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Conserved domains on  [gi|20072770|gb|AAH26134|]
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Pyruvate dehydrogenase kinase, isoenzyme 4 [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 ...
 199-365 1.61e-75

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: 232.23  E-value: 1.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 199 DVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNgkfpgqPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRP-SLTPVE 277
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNS-------RNAPLAGFGYGLPISRLYAKYFQGDLNL 350
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFsdlisgtQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 20072770 351 YSMSGYGTDAIIYLK 365
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 34-195 3.11e-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: 200.42  E-value: 3.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770    34 PLSMKQLLDFGSENACERT--SFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQK 111
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770   112 alsEFVDTLVKVRNRHHNVVPTMAQGILEYKDTctvdpVTNQNLQYFLDRFYMNRISTRMLMNQHILIF--SDSKTGNPS 189
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTeqSNNPSHPPD 152


                  ....*.
gi 20072770   190 HIGSID 195
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 ...
 199-365 1.61e-75

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: 232.23  E-value: 1.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 199 DVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNgkfpgqPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRP-SLTPVE 277
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNS-------RNAPLAGFGYGLPISRLYAKYFQGDLNL 350
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFsdlisgtQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 20072770 351 YSMSGYGTDAIIYLK 365
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 34-195 3.11e-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: 200.42  E-value: 3.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770    34 PLSMKQLLDFGSENACERT--SFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQK 111
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770   112 alsEFVDTLVKVRNRHHNVVPTMAQGILEYKDTctvdpVTNQNLQYFLDRFYMNRISTRMLMNQHILIF--SDSKTGNPS 189
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTeqSNNPSHPPD 152


                  ....*.
gi 20072770   190 HIGSID 195
Cdd:pfam10436 153 YVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 245-365 2.88e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 80.00  E-value: 2.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770    245 PSHLHHMLFELFKNAMRATVEHqenrpslTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPtpvmdnsRN 324
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDK-------RS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 20072770    325 APLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLK 365
Cdd:smart00387  69 RKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 244-365 2.59e-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: 65.85  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770   244 VPSHLHHMLFELFKNAMRATvehqenrPSLTPVEATVVLGkEDLTIKISDRGGGVPLRITDRLFSyTYSTAPTPVMdnsr 323
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHA-------AKAGEITVTLSEG-GELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 20072770   324 naplAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLK 365
Cdd:pfam02518  69 ----GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
198-369 3.51e-11

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 63.00  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 198 CDVVAVVQDAFECAKMLCDQYYLtspelnltQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATvehqenrPSLTPVE 277
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKGI--------RLELDLPPELPLVYADPELLEQVLANLLDNAIKYS-------PPGGTIT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYStaptpvMDNSRNAPlaGFGYGLPISRLYAKYFQGDLNLYSMSGYG 357
Cdd:COG2205 156 ISARREGDGVRISVSDNGPGIPEEELERIFERFYR------GDNSRGEG--GTGLGLAIVKRIVEAHGGTIWVESEPGGG 227

                       170
                ....*....|..
gi 20072770 358 TDAIIYLKALSS 369
Cdd:COG2205 228 TTFTVTLPLAES 239
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 238-373 1.26e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 44.16  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770  238 PIHIVYVPSHLHHMLFELFKNAMRATvehQENRPSLTpVEATVvlgKEDLTIKISDRGGGVPLRITDRLFSYTYStaptp 317
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFT---QQGGVTVR-VRYEE---GDMLTFEVEDSGIGIPEDELDKIFAMYYQ----- 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20072770  318 VMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESVE 373
Cdd:PRK11091 457 VKDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEV 512
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 199-365 1.61e-75

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: 232.23  E-value: 1.61e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 199 DVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNgkfpgqPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRP-SLTPVE 277
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNS-------RNAPLAGFGYGLPISRLYAKYFQGDLNL 350
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFsdlisgtQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 20072770 351 YSMSGYGTDAIIYLK 365
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 34-195 3.11e-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: 200.42  E-value: 3.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770    34 PLSMKQLLDFGSENACERT--SFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQK 111
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770   112 alsEFVDTLVKVRNRHHNVVPTMAQGILEYKDTctvdpVTNQNLQYFLDRFYMNRISTRMLMNQHILIF--SDSKTGNPS 189
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTeqSNNPSHPPD 152


