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Conserved domains on  [gi|59709473|ref|NP_446278|]
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pyruvate dehydrogenase kinase, isozyme 1 precursor [Rattus norvegicus]

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 ...
 222-388 2.01e-76

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: 235.31  E-value: 2.01e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 222 DVVEVIKDGYENARRLCDLYYINSPELELEelnaksPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKG-VYPPIQ 300
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 301 VHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRP-------RVETSRAVPLAGFGYGLPISRLYAQYFQGDLKL 373
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPslddfsdLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 59709473 374 YSLEGYGTDAVIYIK 388
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-218 3.53e-65

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: 205.81  E-value: 3.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473    56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473   134 tiyEFTDTVIRIRNRHNDVIPTMAQGVTEYKESfgvdpVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKH 213
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 59709473   214 -IGSIN 218
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 ...
 222-388 2.01e-76

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: 235.31  E-value: 2.01e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 222 DVVEVIKDGYENARRLCDLYYINSPELELEelnaksPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKG-VYPPIQ 300
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 301 VHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRP-------RVETSRAVPLAGFGYGLPISRLYAQYFQGDLKL 373
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPslddfsdLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 59709473 374 YSLEGYGTDAVIYIK 388
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-218 3.53e-65

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: 205.81  E-value: 3.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473    56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473   134 tiyEFTDTVIRIRNRHNDVIPTMAQGVTEYKESfgvdpVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKH 213
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 59709473   214 -IGSIN 218
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 268-388 3.65e-20

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 85.39  E-value: 3.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473    268 PSHLYHMVFELFKNAMRATMEHhadkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVetsra 347
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK----- 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 59709473    348 vpLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIK 388
Cdd:smart00387  71 --IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 267-388 8.18e-15

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: 70.09  E-value: 8.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473   267 VPSHLYHMVFELFKNAMRATMEHhadkgvyPPIQVHVTlGEEDLTVKMSDRGGGVPLRKIDRLFNyMYSTAPRPRVEtsr 346
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKA-------GEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG--- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 59709473   347 avplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIK 388
Cdd:pfam02518  70 -----GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
215-387 1.35e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.94  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 215 GSINPN---CDVVEVIKDGYENARRLCDLYYInspELELEelnakSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHha 291
Cdd:COG2205  82 GKLSLElepVDLAELLEEAVEELRPLAEEKGI---RLELD-----LPPELPLVYADPELLEQVLANLLDNAIKYSPPG-- 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 292 dkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYstaprpRVETSRAVPlaGFGYGLPISRLYAQYFQGDL 371
Cdd:COG2205 152 -----GTITISARREGDGVRISVSDNGPGIPEEELERIFERFY------RGDNSRGEG--GTGLGLAIVKRIVEAHGGTI 218

                       170
                ....*....|....*.
gi 59709473 372 KLYSLEGYGTDAVIYI 387
Cdd:COG2205 219 WVESEPGGGTTFTVTL 234
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 261-389 6.15e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 42.24  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473  261 PIQVVYVPSHLYHMVFELFKNAMRATmehhaDKGvyppiQVHVTL---GEEDLTVKMSDRGGGVPLRKIDRLFNyMYSTA 337
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFT-----QQG-----GVTVRVryeEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQV 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 59709473  338 PRpRVETSRAVplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKA 389
Cdd:PRK11091 458 KD-SHGGKPAT---GTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHA 505
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 222-388 2.01e-76

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: 235.31  E-value: 2.01e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 222 DVVEVIKDGYENARRLCDLYYINSPELELEelnaksPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKG-VYPPIQ 300
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIE------GDPSIRFPYVPSHLYYILFELLKNAMRATVESHGDDSdDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 301 VHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRP-------RVETSRAVPLAGFGYGLPISRLYAQYFQGDLKL 373
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPslddfsdLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 59709473 374 YSLEGYGTDAVIYIK 388
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-218 3.53e-65

