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Conserved domains on  [gi|17137298|ref|NP_477215|]
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pyruvate dehydrogenase kinase, isoform A [Drosophila melanogaster]

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

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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 ...
 197-366 2.90e-87

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: 262.28  E-value: 2.90e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 197 DLSDVVRDAYENARFLCDQYYLTSPALEIQQHSsepgdnlPIRTVYVPSHLYYMLFELFKNSMRAVVEHHGHDNnDTLPP 276
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP-------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDS-DDLPP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 277 LKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSK-------SDLHTVPLAGYGYGLPISRLYARYFHGDI 349
Cdd:cd16929  73 IKVTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDL 152

                       170
                ....*....|....*..
gi 17137298 350 VLLSCEGFGTDAIIYLK 366
Cdd:cd16929 153 DLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 32-193 8.88e-58

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: 186.17  E-value: 8.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298    32 PLSIKQFMDFGQNACEK---KSYIFLRKELPVRLANIMKEIALLPDNLLHTRSVSEVSSWYVKSFEDVLVYEKaePTHDN 108
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEkllKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPP--PILED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298   109 LQKFVADLDLIRNRHNDVVQTMAQGVIEMKeneggqvDAPTESSIQYFLDRLYMSRISIRMLINQHTLLFGG--NPHAGG 186
Cdd:pfam10436  79 NEKFTELLEEILDRHNDVVPTLAQGVLELK-------KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQsnNPSHPP 151


                  ....*..
gi 17137298   187 RHIGCLD 193
Cdd:pfam10436 152 DYVGIID 158
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 197-366 2.90e-87

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: 262.28  E-value: 2.90e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 197 DLSDVVRDAYENARFLCDQYYLTSPALEIQQHSsepgdnlPIRTVYVPSHLYYMLFELFKNSMRAVVEHHGHDNnDTLPP 276
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP-------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDS-DDLPP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 277 LKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSK-------SDLHTVPLAGYGYGLPISRLYARYFHGDI 349
Cdd:cd16929  73 IKVTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDL 152

                       170
                ....*....|....*..
gi 17137298 350 VLLSCEGFGTDAIIYLK 366
Cdd:cd16929 153 DLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 32-193 8.88e-58

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: 186.17  E-value: 8.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298    32 PLSIKQFMDFGQNACEK---KSYIFLRKELPVRLANIMKEIALLPDNLLHTRSVSEVSSWYVKSFEDVLVYEKaePTHDN 108
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEkllKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPP--PILED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298   109 LQKFVADLDLIRNRHNDVVQTMAQGVIEMKeneggqvDAPTESSIQYFLDRLYMSRISIRMLINQHTLLFGG--NPHAGG 186
Cdd:pfam10436  79 NEKFTELLEEILDRHNDVVPTLAQGVLELK-------KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQsnNPSHPP 151


                  ....*..
gi 17137298   187 RHIGCLD 193
Cdd:pfam10436 152 DYVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 244-366 1.48e-17

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 77.69  E-value: 1.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298    244 PSHLYYMLFELFKNSMRAVVEHhghdnndtlPPLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSdl 323
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG---------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI-- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17137298    324 htvplAGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLK 366
Cdd:smart00387  72 -----GGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 243-366 1.42e-12

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: 63.54  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298   243 VPSHLYYMLFELFKNSmravVEHHGHDnndtlPPLKVAIcKGKEDICVKISDQGGGIPRSQTDQLFKyMYSTAPQPSKSd 322
Cdd:pfam02518   2 DELRLRQVLSNLLDNA----LKHAAKA-----GEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17137298   323 lhtvplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLK 366
Cdd:pfam02518  70 -------GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
196-365 8.15e-12

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 64.54  E-value: 8.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 196 CDLSDVVRDAYENARFLCDQYYLTspaLEIQqhssEPGDNLPIRTVyvPSHLYYMLFELFKNSMRavvehHGHDNndtlP 275
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKGIR---LELD----LPPELPLVYAD--PELLEQVLANLLDNAIK-----YSPPG----G 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 276 PLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCE 355
Cdd:COG2205 153 TITISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG--------GTGLGLAIVKRIVEAHGGTIWVESEP 224

                       170
                ....*....|
gi 17137298 356 GFGTDAIIYL 365
Cdd:COG2205 225 GGGTTFTVTL 234
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 281-367 2.38e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 49.94  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298  281 ICKGKEDICVKISDQGGGIPRSQTDQLFKyMYSTAPQpSKSDLHTVplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTD 360
Cdd:PRK11091 424 RYEEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQVKD-SHGGKPAT---GTGIGLAVSKRLAQAMGGDITVTSEEGKGSC 498


                 ....*..
gi 17137298  361 AIIYLKA 367
Cdd:PRK11091 499 FTLTIHA 505
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 197-366 2.90e-87

