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Conserved domains on  [gi|90108887]
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Chain A, PYRUVATE DEHYDROGENASE KINASE ISOENZYME 2

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 ...
 183-348 1.08e-84

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: 254.96  E-value: 1.08e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 183 NVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINaanskqPIHMVYVPSHLYHMLFELFKNAMRATVESHE-SSLILPPIK 261
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGdDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 262 VMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQ--------PGTGGTPLAGFGYGLPISRLYAKYFQGDLQL 333
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSlddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 90108887 334 FSMEGFGTDAVIYLK 348
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 17-179 1.69e-70

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: 218.53  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    17 PLSMKQFLDFGSSNACEKT--SFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHr 94
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDN- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    95 tlSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYgddpvSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKH 174
Cdd:pfam10436  80 --EKFTELLEEILDRHNDVVPTLAQGVLELKKYL-----SPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 90108887   175 -IGSID 179
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 ...
 183-348 1.08e-84

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: 254.96  E-value: 1.08e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 183 NVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINaanskqPIHMVYVPSHLYHMLFELFKNAMRATVESHE-SSLILPPIK 261
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGdDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 262 VMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQ--------PGTGGTPLAGFGYGLPISRLYAKYFQGDLQL 333
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSlddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 90108887 334 FSMEGFGTDAVIYLK 348
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 17-179 1.69e-70

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: 218.53  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    17 PLSMKQFLDFGSSNACEKT--SFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHr 94
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDN- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    95 tlSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYgddpvSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKH 174
Cdd:pfam10436  80 --EKFTELLEEILDRHNDVVPTLAQGVLELKKYL-----SPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 90108887   175 -IGSID 179
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 229-348 1.08e-19

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.47  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    229 PSHLYHMLFELFKNAMRATVEShesslilPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGtggt 308
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI---- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 90108887    309 plAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLK 348
Cdd:smart00387  72 --GGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 228-348 4.61e-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: 70.86  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887   228 VPSHLYHMLFELFKNAMRATVESHEsslilppIKVMVAlGEEDLSIKMSDRGGGVPLRKIERLFSyMYSTAPTPQPGtgg 307
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGE-------ITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG--- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 90108887   308 tplaGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLK 348
Cdd:pfam02518  70 ----GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
182-347 1.08e-10

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 61.46  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKLLCDKYYmaspdleiQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVEShesslilPPIK 261
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKG--------IRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPG-------GTIT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 262 VMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGtggtplaGFGYGLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:COG2205 156 ISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG-------GTGLGLAIVKRIVEAHGGTIWVESEPGGGT 228


                ....*.
gi 90108887 342 DAVIYL 347
Cdd:COG2205 229 TFTVTL 234
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 222-341 4.03e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 48.78  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887  222 PIHMVYVPSHLYHMLFELFKNAMRATVESHesslilppIKVMV-ALGEEDLSIKMSDRGGGVPLRKIERLFSyMYSTAPT 300
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFTQQGG--------VTVRVrYEEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQVKD 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 90108887  301 pqpGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:PRK11091 460 ---SHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGS 497
 
Name Accession Description Interval E-value
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 183-348 1.08e-84

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: 254.96  E-value: 1.08e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 183 NVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINaanskqPIHMVYVPSHLYHMLFELFKNAMRATVESHE-SSLILPPIK 261
Cdd:cd16929   1 SPKKVVEDASEEARVLCDDYYLSSPELEIEGDP------SIRFPYVPSHLYYILFELLKNAMRATVESHGdDSDDLPPIK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 262 VMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQ--------PGTGGTPLAGFGYGLPISRLYAKYFQGDLQL 333
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQPSlddfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDLDL 154

                       170
                ....*....|....*
gi 90108887 334 FSMEGFGTDAVIYLK 348
Cdd:cd16929 155 QSMEGYGTDVYIYLK 169
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 17-179 1.69e-70