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: 205.81  E-value: 3.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473    56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473   134 tiyEFTDTVIRIRNRHNDVIPTMAQGVTEYKESfgvdpVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKH 213
Cdd:pfam10436  81 ---KFTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 59709473   214 -IGSIN 218
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 268-388 3.65e-20

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 85.39  E-value: 3.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473    268 PSHLYHMVFELFKNAMRATMEHhadkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVetsra 347
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK----- 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 59709473    348 vpLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIK 388
Cdd:smart00387  71 --IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 267-388 8.18e-15

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: 70.09  E-value: 8.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473   267 VPSHLYHMVFELFKNAMRATMEHhadkgvyPPIQVHVTlGEEDLTVKMSDRGGGVPLRKIDRLFNyMYSTAPRPRVEtsr 346
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKA-------GEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG--- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 59709473   347 avplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIK 388
Cdd:pfam02518  70 -----GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
215-387 1.35e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.94  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 215 GSINPN---CDVVEVIKDGYENARRLCDLYYInspELELEelnakSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHha 291
Cdd:COG2205  82 GKLSLElepVDLAELLEEAVEELRPLAEEKGI---RLELD-----LPPELPLVYADPELLEQVLANLLDNAIKYSPPG-- 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 292 dkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYstaprpRVETSRAVPlaGFGYGLPISRLYAQYFQGDL 371
Cdd:COG2205 152 -----GTITISARREGDGVRISVSDNGPGIPEEELERIFERFY------RGDNSRGEG--GTGLGLAIVKRIVEAHGGTI 218

                       170
                ....*....|....*.
gi 59709473 372 KLYSLEGYGTDAVIYI 387
Cdd:COG2205 219 WVESEPGGGTTFTVTL 234
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
252-387 2.48e-10

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 61.46  E-value: 2.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 252 ELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATmehhaDKGVypPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFN 331
Cdd:COG0642 205 ELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYT-----PEGG--TVTVSVRREGDRVRISVEDTGPGIPPEDLERIFE 277

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 59709473 332 YMYSTAPRPRVEtsravplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYI 387
Cdd:COG0642 278 PFFRTDPSRRGG--------GTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
221-381 2.80e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 52.25  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 221 CDVVEVIkdgyenaRRLCDLYYINSPELELEeLNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRatmehHADKGvyPPIQ 300
Cdd:COG5002 240 VDLAELL-------EEVVEELRPLAEEKGIE-LELDLPEDPLLVLGDPDRLEQVLTNLLDNAIK-----YTPEG--GTIT 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 301 VHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYstaprpRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYG 380
Cdd:COG5002 305 VSLREEDDQVRISVRDTGIGIPEEDLPRIFERFY------RVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKG 378


                .
gi 59709473 381 T 381
Cdd:COG5002 379 T 379
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 274-387 2.63e-06

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: 45.74  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 274 MVFELFKNAMRATMEHHAdkgvyPPIQVHVTLGEE--DLTVKMSDRGGGVPLRKIDRLFNYMYST-APRPRvetsravpl 350
Cdd:cd16915   4 IVGNLIDNALDALAATGA-----PNKQVEVFLRDEgdDLVIEVRDTGPGIAPELRDKVFERGVSTkGQGER--------- 69

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 59709473 351 agfGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYI 387
Cdd:cd16915  70 ---GIGLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 278-387 2.78e-06

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 278 LFKNAMRATMEHHADKgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTaprpRVETSRavplagfGYGL 357
Cdd:COG3290 289 LLDNAIEAVEKLPEEE---RRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFST----KLGEGR-------GLGL 354

                        90       100       110
                ....*....|....*....|....*....|
gi 59709473 358 PISRLYAQYFQGDLKLYSLEGYGTDAVIYI 387
Cdd:COG3290 355 ALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 278-387 9.43e-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: 9.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 278 LFKNAMRAtMEHHadkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRprvetsravplaGFGYGL 357
Cdd:COG5000 325 LLKNAIEA-IEEG------GEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPK------------GTGLGL 385