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: 262.28  E-value: 2.90e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 197 DLSDVVRDAYENARFLCDQYYLTSPALEIQQHSsepgdnlPIRTVYVPSHLYYMLFELFKNSMRAVVEHHGHDNnDTLPP 276
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP-------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDS-DDLPP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 277 LKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSK-------SDLHTVPLAGYGYGLPISRLYARYFHGDI 349
Cdd:cd16929  73 IKVTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDL 152

                       170
                ....*....|....*..
gi 17137298 350 VLLSCEGFGTDAIIYLK 366
Cdd:cd16929 153 DLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 32-193 8.88e-58

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: 186.17  E-value: 8.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298    32 PLSIKQFMDFGQNACEK---KSYIFLRKELPVRLANIMKEIALLPDNLLHTRSVSEVSSWYVKSFEDVLVYEKaePTHDN 108
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEkllKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPP--PILED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298   109 LQKFVADLDLIRNRHNDVVQTMAQGVIEMKeneggqvDAPTESSIQYFLDRLYMSRISIRMLINQHTLLFGG--NPHAGG 186
Cdd:pfam10436  79 NEKFTELLEEILDRHNDVVPTLAQGVLELK-------KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQsnNPSHPP 151


                  ....*..
gi 17137298   187 RHIGCLD 193
Cdd:pfam10436 152 DYVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 244-366 1.48e-17

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 77.69  E-value: 1.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298    244 PSHLYYMLFELFKNSMRAVVEHhghdnndtlPPLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSdl 323
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG---------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI-- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 17137298    324 htvplAGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLK 366
Cdd:smart00387  72 -----GGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 243-366 1.42e-12

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: 63.54  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298   243 VPSHLYYMLFELFKNSmravVEHHGHDnndtlPPLKVAIcKGKEDICVKISDQGGGIPRSQTDQLFKyMYSTAPQPSKSd 322
Cdd:pfam02518   2 DELRLRQVLSNLLDNA----LKHAAKA-----GEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17137298   323 lhtvplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLK 366
Cdd:pfam02518  70 -------GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
196-365 8.15e-12

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 64.54  E-value: 8.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 196 CDLSDVVRDAYENARFLCDQYYLTspaLEIQqhssEPGDNLPIRTVyvPSHLYYMLFELFKNSMRavvehHGHDNndtlP 275
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKGIR---LELD----LPPELPLVYAD--PELLEQVLANLLDNAIK-----YSPPG----G 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 276 PLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCE 355
Cdd:COG2205 153 TITISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG--------GTGLGLAIVKRIVEAHGGTIWVESEP 224

                       170
                ....*....|
gi 17137298 356 GFGTDAIIYL 365
Cdd:COG2205 225 GGGTTFTVTL 234
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
197-365 2.98e-09

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 58.00  E-value: 2.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 197 DLSDVVRDAYENARFLCDQYYLTspaLEIQqhssEPGDNLPIRTVyvPSHLYYMLFELFKNSMRavvehHGHDNNdtlpP 276
Cdd:COG0642 183 DLAELLEEVVELFRPLAEEKGIE---LELD----LPDDLPTVRGD--PDRLRQVLLNLLSNAIK-----YTPEGG----T 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 277 LKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSKSdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCEG 356
Cdd:COG0642 245 VTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG--------GTGLGLAIVKRIVELHGGTIEVESEPG 316


                ....*....
gi 17137298 357 FGTDAIIYL 365
Cdd:COG0642 317 KGTTFTVTL 325
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 281-367 2.38e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 49.94  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298  281 ICKGKEDICVKISDQGGGIPRSQTDQLFKyMYSTAPQpSKSDLHTVplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTD 360
Cdd:PRK11091 424 RYEEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQVKD-SHGGKPAT---GTGIGLAVSKRLAQAMGGDITVTSEEGKGSC 498


                 ....*..
gi 17137298  361 AIIYLKA 367
Cdd:PRK11091 499 FTLTIHA 505
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 195-372 5.99e-06

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: 48.03  E-value: 5.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 195 ACDLSDVVRDAyenARFLCDQYYLTSPALEIQQHSSEP---GDNLPIRTVyvpshlyymLFELFKNSMRAVvEHHGHdnn 271
Cdd:COG5000 275 PVDLNELLREV---LALYEPALKEKDIRLELDLDPDLPevlADRDQLEQV---------LINLLKNAIEAI-EEGGE--- 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 272 dtlppLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQpsksdlhtvplaGYGYGLPISRLYARYFHGDIVL 351
Cdd:COG5000 339 -----IEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPK------------GTGLGLAIVKKIVEEHGGTIEL 401

