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Conserved domains on  [gi|4885545|ref|NP_005382|]
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pyruvate dehydrogenase kinase, isozyme 3 isoform 2 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

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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 ...
 192-359 3.94e-77

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: 236.08  E-value: 3.94e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  192 NVADVVKDAYETAKMLCEQYYLVAPELEVEefnakaPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDRKEGYPAVK 271
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  272 TLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEP-------TRAAPLAGFGYGLPISRLYARYFQGDLKL 344
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDfsdlisgTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 4885545  345 YSMEGVGTDAVIYLK 359
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 26-188 1.02e-63

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: 201.19  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545     26 PLSIKQFLDFGRDNACEKT--SYMFLRKELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDpq 103
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILED-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545    104 vLDNFLQVLIKVRNRHNDVVPTMAQGVIEYKEKFGFDpfistNIQYFLDRFYTNRISFRMLINQHTLLFGGDTNPVHPKH 183
Cdd:pfam10436  79 -NEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPE-----EIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 4885545    184 -IGSID 188
Cdd:pfam10436 153 yVGIID 158
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 192-359 3.94e-77

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: 236.08  E-value: 3.94e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  192 NVADVVKDAYETAKMLCEQYYLVAPELEVEefnakaPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDRKEGYPAVK 271
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  272 TLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEP-------TRAAPLAGFGYGLPISRLYARYFQGDLKL 344
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDfsdlisgTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 4885545  345 YSMEGVGTDAVIYLK 359
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 26-188 1.02e-63

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: 201.19  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545     26 PLSIKQFLDFGRDNACEKT--SYMFLRKELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDpq 103
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILED-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545    104 vLDNFLQVLIKVRNRHNDVVPTMAQGVIEYKEKFGFDpfistNIQYFLDRFYTNRISFRMLINQHTLLFGGDTNPVHPKH 183
Cdd:pfam10436  79 -NEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPE-----EIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 4885545    184 -IGSID 188
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 238-359 4.43e-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: 4.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545     238 PSHLFHMLFELFKNSMRATVElyedrkEGYPAVKtlVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLeptr 317
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPE------GGRITVT--LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 4885545     318 aapLAGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLK 359
Cdd:smart00387  71 ---IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 237-359 1.28e-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: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545    237 VPSHLFHMLFELFKNSMRATvelyedrkegYPAVKTLVTLGKED-LSIKISDLGGGVPLRKIDRLFNyMYSTAPRPSLEp 315
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHA----------AKAGEITVTLSEGGeLTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 4885545    316 traaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLK 359
Cdd:pfam02518  70 -------GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
190-358 6.19e-10

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 59.92  E-value: 6.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  190 TCNVADVVKDAYETAKMLCEQYYLvapeleveEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATvelyedrKEGYPa 269
Cdd:COG0642 181 PVDLAELLEEVVELFRPLAEEKGI--------ELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYT-------PEGGT- 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  270 VKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPrpsleptrAAPLAGFGYGLPISRLYARYFQGDLKLYSMEG 349
Cdd:COG0642 245 VTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--------SRRGGGTGLGLAIVKRIVELHGGTIEVESEPG 316


                ....*....
gi 4885545  350 VGTDAVIYL 358
Cdd:COG0642 317 KGTTFTVTL 325
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
277-365 9.04e-05

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 44.57  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545   277 GKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRpsleptraaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVI 356
Cdd:PRK11360 530 SDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597


                 ....*....
gi 4885545   357 YLKALSSES 365
Cdd:PRK11360 598 YLPINPQGN 606
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 192-359 3.94e-77

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: 236.08  E-value: 3.94e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  192 NVADVVKDAYETAKMLCEQYYLVAPELEVEefnakaPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDRKEGYPAVK 271
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  272 TLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEP-------TRAAPLAGFGYGLPISRLYARYFQGDLKL 344
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDfsdlisgTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 4885545  345 YSMEGVGTDAVIYLK 359
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 26-188 1.02e-63