                        90       100       110
                ....*....|....*....|....*....|
gi 59709473 358 PISRLYAQYFQGDLKLYSLEGYGTDAVIYI 387
Cdd:COG5000 386 AIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 268-371 6.81e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 42.06  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 268 PSHLYHMVFELFKNAMRATmehhaDKGVyppiQVHVTLGEEDLTVKM--SDRGGGVPLRKIDRLFNYMYstaprpRVETS 345
Cdd:cd16946   2 RDRLQQLFVNLLENSLRYT-----DTGG----KLRIRAAQTPQEVRLdvEDSAPGVSDDQLARLFERFY------RVESS 66

                        90       100
                ....*....|....*....|....*.
gi 59709473 346 RAVPLAGFGYGLPISRLYAQYFQGDL 371
Cdd:cd16946  67 RNRASGGSGLGLAICHNIALAHGGTI 92
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 299-373 7.93e-05

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: 41.68  E-value: 7.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 59709473 299 IQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTaPRPRVETSRAvplagfGYGLPISRLYAQYFQGDLKL 373
Cdd:cd16945  26 IALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSL-PRPHSGQKST------GLGLAFVQEVAQLHGGRITL 93
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 275-381 8.76e-05

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: 41.61  E-value: 8.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 275 VFELFKNAMRATMEHHADKGVyppIQVHVTLGEED-LTVKMSDRGGGVPLRKIDRLFNYMYSTAPrprvetsravplAGF 353
Cdd:cd16920   5 LINLVRNGIEAMSEGGCERRE---LTIRTSPADDRaVTISVKDTGPGIAEEVAGQLFDPFYTTKS------------EGL 69

                        90       100
                ....*....|....*....|....*...
gi 59709473 354 GYGLPISRLYAQYFQGDLKLYSLEGYGT 381
Cdd:cd16920  70 GMGLSICRSIIEAHGGRLSVESPAGGGA 97
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 268-387 1.50e-04

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 43.63  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 268 PSHLYHMVFELFKNAMRAtMEHHADkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRvetsra 347
Cdd:COG4191 254 PGQLEQVLLNLLINAIDA-MEEGEG----GRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGK------ 322

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 59709473 348 vplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYI 387
Cdd:COG4191 323 ----GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 278-375 2.40e-04

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 43.52  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 278 LFKNAMRATMEHhadkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLrkIDRLFNYMYSTAPrprvetsravplAGFGYGL 357
Cdd:COG4192 551 LLVNALDAVATQ-------PQISVDLLSNAENLRVAISDNGNGWPL--VDKLFTPFTTTKE------------VGLGLGL 609

                        90
                ....*....|....*...
gi 59709473 358 PISRLYAQYFQGDLKLYS 375
Cdd:COG4192 610 SICRSIMQQFGGDLYLAS 627
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 261-389 6.15e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 42.24  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473  261 PIQVVYVPSHLYHMVFELFKNAMRATmehhaDKGvyppiQVHVTL---GEEDLTVKMSDRGGGVPLRKIDRLFNyMYSTA 337
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFT-----QQG-----GVTVRVryeEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQV 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 59709473  338 PRpRVETSRAVplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKA 389
Cdd:PRK11091 458 KD-SHGGKPAT---GTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHA 505
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 261-385 6.36e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 39.31  E-value: 6.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 261 PIQVVYVPSHLYHMVFELFKNAMRatmehhadkgvYPP--IQVHVTLGEEDLTV-KMSDRGGGVPLRKIDRLFNYMYSTA 337
Cdd:cd16940   4 DIQVQGDALLLFLLLRNLVDNAVR-----------YSPqgSRVEIKLSADDGAViRVEDNGPGIDEEELEALFERFYRSD 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 59709473 338 PRprvetsravPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVI 385
Cdd:cd16940  73 GQ---------NYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWV 111
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 278-373 1.61e-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: 37.79  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 278 LFKNAMRatmehHADKGVyppiQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNymystaPRPRVETSRAVPLAGFGYGL 357
Cdd:cd16939   8 LLRNALR-----YAHRTV----RIALLVSGGRLTLIVEDDGPGIPAAARERVFE------PFVRLDPSRDRATGGFGLGL 72

