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Conserved domains on  [gi|6322147|ref|NP_012222|]
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protein kinase PKP1 [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

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 ...
 216-383 6.95e-73

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: 224.91  E-value: 6.95e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  216 PIAQLIKHVSDYVNDICFVKfnTQRTPVLIHPPSQDITFTCIPPILEYIMTEVFKNAFEAQIALGK----EHMPIEINLL 291
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDY--YLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGddsdDLPPIKVTVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  292 KpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSADSESTDLPGEQINNVSGMGFGLPMCKTYLELFGGKIDVQSL 371
Cdd:cd16929  79 K-GDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFSDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSM 157

                       170
                ....*....|..
gi 6322147  372 LGWGTDVYIKLK 383
Cdd:cd16929 158 EGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 55-212 6.11e-36

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: 128.77  E-value: 6.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147     55 PLNYEYFLQYRPPLTkkeeYMLTIKTINLLLS----LTCKRLNAIQRLPYNAVINPHIERTNSLYLKSLQTLLSIAYPyE 130
Cdd:pfam10436   1 PLSLRQLLDFGRSLS----EEKLLKSANFLREelpvRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-I 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147    131 LHNPPKIQAKFTELLDDHEDAIVVLAKGLQEIQSCYPKFQISQFLNFHLKERITMKLLVTHYLSL-MAQNKGDTNKRMIG 209
Cdd:pfam10436  76 LEDNEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALtEQSNNPSHPPDYVG 155


                  ...
gi 6322147    210 ILH 212
Cdd:pfam10436 156 IID 158
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 216-383 6.95e-73

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: 224.91  E-value: 6.95e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  216 PIAQLIKHVSDYVNDICFVKfnTQRTPVLIHPPSQDITFTCIPPILEYIMTEVFKNAFEAQIALGK----EHMPIEINLL 291
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDY--YLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGddsdDLPPIKVTVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  292 KpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSADSESTDLPGEQINNVSGMGFGLPMCKTYLELFGGKIDVQSL 371
Cdd:cd16929  79 K-GDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFSDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSM 157

                       170
                ....*....|..
gi 6322147  372 LGWGTDVYIKLK 383
Cdd:cd16929 158 EGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 55-212 6.11e-36

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: 128.77  E-value: 6.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147     55 PLNYEYFLQYRPPLTkkeeYMLTIKTINLLLS----LTCKRLNAIQRLPYNAVINPHIERTNSLYLKSLQTLLSIAYPyE 130
Cdd:pfam10436   1 PLSLRQLLDFGRSLS----EEKLLKSANFLREelpvRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-I 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147    131 LHNPPKIQAKFTELLDDHEDAIVVLAKGLQEIQSCYPKFQISQFLNFHLKERITMKLLVTHYLSL-MAQNKGDTNKRMIG 209
Cdd:pfam10436  76 LEDNEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALtEQSNNPSHPPDYVG 155


                  ...
gi 6322147    210 ILH 212
Cdd:pfam10436 156 IID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 258-383 1.98e-19

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.08  E-value: 1.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147     258 PPILEYIMTEVFKNAFEAqialGKEHMPIEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSadsestdl 337
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKY----TPEGGRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSR-------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6322147     338 pgeqinNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:smart00387  70 ------KIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 258-383 1.19e-14

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: 69.70  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147    258 PPILEYIMTEVFKNAFEAqiALGKEHMPIEINllkpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSadsestdl 337
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKH--AAKAGEITVTLS----EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG-------- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6322147    338 pgeqinnvSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:pfam02518  69 --------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
243-382 6.52e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 67.62  E-value: 6.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  243 VLIHPPSQDITFTCIPPILEYIMTEVFKNAfeaqIALGKEHMPIEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSY 322
Cdd:COG2205 115 LELDLPPELPLVYADPELLEQVLANLLDNA----IKYSPPGGTITISA-RREGDGVRISVSDNGPGIPEEELERIFERFY 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  323 SthtqqsadsestdlpGEQINNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG2205 190 R---------------GDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
251-383 7.57e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 51.12  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147   251 DITFTC-----IPPI------LEYIMTEVFKNAFEAQIALGKehmpIEINLLKPDDDELYLRIRDHGGGITPEVEALMFN 319
Cdd:PRK11360 480 RVDFETeldneLPPIwadpelLKQVLLNILINAVQAISARGK----IRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFD 555

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322147   320 YSYSTHTQqsadsestdlpgeqinnvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:PRK11360 556 PFFTTKAK-------------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 216-383 6.95e-73