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: 201.19  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545     26 PLSIKQFLDFGRDNACEKT--SYMFLRKELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDpq 103
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILED-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545    104 vLDNFLQVLIKVRNRHNDVVPTMAQGVIEYKEKFGFDpfistNIQYFLDRFYTNRISFRMLINQHTLLFGGDTNPVHPKH 183
Cdd:pfam10436  79 -NEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPE-----EIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 4885545    184 -IGSID 188
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 238-359 4.43e-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: 4.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545     238 PSHLFHMLFELFKNSMRATVElyedrkEGYPAVKtlVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLeptr 317
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPE------GGRITVT--LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK---- 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 4885545     318 aapLAGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLK 359
Cdd:smart00387  71 ---IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 237-359 1.28e-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: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545    237 VPSHLFHMLFELFKNSMRATvelyedrkegYPAVKTLVTLGKED-LSIKISDLGGGVPLRKIDRLFNyMYSTAPRPSLEp 315
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHA----------AKAGEITVTLSEGGeLTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 4885545    316 traaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLK 359
Cdd:pfam02518  70 -------GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
190-358 6.19e-10

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 59.92  E-value: 6.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  190 TCNVADVVKDAYETAKMLCEQYYLvapeleveEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATvelyedrKEGYPa 269
Cdd:COG0642 181 PVDLAELLEEVVELFRPLAEEKGI--------ELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYT-------PEGGT- 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  270 VKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPrpsleptrAAPLAGFGYGLPISRLYARYFQGDLKLYSMEG 349
Cdd:COG0642 245 VTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--------SRRGGGTGLGLAIVKRIVELHGGTIEVESEPG 316


                ....*....
gi 4885545  350 VGTDAVIYL 358
Cdd:COG0642 317 KGTTFTVTL 325
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
190-363 1.89e-09

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 57.61  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  190 TCNVADVVKDAYETAKMLCEQYYLvapELEVEefnakAPDKPIQVVYVPSHLFHMLFELFKNSMRAT-----VELYedrk 264
Cdd:COG2205  90 PVDLAELLEEAVEELRPLAEEKGI---RLELD-----LPPELPLVYADPELLEQVLANLLDNAIKYSppggtITIS---- 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  265 egypavktlVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEptraaplaGFGYGLPISRLYARYFQGDLKL 344
Cdd:COG2205 158 ---------ARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG--------GTGLGLAIVKRIVEAHGGTIWV 220

                       170
                ....*....|....*....
gi 4885545  345 YSMEGVGTDAVIYLKALSS 363
Cdd:COG2205 221 ESEPGGGTTFTVTLPLAES 239
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 190-364 9.11e-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: 47.65  E-value: 9.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  190 TCNVADVVKDAYEtakmlceqyyLVAPELEVE--EFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATvelyedrkEGY 267
Cdd:COG5000 275 PVDLNELLREVLA----------LYEPALKEKdiRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAI--------EEG 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  268 PAVKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRpsleptraaplaGFGYGLPISRLYARYFQGDLKLYSM 347
Cdd:COG5000 337 GEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPK------------GTGLGLAIVKKIVEEHGGTIELESR 404

                       170
                ....*....|....*..
gi 4885545  348 EGVGTDAVIYLKALSSE 364
Cdd:COG5000 405 PGGGTTFTIRLPLAEEA 421
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 281-358 3.01e-05

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 43.14  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  281 LSIKISDLGGGVPLRKIDRLFNYMYSTAPrpsleptraaplAGFGYGLPISRLY--ARYFQGDLKLYSMEGVGTDAVIYL 358
Cdd:cd16919  48 VCLEVSDTGSGMPAEVLRRAFEPFFTTKE------------VGKGTGLGLSMVYgfVKQSGGHLRIYSEPGVGTTVRIYL 115
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
277-365 9.04e-05

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 44.57  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545   277 GKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRpsleptraaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVI 356
Cdd:PRK11360 530 SDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597


                 ....*....
gi 4885545   357 YLKALSSES 365
Cdd:PRK11360 598 YLPINPQGN 606
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
190-363 1.29e-04

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 43.77  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  190 TCNVADVVKDAYETAKMLceqyylvAPELEVEeFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATvelyedrKEGypa 269
Cdd:COG5002 239 PVDLAELLEEVVEELRPL-------AEEKGIE-LELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYT-------PEG--- 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  270 VKTLVTLGKED--LSIKISDLGGGVPLRKIDRLFNYMYSTaprpslEPTRAAPLAGFGYGLPISRLYARYFQGDLKLYSM 347
Cdd:COG5002 301 GTITVSLREEDdqVRISVRDTGIGIPEEDLPRIFERFYRV------DKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESE 374