                  ....*.
gi 20072770   190 HIGSID 195
Cdd:pfam10436 153 YVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 245-365 2.88e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 80.00  E-value: 2.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770    245 PSHLHHMLFELFKNAMRATVEHqenrpslTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPtpvmdnsRN 324
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDK-------RS 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 20072770    325 APLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLK 365
Cdd:smart00387  69 RKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 244-365 2.59e-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: 65.85  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770   244 VPSHLHHMLFELFKNAMRATvehqenrPSLTPVEATVVLGkEDLTIKISDRGGGVPLRITDRLFSyTYSTAPTPVMdnsr 323
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHA-------AKAGEITVTLSEG-GELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGG---- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 20072770   324 naplAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLK 365
Cdd:pfam02518  69 ----GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
198-369 3.51e-11

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 63.00  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 198 CDVVAVVQDAFECAKMLCDQYYLtspelnltQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATvehqenrPSLTPVE 277
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKGI--------RLELDLPPELPLVYADPELLEQVLANLLDNAIKYS-------PPGGTIT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYStaptpvMDNSRNAPlaGFGYGLPISRLYAKYFQGDLNLYSMSGYG 357
Cdd:COG2205 156 ISARREGDGVRISVSDNGPGIPEEELERIFERFYR------GDNSRGEG--GTGLGLAIVKRIVEAHGGTIWVESEPGGG 227

                       170
                ....*....|..
gi 20072770 358 TDAIIYLKALSS 369
Cdd:COG2205 228 TTFTVTLPLAES 239
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
199-364 1.11e-09

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 59.54  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 199 DVVAVVQDAFECAKMLCDQYYLtspELNLTqvngkFPGQPIHIVYVPSHLHHMLFELFKNAMRATvehqenrPSLTPVEA 278
Cdd:COG0642 183 DLAELLEEVVELFRPLAEEKGI---ELELD-----LPDDLPTVRGDPDRLRQVLLNLLSNAIKYT-------PEGGTVTV 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 279 TVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTaptpvmDNSRNAPlaGFGYGLPISRLYAKYFQGDLNLYSMSGYGT 358
Cdd:COG0642 248 SVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRT------DPSRRGG--GTGLGLAIVKRIVELHGGTIEVESEPGKGT 319


                ....*.
gi 20072770 359 DAIIYL 364
Cdd:COG0642 320 TFTVTL 325
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 163-364 1.17e-06

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 50.23  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 163 YMNRISTRMlmnQHILIFSDSKTGNPshigsidpncDVVAVVQDAFECAKMLcdqyyltSPELNLTqVNGKFPGQPIhiv 242
Cdd:COG3290 222 YIDEISEEL---QELIDSLLSRIGNP----------VLAALLLGKAARARER-------GIDLTID-IDSDLPDLPL--- 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 243 yVPSHLHHMLFELFKNAMRATVEHQENRPSltpVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPtpvmDNS 322
Cdd:COG3290 278 -SDTDLVTILGNLLDNAIEAVEKLPEEERR---VELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKL----GEG 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20072770 323 RnaplagfGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYL 364
Cdd:COG3290 350 R-------GLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
198-369 2.32e-06

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 49.17  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 198 CDVVAVVQDAFECAKMLCDQyyltspelNLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATvehqenrPSLTPVE 277
Cdd:COG5002 240 VDLAELLEEVVEELRPLAEE--------KGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYT-------PEGGTIT 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVP----LRITDRLFsytysTAptpvmDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSM 353
Cdd:COG5002 305 VSLREEDDQVRISVRDTGIGIPeedlPRIFERFY-----RV-----DKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESE 374

                       170
                ....*....|....*.
gi 20072770 354 SGYGTDAIIYLKALSS 369
Cdd:COG5002 375 PGKGTTFTITLPLARE 390
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 198-370 4.23e-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: 48.42  E-value: 4.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 198 CDVVAVVQDAfecAKMLCDQYYLTSPELNLTqvngkFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQEnrpsltpVE 277
Cdd:COG5000 276 VDLNELLREV---LALYEPALKEKDIRLELD-----LDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGE-------IE 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 278 ATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTpvmdnsrnaplaGFGYGLPISRLYAKYFQGDLNLYSMSGYG 357
Cdd:COG5000 341 VSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPK------------GTGLGLAIVKKIVEEHGGTIELESRPGGG 408

                       170
                ....*....|...
gi 20072770 358 TDAIIYLKALSSE 370
Cdd:COG5000 409 TTFTIRLPLAEEA 421
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 248-358 1.04e-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: 41.23  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 248 LHHMLFELFKNAMRATVEHQENRPSLTPVEATVvlGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTpvmdnsrnapl 327
Cdd:cd16920   1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPA--DDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE----------- 67