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: 224.91  E-value: 6.95e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  216 PIAQLIKHVSDYVNDICFVKfnTQRTPVLIHPPSQDITFTCIPPILEYIMTEVFKNAFEAQIALGK----EHMPIEINLL 291
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDY--YLSSPELEIEGDPSIRFPYVPSHLYYILFELLKNAMRATVESHGddsdDLPPIKVTVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  292 KpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSADSESTDLPGEQINNVSGMGFGLPMCKTYLELFGGKIDVQSL 371
Cdd:cd16929  79 K-GDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSLDDFSDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSM 157

                       170
                ....*....|..
gi 6322147  372 LGWGTDVYIKLK 383
Cdd:cd16929 158 EGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 55-212 6.11e-36

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: 128.77  E-value: 6.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147     55 PLNYEYFLQYRPPLTkkeeYMLTIKTINLLLS----LTCKRLNAIQRLPYNAVINPHIERTNSLYLKSLQTLLSIAYPyE 130
Cdd:pfam10436   1 PLSLRQLLDFGRSLS----EEKLLKSANFLREelpvRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPP-I 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147    131 LHNPPKIQAKFTELLDDHEDAIVVLAKGLQEIQSCYPKFQISQFLNFHLKERITMKLLVTHYLSL-MAQNKGDTNKRMIG 209
Cdd:pfam10436  76 LEDNEKFTELLEEILDRHNDVVPTLAQGVLELKKYLSPEEIQSFLDRFLRSRIGIRLLAEQHIALtEQSNNPSHPPDYVG 155


                  ...
gi 6322147    210 ILH 212
Cdd:pfam10436 156 IID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 258-383 1.98e-19

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.08  E-value: 1.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147     258 PPILEYIMTEVFKNAFEAqialGKEHMPIEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSadsestdl 337
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKY----TPEGGRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSR-------- 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6322147     338 pgeqinNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:smart00387  70 ------KIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 258-383 1.19e-14

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: 69.70  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147    258 PPILEYIMTEVFKNAFEAqiALGKEHMPIEINllkpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSadsestdl 337
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKH--AAKAGEITVTLS----EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG-------- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6322147    338 pgeqinnvSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:pfam02518  69 --------GGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
243-382 6.52e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 67.62  E-value: 6.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  243 VLIHPPSQDITFTCIPPILEYIMTEVFKNAfeaqIALGKEHMPIEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSY 322
Cdd:COG2205 115 LELDLPPELPLVYADPELLEQVLANLLDNA----IKYSPPGGTITISA-RREGDGVRISVSDNGPGIPEEELERIFERFY 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  323 SthtqqsadsestdlpGEQINNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG2205 190 R---------------GDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
212-382 3.86e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 66.86  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  212 HRDLPIAQLIKHVSDYVNDICFVKFNTqrtpVLIHPPSQDITFTCIPPILEYIMTEVFKNAFEAqialGKEHMPIEINLl 291
Cdd:COG0642 179 PEPVDLAELLEEVVELFRPLAEEKGIE----LELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKY----TPEGGTVTVSV- 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  292 KPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqiNNVSGMGFGLPMCKTYLELFGGKIDVQSL 371
Cdd:COG0642 250 RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS---------------RRGGGTGLGLAIVKRIVELHGGTIEVESE 314

                       170
                ....*....|.
gi 6322147  372 LGWGTDVYIKL 382
Cdd:COG0642 315 PGKGTTFTVTL 325
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 270-376 1.30e-10

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: 57.79  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  270 KNAFEAQIALGKEHMPIEINLLKPDDDELYLRIRDHGGGITPEVEALMFNYSYSThtqqsadsestdlpgeqinNVSGMG 349
Cdd:cd16920  10 RNGIEAMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTT-------------------KSEGLG 70

                        90       100
                ....*....|....*....|....*..
gi 6322147  350 FGLPMCKTYLELFGGKIDVQSLLGWGT 376
Cdd:cd16920  71 MGLSICRSIIEAHGGRLSVESPAGGGA 97
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 271-376 4.35e-10

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: 56.53  E-value: 4.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  271 NAFEAQIALGKEHMPIEInLLKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqinnvSGMGF 350
Cdd:cd16915  11 NALDALAATGAPNKQVEV-FLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ------------------GERGI 71

                        90       100
                ....*....|....*....|....*.
gi 6322147  351 GLPMCKTYLELFGGKIDVQSLLGWGT 376
Cdd:cd16915  72 GLALVRQSVERLGGSITVESEPGGGT 97
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 185-382 7.92e-10

