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Conserved domains on  [gi|2769203230|ref|WP_366141484|]
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helix-turn-helix transcriptional regulator [uncultured Sulfitobacter sp.]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 14398448)

AraC family transcriptional regulator containing a cupin domain as its effector domain and an AraC family helix-turn-helix (HTH) DNA binding domain, controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

CATH:  2.60.120.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0043565
PubMed:  11282467|33837749|9409145|12270809|19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 4-97 4.10e-25

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


:

Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 94.95  E-value: 4.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230   4 IVGLGSAYDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMRTAYL--SRAYPL 81
Cdd:cd06124     1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIdpEAAAGL 80

                          90
                  ....*....|....*.
gi 2769203230  82 PHKnVRVLSVSPLMRE 97
Cdd:cd06124    81 PAE-PCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
160-238 8.25e-21

Helix-turn-helix domain;


:

Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.41  E-value: 8.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 160 WAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKL--SAGQSVTETAFDVGFETPSAFIHAFHTLIGETPGQFMG 237
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLleDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2769203230 238 R 238
Cdd:pfam12833  81 R 81
 
Name Accession Description Interval E-value
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 4-97 4.10e-25

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 94.95  E-value: 4.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230   4 IVGLGSAYDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMRTAYL--SRAYPL 81
Cdd:cd06124     1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIdpEAAAGL 80

                          90
                  ....*....|....*.
gi 2769203230  82 PHKnVRVLSVSPLMRE 97
Cdd:cd06124    81 PAE-PCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
160-238 8.25e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.41  E-value: 8.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 160 WAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKL--SAGQSVTETAFDVGFETPSAFIHAFHTLIGETPGQFMG 237
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLleDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2769203230 238 R 238
Cdd:pfam12833  81 R 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 135-235 4.61e-19

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 84.72  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 135 PSDPRIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQSVTETAFDVGF 214
Cdd:COG2169    81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGF 160

                          90       100
                  ....*....|....*....|.
gi 2769203230 215 ETPSAFIHAFHTLIGETPGQF 235
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAY 181
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
16-235 1.06e-18

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 82.52  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  16 HIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMRTAYLSRAYPLPHKNVRVLSVSPLM 95
Cdd:COG2207    38 LLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  96 REVLIRLAEGHEQRLNILLADLLvheigegkLESLKIPIPSDPRIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSI 175
Cdd:COG2207   118 LLLLLLLLLLLALLRALELLLLL--------LLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769203230 176 RAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFDVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:COG2207   190 KEETGTSPKQYLRELRLERAKRLLAETDlSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
156-236 1.07e-17

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 75.28  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  156 TLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFDVGFETPSAFIHAFHTLIGETPGQ 234
Cdd:smart00342   3 TLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTPSE 82


                   ..
gi 2769203230  235 FM 236
Cdd:smart00342  83 YR 84
ftrA PRK09393
transcriptional activator FtrA; Provisional
 133-235 2.41e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 50.73  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 133 PIPSDP--RIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKL-SAGQSVTETA 209
Cdd:PRK09393  211 PVASREsdRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLeSSALSIDQIA 290

                          90       100
                  ....*....|....*....|....*.
gi 2769203230 210 FDVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:PRK09393  291 ERAGFGSEESLRHHFRRRAATSPAAY 316
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 11-71 5.40e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 34.54  E-value: 5.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769203230  11 YDAGTHIAPHAHTAH-QIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMR 71
Cdd:pfam07883   5 LPPGESSPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPAR 66
 
Name Accession Description Interval E-value
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 4-97 4.10e-25

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 94.95  E-value: 4.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230   4 IVGLGSAYDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMRTAYL--SRAYPL 81
Cdd:cd06124     1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIdpEAAAGL 80

                          90
                  ....*....|....*.
gi 2769203230  82 PHKnVRVLSVSPLMRE 97
Cdd:cd06124    81 PAE-PCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
160-238 8.25e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.41  E-value: 8.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 160 WAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKL--SAGQSVTETAFDVGFETPSAFIHAFHTLIGETPGQFMG 237
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLleDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2769203230 238 R 238
Cdd:pfam12833  81 R 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 135-235 4.61e-19

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 84.72  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 135 PSDPRIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQSVTETAFDVGF 214
Cdd:COG2169    81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGF 160

                          90       100
                  ....*....|....*....|.
gi 2769203230 215 ETPSAFIHAFHTLIGETPGQF 235
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAY 181
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
16-235 1.06e-18