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: 218.53  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    17 PLSMKQFLDFGSSNACEKT--SFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHr 94
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDN- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    95 tlSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYgddpvSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKH 174
Cdd:pfam10436  80 --EKFTELLEEILDRHNDVVPTLAQGVLELKKYL-----SPEEIQSFLDRFLRSRIGIRLLAEQHIALTEQSNNPSHPPD 152


                  ....*.
gi 90108887   175 -IGSID 179
Cdd:pfam10436 153 yVGIID 158
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 229-348 1.08e-19

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.47  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887    229 PSHLYHMLFELFKNAMRATVEShesslilPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGtggt 308
Cdd:smart00387   3 PDRLRQVLSNLLDNAIKYTPEG-------GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKI---- 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 90108887    309 plAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLK 348
Cdd:smart00387  72 --GGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 228-348 4.61e-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: 70.86  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887   228 VPSHLYHMLFELFKNAMRATVESHEsslilppIKVMVAlGEEDLSIKMSDRGGGVPLRKIERLFSyMYSTAPTPQPGtgg 307
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGE-------ITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFE-PFSTADKRGGG--- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 90108887   308 tplaGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLK 348
Cdd:pfam02518  70 ----GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
182-347 1.08e-10

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 61.46  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKLLCDKYYmaspdleiQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVEShesslilPPIK 261
Cdd:COG2205  91 VDLAELLEEAVEELRPLAEEKG--------IRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPG-------GTIT 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 262 VMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGtggtplaGFGYGLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:COG2205 156 ISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEG-------GTGLGLAIVKRIVEAHGGTIWVESEPGGGT 228


                ....*.
gi 90108887 342 DAVIYL 347
Cdd:COG2205 229 TFTVTL 234
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
183-347 2.98e-10

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 61.08  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 183 NVSEVVKDAYDMAKLLCdkyymASPDLEIqEINAANSKQPIHMVyvPSHLYHMLFELFKNAMRATVESHesslilpPIKV 262
Cdd:COG0642 183 DLAELLEEVVELFRPLA-----EEKGIEL-ELDLPDDLPTVRGD--PDRLRQVLLNLLSNAIKYTPEGG-------TVTV 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 263 MVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGtggtplaGFGYGLPISRLYAKYFQGDLQLFSMEGFGTD 342
Cdd:COG0642 248 SVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGG-------GTGLGLAIVKRIVELHGGTIEVESEPGKGTT 320


                ....*
gi 90108887 343 AVIYL 347
Cdd:COG0642 321 FTVTL 325
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 182-347 8.58e-07

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 50.57  E-value: 8.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKLLCdKYYMASPDLEIQEinaanskqPIHMVYV-PSHLYHMLFELFKNAMRATVESHEsslilPPI 260
Cdd:COG4191 215 VDLNELIDEALELLRPRL-KARGIEVELDLPP--------DLPPVLGdPGQLEQVLLNLLINAIDAMEEGEG-----GRI 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 261 KVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQpGTGgtpLagfgyGLPISRLYAKYFQGDLQLFSMEGFG 340
Cdd:COG4191 281 TISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGK-GTG---L-----GLSISYGIVEKHGGRIEVESEPGGG 351


                ....*..
gi 90108887 341 TDAVIYL 347
Cdd:COG4191 352 TTFTITL 358
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 239-347 1.61e-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: 46.13  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 239 LFKNAMRATVESHEsslilPPIKVMVALGEE--DLSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpgtggtplAGFGYG 316
Cdd:cd16915   8 LIDNALDALAATGA-----PNKQVEVFLRDEgdDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ----------GERGIG 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 90108887 317 LPISRLYAKYFQGDLQLFSMEGFGTDAVIYL 347
Cdd:cd16915  73 LALVRQSVERLGGSITVESEPGGGTTFSIRI 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 197-347 3.18e-06