                        90       100       110
                ....*....|....*....|....*....|.
gi 20072770 328 aGFGYGLPISRLYAKYFQGDLNLYSMSGYGT 358
Cdd:cd16920  68 -GLGMGLSICRSIIEAHGGRLSVESPAGGGA 97
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 238-373 1.26e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 44.16  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770  238 PIHIVYVPSHLHHMLFELFKNAMRATvehQENRPSLTpVEATVvlgKEDLTIKISDRGGGVPLRITDRLFSYTYStaptp 317
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFT---QQGGVTVR-VRYEE---GDMLTFEVEDSGIGIPEDELDKIFAMYYQ----- 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20072770  318 VMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESVE 373
Cdd:PRK11091 457 VKDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEV 512
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 198-352 1.29e-04

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 44.29  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 198 CDVVAVVQDAFEC----AKMLCDQyyLTSPELNLTQVNgkfpgqpihivyvPSHLHHMLFELFKNAMRATVEHQEnrpsl 273
Cdd:COG4192 505 VDLRQVIEQAWELvesrAKPQQIT--LHIPDDLMVQGD-------------QVLLEQVLVNLLVNALDAVATQPQ----- 564

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072770 274 tpVEATVVLGKEDLTIKISDRGGGVPlrITDRLFSYTYSTAPTpvmdnsrnaplaGFGYGLPISRLYAKYFQGDLNLYS 352
Cdd:COG4192 565 --ISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKEV------------GLGLGLSICRSIMQQFGGDLYLAS 627
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 245-364 4.94e-04

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 42.09  E-value: 4.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 245 PSHLHHMLFELFKNAMRATVEHQENRpsltpVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVmdnsrn 324
Cdd:COG4191 254 PGQLEQVLLNLLINAIDAMEEGEGGR-----ITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGK------ 322

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20072770 325 aplaGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYL 364
Cdd:COG4191 323 ----GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
245-371 1.37e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 40.72  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770  245 PSHLHHMLFELFKNAMRATvehqENRPSLTpVEaTVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTpvmdnsrn 324
Cdd:PRK11360 498 PELLKQVLLNILINAVQAI----SARGKIR-IR-TWQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK-------- 563

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 20072770  325 aplaGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSES 371
Cdd:PRK11360 564 ----GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGN 606
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 248-350 3.03e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 37.02  E-value: 3.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 248 LHHMLFELFKNAMRatveHQENRpsltpVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSytystaPTPVMDNSRNAPL 327
Cdd:cd16939   1 MARALDNLLRNALR----YAHRT-----VRIALLVSGGRLTLIVEDDGPGIPAAARERVFE------PFVRLDPSRDRAT 65

                        90       100
                ....*....|....*....|...
gi 20072770 328 AGFGYGLPISRLYAKYFQGDLNL 350
Cdd:cd16939  66 GGFGLGLAIVHRVALWHGGHVEC 88
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 287-364 3.41e-03

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: 36.97  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 287 LTIKISDRGGGVPLRITDRLFSYTYSTAPTpvmdnsrnaplaGFGYGLPISRLY--AKYFQGDLNLYSMSGYGTDAIIYL 364
Cdd:cd16919  48 VCLEVSDTGSGMPAEVLRRAFEPFFTTKEV------------GKGTGLGLSMVYgfVKQSGGHLRIYSEPGVGTTVRIYL 115
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 220-364 9.06e-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: 9.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 220 LTSPELNLT--QVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPSLTPVEATVVLgkedltIKISDRGGG 297
Cdd:COG5809 350 LLQPQALLKnvQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEDDDKVV------ISVTDEGCG 423

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20072770 298 VPLRITDRLFSYTYSTAPTpvmdnsrnaplaGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYL 364
Cdd:COG5809 424 IPEERLKKLGEPFYTTKEK------------GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 255-364 9.11e-03

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: 35.73  E-value: 9.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072770 255 LFKNAMRATVEHQEnrpslTPVEATVVLGKE--DLTIKISDRGGGVPLRITDRLFSYTYSTAPTpvmdnsrnaplAGFGY 332
Cdd:cd16915   8 LIDNALDALAATGA-----PNKQVEVFLRDEgdDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ-----------GERGI 71

                        90       100       110
                ....*....|....*....|....*....|..
gi 20072770 333 GLPISRLYAKYFQGDLNLYSMSGYGTDAIIYL 364
Cdd:cd16915  72 GLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
 
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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