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: 59.98  E-value: 7.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  185 MKLLVTHYLSLmAqnkgdtnkRMIGILHRDLPIAQLIKHVSDYVNDICFVKfntqRTPVLIHPPSQDITFTCIPPILEYI 264
Cdd:COG5000 255 LKRIVDEFLDF-A--------RLPEPQLEPVDLNELLREVLALYEPALKEK----DIRLELDLDPDLPEVLADRDQLEQV 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  265 MTEVFKNAFEAQIALGKehmpIEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTqqsadsestdlpgeqinn 344
Cdd:COG5000 322 LINLLKNAIEAIEEGGE----IEVST-RREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP------------------ 378

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6322147  345 vSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG5000 379 -KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 243-382 8.55e-10

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 59.81  E-value: 8.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  243 VLIHPPSQDITFTCIPPILEYIMTEVFKNAFEAqIAlGKEHMPIEINLlKPDDDELYLRIRDHGGGITPEVEALMFN--Y 320
Cdd:COG4191 239 VELDLPPDLPPVLGDPGQLEQVLLNLLINAIDA-ME-EGEGGRITIST-RREGDYVVISVRDNGPGIPPEVLERIFEpfF 315

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322147  321 SysthtqqsadsesTDLPGEqinnvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG4191 316 T-------------TKPVGK------GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 271-382 9.84e-09

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 56.78  E-value: 9.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  271 NAFEAQIALGKEHMPIEINLLKpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQsadsestdlpgeqinnvsGMGF 350
Cdd:COG3290 292 NAIEAVEKLPEEERRVELSIRD-DGDELVIEVEDSGPGIPEELLEKIFERGFSTKLGE------------------GRGL 352

                        90       100       110
                ....*....|....*....|....*....|..
gi 6322147  351 GLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG3290 353 GLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 257-382 6.35e-08

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: 54.21  E-value: 6.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  257 IPPIL--EYIMTEVF----KNAFEAqIALGKEhmpIEINLLKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsa 330
Cdd:COG5809 370 IPDILgdENQLKQVFinllKNAIEA-MPEGGN---ITIETKAEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEK--- 442

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6322147  331 dsestdlpgeqinnvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG5809 443 ----------------GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
269-382 5.36e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 51.00  E-value: 5.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  269 FKNAFEA-----QIALGKEHMPIEINLLKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqin 343
Cdd:COG3852 253 VRNAAEAmpeggTITIRTRVERQVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKEK---------------- 316

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322147  344 nvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG3852 317 ---GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYL 352
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
251-383 7.57e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 51.12  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147   251 DITFTC-----IPPI------LEYIMTEVFKNAFEAQIALGKehmpIEINLLKPDDDELYLRIRDHGGGITPEVEALMFN 319
Cdd:PRK11360 480 RVDFETeldneLPPIwadpelLKQVLLNILINAVQAISARGK----IRIRTWQYSDGQVAVSIEDNGCGIDPELLKKIFD 555

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322147   320 YSYSTHTQqsadsestdlpgeqinnvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:PRK11360 556 PFFTTKAK-------------------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 271-382 1.72e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 49.91  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147   271 NAFEAqiALGKEHMPIEInLLKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHtqqsadsestdlpGEqinnvsGMGF 350
Cdd:PRK11086 444 NALEA--VGGEEGGEISV-SLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTK-------------GS------NRGV 501

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6322147   351 GLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:PRK11086 502 GLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 260-382 3.17e-06

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 47.19  E-value: 3.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  260 ILEYI---MTEVFKNAF-------EAQIALGK-EHMPIEINLlKPDDDELYLRIRDHGGGITPEV---EALMFNYSYSTH 325
Cdd:cd16916  35 VLEKLadpLTHLLRNAVdhgieapEERLAAGKpPEGTITLRA-EHQGNQVVIEVSDDGRGIDREKireKAIERGLITADE 113

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322147  326 TQQSADSESTDL---PG----EQINNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:cd16916 114 AATLSDDEVLNLifaPGfstaEQVTDVSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
213-382 6.09e-06

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 48.01  E-value: 6.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  213 RDLPIAQLIKHVSDYVNdicfVKFNTQRTPVLIHPPSQDITFTCIPPILEYIMTEVFKNAfeaqIALGKEHMPIEINLlK 292
Cdd:COG5002 238 EPVDLAELLEEVVEELR----PLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNA----IKYTPEGGTITVSL-R 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  293 PDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSADSEstdlpgeqinnvsGMGFGLPMCKTYLELFGGKIDVQSLL 372
Cdd:COG5002 309 EEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETG-------------GTGLGLAIVKHIVEAHGGRIWVESEP 375

