NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398364691|ref|NP_011456|]
View 

protein kinase PKP2 [Saccharomyces cerevisiae S288C]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
248-477 3.20e-62

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: 200.26  E-value: 3.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 248 SAKKYLLEASEESQKFIQDmyfKDIPMPEFIIEGDTQLSFYFLPTHLKYLLGEILRNTYEATMKHYIRKgLEKPEPIIVT 327
Cdd:cd16929    1 SPKKVVEDASEEARVLCDD---YYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDD-SDDLPPIKVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 328 VVSNDESYLFRISDKAGGVLHDDENLWSFGKSKERAQESLNNFHklpglqtvsiydevhshtkynsklkslqsitlkpym 407
Cdd:cd16929   77 VAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFS------------------------------------ 120
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 408 htslepmsypsiinghikyetPLIELLKRSFRYKLGIGLAMCKVYAEYWNGDLSLHSMPGYGTDVVLKLG 477
Cdd:cd16929  121 ---------------------DLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
79-244 1.14e-37

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: 135.32  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691   79 PVSLTQLAQYyddSTKLTRTKIINSGKFVKEELVIRIAHKLNQLQQLPFNVVNNFHFVQVYESYYNIFESFRKYPTIrTL 158
Cdd:pfam10436   1 PLSLRQLLDF---GRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-IL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691  159 EDASQFADFIKNMLEGFNTlNLPHLIMGALECTilDLYPREKMDQLLSDLLRARISRRLIVEEHVSITANYTSGKEENTL 238
Cdd:pfam10436  77 EDNEKFTELLEEILDRHND-VVPTLAQGVLELK--KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPDY 153

                  ....*.
gi 398364691  239 VlGDIF 244
Cdd:pfam10436 154 V-GIID 158
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
248-477 3.20e-62

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: 200.26  E-value: 3.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 248 SAKKYLLEASEESQKFIQDmyfKDIPMPEFIIEGDTQLSFYFLPTHLKYLLGEILRNTYEATMKHYIRKgLEKPEPIIVT 327
Cdd:cd16929    1 SPKKVVEDASEEARVLCDD---YYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDD-SDDLPPIKVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 328 VVSNDESYLFRISDKAGGVLHDDENLWSFGKSKERAQESLNNFHklpglqtvsiydevhshtkynsklkslqsitlkpym 407
Cdd:cd16929   77 VAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFS------------------------------------ 120
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 408 htslepmsypsiinghikyetPLIELLKRSFRYKLGIGLAMCKVYAEYWNGDLSLHSMPGYGTDVVLKLG 477
Cdd:cd16929  121 ---------------------DLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
79-244 1.14e-37

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: 135.32  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691   79 PVSLTQLAQYyddSTKLTRTKIINSGKFVKEELVIRIAHKLNQLQQLPFNVVNNFHFVQVYESYYNIFESFRKYPTIrTL 158
Cdd:pfam10436   1 PLSLRQLLDF---GRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-IL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691  159 EDASQFADFIKNMLEGFNTlNLPHLIMGALECTilDLYPREKMDQLLSDLLRARISRRLIVEEHVSITANYTSGKEENTL 238
Cdd:pfam10436  77 EDNEKFTELLEEILDRHND-VVPTLAQGVLELK--KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPDY 153

                  ....*.
gi 398364691  239 VlGDIF 244
Cdd:pfam10436 154 V-GIID 158
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
443-476 9.96e-05

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: 41.58  E-value: 9.96e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 398364691  443 GIGLAMCKVYAEYWNGDLSLHSMPGYGTDVVLKL 476
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
248-477 3.20e-62

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: 200.26  E-value: 3.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 248 SAKKYLLEASEESQKFIQDmyfKDIPMPEFIIEGDTQLSFYFLPTHLKYLLGEILRNTYEATMKHYIRKgLEKPEPIIVT 327
Cdd:cd16929    1 SPKKVVEDASEEARVLCDD---YYLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDD-SDDLPPIKVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 328 VVSNDESYLFRISDKAGGVLHDDENLWSFGKSKERAQESLNNFHklpglqtvsiydevhshtkynsklkslqsitlkpym 407
Cdd:cd16929   77 VAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFS------------------------------------ 120
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691 408 htslepmsypsiinghikyetPLIELLKRSFRYKLGIGLAMCKVYAEYWNGDLSLHSMPGYGTDVVLKLG 477
Cdd:cd16929  121 ---------------------DLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
79-244 1.14e-37

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: 135.32  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691   79 PVSLTQLAQYyddSTKLTRTKIINSGKFVKEELVIRIAHKLNQLQQLPFNVVNNFHFVQVYESYYNIFESFRKYPTIrTL 158
Cdd:pfam10436   1 PLSLRQLLDF---GRSLSEEKLLKSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-IL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364691  159 EDASQFADFIKNMLEGFNTlNLPHLIMGALECTilDLYPREKMDQLLSDLLRARISRRLIVEEHVSITANYTSGKEENTL 238
Cdd:pfam10436  77 EDNEKFTELLEEILDRHND-VVPTLAQGVLELK--KYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPDY 153

                  ....*.
gi 398364691  239 VlGDIF 244
Cdd:pfam10436 154 V-GIID 158
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
443-476 9.96e-05

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: 41.58  E-value: 9.96e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 398364691  443 GIGLAMCKVYAEYWNGDLSLHSMPGYGTDVVLKL 476
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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