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 48.69  E-value: 3.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 197 LLCDKYYMAS---PDLEIqEINAANSKQPIhmvyVPSHLYHMLFELFKNAMRATVESHESSlilPPIKVMVALGEEDLSI 273
Cdd:COG3290 249 LLLGKAARARergIDLTI-DIDSDLPDLPL----SDTDLVTILGNLLDNAIEAVEKLPEEE---RRVELSIRDDGDELVI 320

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90108887 274 KMSDRGGGVPLRKIERLFSYMYSTaptpqPGTGGTplagfGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYL 347
Cdd:COG3290 321 EVEDSGPGIPEELLEKIFERGFST-----KLGEGR-----GLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 232-347 3.60e-06

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: 45.47  E-value: 3.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 232 LYHMLFELFKNAMRATVESHesslilppiKVMVALGEEDLS-IKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTggtpl 310
Cdd:cd16940  14 LFLLLRNLVDNAVRYSPQGS---------RVEIKLSADDGAvIRVEDNGPGIDEEELEALFERFYRSDGQNYGGS----- 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 90108887 311 agfGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYL 347
Cdd:cd16940  80 ---GLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 222-341 4.03e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 48.78  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887  222 PIHMVYVPSHLYHMLFELFKNAMRATVESHesslilppIKVMV-ALGEEDLSIKMSDRGGGVPLRKIERLFSyMYSTAPT 300
Cdd:PRK11091 389 PHKVITDGTRLRQILWNLISNAVKFTQQGG--------VTVRVrYEEGDMLTFEVEDSGIGIPEDELDKIFA-MYYQVKD 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 90108887  301 pqpGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:PRK11091 460 ---SHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGS 497
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 182-347 7.71e-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: 7.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKllcdkyymasPDLEIQEIN-AANSKQPIHMVYV-PSHLYHMLFELFKNAMRATVEShesslilPP 259
Cdd:COG5000 276 VDLNELLREVLALYE----------PALKEKDIRlELDLDPDLPEVLAdRDQLEQVLINLLKNAIEAIEEG-------GE 338

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 260 IKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpGTggtplagfGYGLPISRLYAKYFQGDLQLFSMEGF 339
Cdd:COG5000 339 IEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPK---GT--------GLGLAIVKKIVEEHGGTIELESRPGG 407


                ....*...
gi 90108887 340 GTDAVIYL 347
Cdd:COG5000 408 GTTFTIRL 415
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 260-333 2.93e-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: 42.83  E-value: 2.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90108887 260 IKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTaPTPQPGTGGTplagfGYGLPISRLYAKYFQGDLQL 333
Cdd:cd16945  26 IALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSL-PRPHSGQKST-----GLGLAFVQEVAQLHGGRITL 93
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
182-349 3.15e-05

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 45.70  E-value: 3.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKLLCDKYymaspDLEIQeinaANSKQPIHMVYV-PSHLYHMLFELFKNAMRATVESHEsslilppI 260
Cdd:COG5002 240 VDLAELLEEVVEELRPLAEEK-----GIELE----LDLPEDPLLVLGdPDRLEQVLTNLLDNAIKYTPEGGT-------I 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 261 KVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTplagfGYGLPISRLYAKYFQGDLQLFSMEGFG 340
Cdd:COG5002 304 TVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGT-----GLGLAIVKHIVEAHGGRIWVESEPGKG 378


                ....*....
gi 90108887 341 TDAVIYLKA 349
Cdd:COG5002 379 TTFTITLPL 387
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 236-341 1.88e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 40.46  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 236 LFELFKNAMRATVESHESSLILPpIKVMVAlGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpgtggtplaGFGY 315
Cdd:cd16920   5 LINLVRNGIEAMSEGGCERRELT-IRTSPA-DDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE-----------GLGM 71

                        90       100
                ....*....|....*....|....*.
gi 90108887 316 GLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:cd16920  72 GLSICRSIIEAHGGRLSVESPAGGGA 97
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 271-347 3.64e-04