                       170
                ....*....|
gi 6322147  373 GWGTDVYIKL 382
Cdd:COG5002 376 GKGTTFTITL 385
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 270-383 3.93e-05

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 45.49  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  270 KNAFEAqialgkehMP----IEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqinnv 345
Cdd:COG5805 405 KNAIEA--------MPnggtITIHT-EEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEK------------------ 457

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6322147  346 sGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:COG5805 458 -GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 286-383 4.95e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 42.09  E-value: 4.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  286 IEINLLKPDDDELYLR--IRDHGGGITPEVEALMFNysysTHTQqsADSESTDLPGeqinnvsGMGFGLPMCKTYLELFG 363
Cdd:cd16922  23 LRVSLEEEEEDGVQLRfsVEDTGIGIPEEQQARLFE----PFSQ--ADSSTTRKYG-------GTGLGLAISKKLVELMG 89

                        90       100
                ....*....|....*....|
gi 6322147  364 GKIDVQSLLGWGTDVYIKLK 383
Cdd:cd16922  90 GDISVESEPGQGSTFTFTLP 109
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 295-382 1.28e-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: 41.24  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  295 DDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqinNVSGMGFGLPMCKTYLELFGGKIDVQSLLGW 374
Cdd:cd16940  42 DDGAVIRVEDNGPGIDEEELEALFERFYRSDGQ----------------NYGGSGLGLSIVKRIVELHGGQIFLGNAQGG 105


                ....*...
gi 6322147  375 GTDVYIKL 382
Cdd:cd16940 106 GLEAWVRL 113
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 286-382 2.65e-04

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 42.85  E-value: 2.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  286 IEINLlKPDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQqsadsestdlpgeqiNNVSGMGFGLPMCKTYLELFGGK 365
Cdd:COG4251 418 IEIGA-EREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR---------------DEYEGTGIGLAIVKKIVERHGGR 481

                        90
                ....*....|....*..
gi 6322147  366 IDVQSLLGWGTDVYIKL 382
Cdd:COG4251 482 IWVESEPGEGATFYFTL 498
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 258-376 4.44e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 39.33  E-value: 4.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  258 PPILEYIMTEVFKNAFEAQIALGKehmpIEINLLKpDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQsadsestdl 337
Cdd:cd16943   1 PSQLNQVLLNLLVNAAQAMEGRGR----ITIRTWA-HVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVG--------- 66

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322147  338 pgeqinnvSGMGFGLPMCKTYLELFGGKIDVQSLLGWGT 376
Cdd:cd16943  67 --------EGTGLGLSLSYRIIQKHGGTIRVASVPGGGT 97
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 264-383 8.35e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 38.67  E-value: 8.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  264 IMTEVFKNAFEAqiALGKEHMPIEINLLKPDDDE--LYLRIRDHGGGITPEVEALMFNySYSThtqqsaDSEStdlpgeq 341
Cdd:cd16944   8 VLTNILKNAAEA--IEGRPSDVGEVRIRVEADQDgrIVLIVCDNGKGFPREMRHRATE-PYVT------TRPK------- 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6322147  342 innvsGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKLK 383
Cdd:cd16944  72 -----GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 293-382 1.51e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 37.69  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  293 PDDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQsaDSEstdlpgeqinnvsGMGFGLPMCKTYLELFGGKIDVQSLL 372
Cdd:cd16921  30 DVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSRE--EYE-------------GTGVGLAIVRKIIERHGGRIWLESEP 94

                        90
                ....*....|
gi 6322147  373 GWGTDVYIKL 382
Cdd:cd16921  95 GEGTTFYFTL 104
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 294-366 3.84e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 3.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322147  294 DDDELYLRIRDHGGGITPEVEALMFNYSYSTHTQQSADSEstdlpgeqinnvsGMGFGLPMCKTYLELFGGKI 366
Cdd:cd16949  27 DGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESG-------------GTGLGLAIAERAIEQHGGKI 86
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
274-382 4.07e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 39.39  E-value: 4.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322147  274 EAQIALGKehmP----IEINLlKPDDDELYLRIRDHGGGI---------------TPEVEALMfnysysthtqqsADSES 334
Cdd:COG0643 298 EERLAAGK---PetgtITLSA-YHEGGRVVIEVSDDGRGLdlekirakaiekgliTAEEAAAL------------SDEEL 361

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6322147  335 TDL---PG----EQINNVSGMGFGLPMCKTYLELFGGKIDVQSLLGWGTDVYIKL 382
Cdd:COG0643 362 LELifaPGfstaEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRL 416
 
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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