                       170
                ....*....|....*.
gi 4885545  348 EGVGTDAVIYLKALSS 363
Cdd:COG5002 375 PGKGTTFTITLPLARE 390
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 245-352 3.60e-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: 39.69  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  245 LFELFKNSMRATVELYEDRKEgypAVKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPrpsleptraaplAGF 324
Cdd:cd16920   5 LINLVRNGIEAMSEGGCERRE---LTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKS------------EGL 69

                        90       100
                ....*....|....*....|....*...
gi 4885545  325 GYGLPISRLYARYFQGDLKLYSMEGVGT 352
Cdd:cd16920  70 GMGLSICRSIIEAHGGRLSVESPAGGGA 97
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 265-358 3.84e-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: 39.58  E-value: 3.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  265 EGYPAVKTLVTLGKE--DLSIKISDLGGGVPLRKIDRLFNYMYSTAPRpsleptraaplAGFGYGLPISRLYARYFQGDL 342
Cdd:cd16915  19 TGAPNKQVEVFLRDEgdDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ-----------GERGIGLALVRQSVERLGGSI 87

                        90
                ....*....|....*.
gi 4885545  343 KLYSMEGVGTDAVIYL 358
Cdd:cd16915  88 TVESEPGGGTTFSIRI 103
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 191-358 7.64e-04

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 41.32  E-value: 7.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  191 CNVADVVKdayETAKMLceQYYLVAPELEVEefnaKAPDKPIQVVYV-PSHLFHMLFELFKNSMRATvelyEDRKEGYPA 269
Cdd:COG4191 215 VDLNELID---EALELL--RPRLKARGIEVE----LDLPPDLPPVLGdPGQLEQVLLNLLINAIDAM----EEGEGGRIT 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  270 VKTlvTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTapRPSLEptraaplaGFGYGLPISRLYARYFQGDLKLYSMEG 349
Cdd:COG4191 282 IST--RREGDYVVISVRDNGPGIPPEVLERIFEPFFTT--KPVGK--------GTGLGLSISYGIVEKHGGRIEVESEPG 349


                ....*....
gi 4885545  350 VGTDAVIYL 358
Cdd:COG4191 350 GGTTFTITL 358
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 216-358 7.67e-04

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 41.37  E-value: 7.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  216 PELEVEEfNAKAPDKPIQvvyvPSHLFHMLFELFKNSMRATVELYEDRKEgypaVKTLVTLGKEDLSIKISDLGGGVPLR 295
Cdd:COG3290 262 IDLTIDI-DSDLPDLPLS----DTDLVTILGNLLDNAIEAVEKLPEEERR----VELSIRDDGDELVIEVEDSGPGIPEE 332

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4885545  296 KIDRLFNYMYSTAPRpsleptraaplAGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYL 358
Cdd:COG3290 333 LLEKIFERGFSTKLG-----------EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 281-352 1.11e-03

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: 38.24  E-value: 1.11e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4885545  281 LSIKISDLGGGVPLRKIDRLFNyMYSTAPRPSlepTRAAplAGFGYGLPISRLYARYFQGDLKLYSMEGVGT 352
Cdd:cd16922  37 LRFSVEDTGIGIPEEQQARLFE-PFSQADSST---TRKY--GGTGLGLAISKKLVELMGGDISVESEPGQGS 102
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 270-344 2.29e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 37.44  E-value: 2.29e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4885545  270 VKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTaPRPSLEPTRAaplagfGYGLPISRLYARYFQGDLKL 344
Cdd:cd16945  26 IALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSL-PRPHSGQKST------GLGLAFVQEVAQLHGGRITL 93
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
238-365 5.82e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 38.67  E-value: 5.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885545  238 PSHLFHMLFELFKNSMRA-------TVELYEDRkegypavktLVTLGKED----LSIKISDLGGGVPLRKIDRLFNYMYS 306
Cdd:COG3852 242 PDQLIQVLLNLVRNAAEAmpeggtiTIRTRVER---------QVTLGGLRprlyVRIEVIDNGPGIPEEILDRIFEPFFT 312

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4885545  307 TapRPSleptraaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLKALSSES 365
Cdd:COG3852 313 T--KEK----------GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEE 359
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 283-358 8.94e-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: 38.03  E-value: 8.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4885545  283 IKISDLGGGVPLRKIDRLFNYMYSTAPRpsleptraaplaGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYL 358
Cdd:COG5809 415 ISVTDEGCGIPEERLKKLGEPFYTTKEK------------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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