

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6753164   359 qsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGT--DVYLRLRHIDGR 406
Cdd:PRK11360 566 --------GLGLALSQRIINAHGGDIEVESEPGVGTtfTLYLPINPQGNQ 607
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 273-394 1.06e-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: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  273 LPELLKNAMRATMESHLDTPYNVPDVVITIANNDID-LIIRISDRGGGIAHKDLDRVMDYHFTTAEAstqdprinplfgh 351
Cdd:cd16920   1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPADDRaVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------------- 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6753164  352 ldmhsggqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGT 394
Cdd:cd16920  68 -------------GLGMGLSICRSIIEAHGGRLSVESPAGGGA 97
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
276-409 1.42e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 40.60  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  276 LLKNAMRATMES---HLDTpYNVPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEastqdprinplfghl 352
Cdd:COG3852 252 LVRNAAEAMPEGgtiTIRT-RVERQVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKE--------------- 315

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6753164  353 dmhsggqsgpmHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREES 409
Cdd:COG3852 316 -----------KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 269-334 1.43e-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: 1.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6753164  269 LDYILPELLKNAMRATMESHldtpynvpDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFT 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 1.62e-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: 37.79  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164  266 PMPLDYILPELLKNAMRAtMESHldtpynvPDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTqdpri 345
Cdd:cd16943   1 PSQLNQVLLNLLVNAAQA-MEGR-------GRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE----- 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6753164  346 nplfghldmhsggqsgpmhGFGFGLPTSRAYAEYLGGSLQLQSLQGIGT 394
Cdd:cd16943  68 -------------------GTGLGLSLSYRIIQKHGGTIRVASVPGGGT 97
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
258-400 1.73e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 40.54  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   258 VAARFPFIPMPLDYILPELLK---NAMRATMEshldtpynvpDVVITIA--NNDIDLIIRISDRGGGIAHKDLDRVMDYH 332
Cdd:PRK10364 335 ANDTLPEIQADPDRLTQVLLNlylNAIQAIGQ----------HGVISVTasESGAGVKISVTDSGKGIAADQLEAIFTPY 404

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6753164   333 FTTAEASTqdprinplfghldmhsggqsgpmhgfGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRL 400
Cdd:PRK10364 405 FTTKAEGT--------------------------GLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWL 446
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 272-409 8.91e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 38.36  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   272 ILPELLKNAMRAT--MESHldtpynvpDVVITIANNDIDLIIRISDRGGGIAHKDLDRVMDYHFTTaeastqdprinplf 349
Cdd:PRK11086 437 ILGNLIENALEAVggEEGG--------EISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYST-------------- 494

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753164   350 ghldmhsggqSGPMHGFGFGLptSRAYAEYLGGSLQLQSLQGIGTDVYLRLRhIDGREES 409
Cdd:PRK11086 495 ----------KGSNRGVGLYL--VKQSVENLGGSIAVESEPGVGTQFFVQIP-WDGERSN 541
 
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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