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: 40.06  E-value: 3.64e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90108887 271 LSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpgtggtplaGFGYGLPISRLY--AKYFQGDLQLFSMEGFGTDAVIYL 347
Cdd:cd16919  48 VCLEVSDTGSGMPAEVLRRAFEPFFTTKEV-----------GKGTGLGLSMVYgfVKQSGGHLRIYSEPGVGTTVRIYL 115
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 231-335 1.43e-03

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 40.83  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 231 HLYHMLFELFKNAMRATVEShesslilPPIKVMVALGEEDLSIKMSDRGGGVPLrkIERLFSYMYSTAPTpqpgtggtpl 310
Cdd:COG4192 543 LLEQVLVNLLVNALDAVATQ-------PQISVDLLSNAENLRVAISDNGNGWPL--VDKLFTPFTTTKEV---------- 603

                        90       100
                ....*....|....*....|....*
gi 90108887 311 aGFGYGLPISRLYAKYFQGDLQLFS 335
Cdd:COG4192 604 -GLGLGLSICRSIMQQFGGDLYLAS 627
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 239-347 1.54e-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: 40.34  E-value: 1.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 239 LFKNAMRATVEshesslilpPIKVMVALGEED---LSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpgtgGTplagfGY 315
Cdd:COG5809 387 LLKNAIEAMPE---------GGNITIETKAEDddkVVISVTDEGCGIPEERLKKLGEPFYTTKEK------GT-----GL 446

                        90       100       110
                ....*....|....*....|....*....|..
gi 90108887 316 GLPISRLYAKYFQGDLQLFSMEGFGTDAVIYL 347
Cdd:COG5809 447 GLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
236-354 2.33e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 39.95  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887  236 LFELFKNAMRATVESHEsslilppIKVMVAL-GEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpGTggtplagfG 314
Cdd:PRK11360 505 LLNILINAVQAISARGK-------IRIRTWQySDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK---GT--------G 566

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 90108887  315 YGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDS 354
Cdd:PRK11360 567 LGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGN 606
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 235-341 3.17e-03

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


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 37.09  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 235 MLFELFKNAMRATVESHesslilppIKVMVALGEED-----LSIKMSDRGGGVPLRKIERLFSyMYSTAPTP-QPGTGGT 308
Cdd:cd16922   4 ILLNLLGNAIKFTEEGE--------VTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFE-PFSQADSStTRKYGGT 74

                        90       100       110
                ....*....|....*....|....*....|...
gi 90108887 309 plagfGYGLPISRLYAKYFQGDLQLFSMEGFGT 341
Cdd:cd16922  75 -----GLGLAISKKLVELMGGDISVESEPGQGS 102
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
 260-351 4.77e-03

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 39.06  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887  260 IKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYStapTPQPGTG--GTplagfGYGLPISRLYAKYFQGDLQLFSME 337
Cdd:PRK11100 390 ITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYS---LPRPANGrkST-----GLGLAFVREVARLHGGEVTLRNRP 461

                         90
                 ....*....|....
gi 90108887  338 GFGTDAVIYLKALS 351
Cdd:PRK11100 462 EGGVLATLTLPRHF 475
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
182-354 8.13e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 37.90  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 182 CNVSEVVKDAYDMAKLLCDKyymaspDLEIQEiNAANSkqpIHMVYV-PSHLYHMLFELFKNAMRATVESHE---SSLIL 257
Cdd:COG3852 204 VNLHEVLERVLELLRAEAPK------NIRIVR-DYDPS---LPEVLGdPDQLIQVLLNLVRNAAEAMPEGGTitiRTRVE 273

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90108887 258 PPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTpqpGTGgtpLagfgyGLPISRLYAKYFQGDLQLFSME 337
Cdd:COG3852 274 RQVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKEK---GTG---L-----GLAIVQKIVEQHGGTIEVESEP 342

                       170
                ....*....|....*..
gi 90108887 338 GFGTDAVIYLKALSTDS 354
Cdd:COG3852 343 GKGTTFRIYLPLEQAEE 359
 
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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