                       170       180
                ....*....|....*....|.
gi 17137298 352 LSCEGFGTDAIIYLKALSDEA 372
Cdd:COG5000 402 ESRPGGGTTFTIRLPLAEEAE 422
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 195-365 7.06e-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: 7.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 195 ACDLSDVVRDAyenARFLcdQYYLTSPALEIQQhssEPGDNLPirTVYV-PSHLYYMLFELFKNSMRAVVEHHGhdnndt 273
Cdd:COG4191 214 PVDLNELIDEA---LELL--RPRLKARGIEVEL---DLPPDLP--PVLGdPGQLEQVLLNLLINAIDAMEEGEG------ 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 274 lPPLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQPSksdlhtvplaGYGYGLPISRLYARYFHGDIVLLS 353
Cdd:COG4191 278 -GRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGK----------GTGLGLSISYGIVEKHGGRIEVES 346

                       170
                ....*....|..
gi 17137298 354 CEGFGTDAIIYL 365
Cdd:COG4191 347 EPGGGTTFTITL 358
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 254-365 1.16e-05

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 254 LFKNSMRAVVEHHGHDnndtlPPLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYSTapqpsKSDLHTvplagyGY 333
Cdd:COG3290 289 LLDNAIEAVEKLPEEE-----RRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFST-----KLGEGR------GL 352

                        90       100       110
                ....*....|....*....|....*....|..
gi 17137298 334 GLPISRLYARYFHGDIVLLSCEGFGTDAIIYL 365
Cdd:COG3290 353 GLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 195-353 4.59e-05

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 45.45  E-value: 4.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 195 ACDLSDVVRDAYEnarFLCDQYYLTSPALEIQQHSSEPGDNLPIRTVYVpshlyymlfELFKNSMRAVVEHhghdnndtl 274
Cdd:COG4192 504 PVDLRQVIEQAWE---LVESRAKPQQITLHIPDDLMVQGDQVLLEQVLV---------NLLVNALDAVATQ--------- 562

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137298 275 PPLKVAICKGKEDICVKISDQGGGIPrsQTDQLFKYMYSTapqpsKSdlhtvplAGYGYGLPISRLYARYFHGDIVLLS 353
Cdd:COG4192 563 PQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTT-----KE-------VGLGLGLSICRSIMQQFGGDLYLAS 627
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
288-374 6.48e-05

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 44.84  E-value: 6.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 288 ICVKISDQGGGIPRSQTDQLFKYMYSTAPQpsksdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYLKA 367
Cdd:COG3852 287 VRIEVIDNGPGIPEEILDRIFEPFFTTKEK------------GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPL 354


                ....*..
gi 17137298 368 LSDEANE 374
Cdd:COG3852 355 EQAEEEP 361
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 287-365 1.10e-04

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: 41.12  E-value: 1.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137298 287 DICVKISDQGGGIPRSQTDQLFKYMYSTAPQpsksdlhtvplAGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYL 365
Cdd:cd16915  36 DLVIEVRDTGPGIAPELRDKVFERGVSTKGQ-----------GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 288-359 1.32e-04

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: 40.84  E-value: 1.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17137298 288 ICVKisDQGGGIPRSQTDQLFKYMYSTAPQpsksdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCEGFGT 359
Cdd:cd16920  40 ISVK--DTGPGIAEEVAGQLFDPFYTTKSE------------GLGMGLSICRSIIEAHGGRLSVESPAGGGA 97
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
284-366 1.54e-04

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 43.80  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298  284 GKEDICVKISDQGGGIPRSQTDQLFKYMYSTAPQpsksdlhtvplaGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAII 363
Cdd:PRK11360 530 SDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597


                 ...
gi 17137298  364 YLK 366
Cdd:PRK11360 598 YLP 600
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
196-370 4.01e-04

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 42.23  E-value: 4.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 196 CDLSDVVRDAYENARFLCDQYyltspalEIQQHSSEPGDNLPIRTVyvPSHLYYMLFELFKNSMRavvehHGHDNndtlP 275
Cdd:COG5002 240 VDLAELLEEVVEELRPLAEEK-------GIELELDLPEDPLLVLGD--PDRLEQVLTNLLDNAIK-----YTPEG----G 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 276 PLKVAICKGKEDICVKISDQGGGIPRSQTDQLFKYMYstapQPSKSDLHTVPlaGYGYGLPISRLYARYFHGDIVLLSCE 355
Cdd:COG5002 302 TITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFY----RVDKSRSRETG--GTGLGLAIVKHIVEAHGGRIWVESEP 375

                       170
                ....*....|....*
gi 17137298 356 GFGTDAIIYLKALSD 370
Cdd:COG5002 376 GKGTTFTITLPLARE 390
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 254-365 6.59e-03

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: 38.42  E-value: 6.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137298 254 LFKNSMRA-------VVEHHGHDNNdtlpplKVAIckgkedicvKISDQGGGIPRSQTDQLFKYMYSTapqpsKSDlhtv 326
Cdd:COG5809 387 LLKNAIEAmpeggniTIETKAEDDD------KVVI---------SVTDEGCGIPEERLKKLGEPFYTT-----KEK---- 442

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17137298 327 plaGYGYGLPISRLYARYFHGDIVLLSCEGFGTDAIIYL 365
Cdd:COG5809 443 ---GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
 
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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