                        90
                ....*....|....*.
gi 59709473 358 PISRLYAQYFQGDLKL 373
Cdd:cd16939  73 AIVHRVALWHGGHVEC 88
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 297-361 1.74e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 37.94  E-value: 1.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59709473 297 PPIQVHVTL----GEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAvplagfGYGLPISR 361
Cdd:cd16953  17 PPDTGRITVsampTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHS------GLGLSISR 79
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 310-387 2.27e-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: 37.74  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 310 LTVKMSDRGGGVPLRKIDRLFNYMYSTAPrprvetsravplAGFGYGLPISRLYAQYFQ--GDLKLYSLEGYGTDAVIYI 387
Cdd:cd16919  48 VCLEVSDTGSGMPAEVLRRAFEPFFTTKE------------VGKGTGLGLSMVYGFVKQsgGHLRIYSEPGVGTTVRIYL 115
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
 299-385 2.75e-03

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 39.83  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473  299 IQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTaPRPrvETSRavplAGFGYGLPISRLYAQYFQGDLKLYSLEG 378
Cdd:PRK11100 390 ITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYSL-PRP--ANGR----KSTGLGLAFVREVARLHGGEVTLRNRPE 462


                 ....*..
gi 59709473  379 YGTDAVI 385
Cdd:PRK11100 463 GGVLATL 469
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 278-381 5.14e-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: 39.19  E-value: 5.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 278 LFKNAMRATmehhaDKGVYppIQVHVTLGEED-LTVKMSDRGGGVPLRKIDRLFNYMYSTAPRprvetsravplaGFGYG 356
Cdd:COG5809 387 LLKNAIEAM-----PEGGN--ITIETKAEDDDkVVISVTDEGCGIPEERLKKLGEPFYTTKEK------------GTGLG 447

                        90       100
                ....*....|....*....|....*
gi 59709473 357 LPISRLYAQYFQGDLKLYSLEGYGT 381
Cdd:COG5809 448 LMVSYKIIEEHGGKITVESEVGKGT 472
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 275-380 5.54e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 36.28  E-value: 5.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 275 VFELFKNAMRAtMEHHADkgvyPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRvetsravplaGFG 354
Cdd:cd16976   5 LMNLLQNALDA-MGKVEN----PRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGK----------GTG 69

                        90       100
                ....*....|....*....|....*.
gi 59709473 355 YGLPISRLYAQYFQGDLKLYSLEGYG 380
Cdd:cd16976  70 LGLSISYGIVEEHGGRLSVANEEGAG 95
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
306-394 6.49e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 38.80  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473  306 GEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRprvetsravplaGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVI 385
Cdd:PRK11360 530 SDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597


                 ....*....
gi 59709473  386 YIKALSTES 394
Cdd:PRK11360 598 YLPINPQGN 606
PRK15347 PRK15347
two component system sensor kinase;
299-381 6.50e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 38.85  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473  299 IQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYstaprpRVETSRAvplaGFGYGLPISRLYAQYFQGDLKLYSLEG 378
Cdd:PRK15347 534 IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFY------QADTHSQ----GTGLGLTIASSLAKMMGGELTLFSTPG 603


                 ...
gi 59709473  379 YGT 381
Cdd:PRK15347 604 VGS 606
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 299-387 6.90e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 35.89  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59709473 299 IQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNymystaPRPRVETSRAVplAGFGYGLPISRLYAQYFQGDLKLYSLEG 378
Cdd:cd16950  20 VEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQ------PFYRGDNARGT--SGTGLGLAIVQRISDAHGGSLTLANRAG 91


                ....*....
gi 59709473 379 YGTDAVIYI 387
Cdd:cd16950  92 GGLCARIEL 100
 
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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