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 82.52  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  16 HIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMRTAYLSRAYPLPHKNVRVLSVSPLM 95
Cdd:COG2207    38 LLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  96 REVLIRLAEGHEQRLNILLADLLvheigegkLESLKIPIPSDPRIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSI 175
Cdd:COG2207   118 LLLLLLLLLLLALLRALELLLLL--------LLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769203230 176 RAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFDVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:COG2207   190 KEETGTSPKQYLRELRLERAKRLLAETDlSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
156-236 1.07e-17

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 75.28  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230  156 TLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFDVGFETPSAFIHAFHTLIGETPGQ 234
Cdd:smart00342   3 TLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTPSE 82


                   ..
gi 2769203230  235 FM 236
Cdd:smart00342  83 YR 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 135-235 1.40e-12

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 65.95  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 135 PSDPRIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSIRAETGMTFRE-LRRLsRVMVALDKL-SAGQSVTETAFDV 212
Cdd:COG4977   207 HRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARyLQRL-RLERARRLLeTTDLSIEEIAAAC 285

                          90       100
                  ....*....|....*....|...
gi 2769203230 213 GFETPSAFIHAFHTLIGETPGQF 235
Cdd:COG4977   286 GFGSASHFRRAFRRRFGVSPSAY 308
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
11-71 9.30e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 51.77  E-value: 9.30e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769203230  11 YDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMR 71
Cdd:COG1917    30 FEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAV 90
ftrA PRK09393
transcriptional activator FtrA; Provisional
 133-235 2.41e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 50.73  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 133 PIPSDP--RIAKLALHFQTAPDDRTTLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKL-SAGQSVTETA 209
Cdd:PRK09393  211 PVASREsdRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLeSSALSIDQIA 290

                          90       100
                  ....*....|....*....|....*.
gi 2769203230 210 FDVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:PRK09393  291 ERAGFGSEESLRHHFRRRAATSPAAY 316
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
11-71 6.16e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 38.58  E-value: 6.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769203230  11 YDAGTHIAPHAHTAH-QIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMR 71
Cdd:COG0662    34 VPPGAELSLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLE 95
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 10-70 8.81e-04

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 37.10  E-value: 8.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769203230  10 AYDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDM 70
Cdd:cd02230    17 AFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKM 77
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 16-61 8.88e-04

AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, similar to Escherichia coli 4-hydroxyphenylacetate catabolism regulatory protein HpaA (also known as 4HPA). HpaA is encoded by the hpaA gene which is located upstream of hpaBC. It is activated by 4-HPA, 3-HPA and phenylacetate, and represents a member of the AraC/XylS family of regulators that recognizes aromatic effectors. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380403 [Multi-domain]  Cd Length: 98  Bit Score: 37.48  E-value: 8.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2769203230  16 HIAPHAHTA-HQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHA 61
Cdd:cd06999    34 EIAPHRHADlFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHG 80
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 139-236 1.07e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 39.59  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 139 RIAKLALHFQ------TAPDDRTTLKHWAKRLGYSERSLIRSIrAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFD 211
Cdd:PRK15185  201 SSAQITLKERvyniisSSPSRQWKLTDVADHIFMSTSTLKRKL-AEEGTSFSDIYLSARMNQAAKLLRIGNhNVNAVALK 279

                          90       100
                  ....*....|....*....|....*
gi 2769203230 212 VGFETPSAFIHAFHTLIGETPGQFM 236
Cdd:PRK15185  280 CGYDSTSYFIQCFKKYFKTTPSTFI 304
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
135-235 1.16e-03

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 39.39  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 135 PSDPRIAKLA----LHFQTAPddrTTLKHWAKRLGYSERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQSVTETAF 210
Cdd:PRK15435   79 PQQHRLDKIThacrLLEQETP---VTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSIL 155

                          90       100
                  ....*....|....*....|....*
gi 2769203230 211 DVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:PRK15435  156 NAGFPDSSSYYRKADETLGMTAKQF 180
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 11-68 2.26e-03

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 36.68  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2769203230  11 YDAGTHIAPHAHTAHQIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPV 68
Cdd:cd02238    34 FEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALEDS 91
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 11-71 5.40e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 34.54  E-value: 5.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769203230  11 YDAGTHIAPHAHTAH-QIAHAISGTMRVTVHDFVWFVPTGRALWIPAMTLHAIDCVGPVDMR 71
Cdd:pfam07883   5 LPPGESSPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPAR 66
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
167-235 6.64e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 36.96  E-value: 6.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769203230 167 SERSLIRSIRAETGMTFRELRRLSRVMVALDKLSAGQ-SVTETAFDVGFETPSAFIHAFHTLIGETPGQF 235
Cdd:PRK13502  205 SERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPlMISEISMQCGFEDSNYFSVVFTRETGMTPSQW 274
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 12-76 8.81e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 34.38  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2769203230  12 DAGTHIAPHAHTAH-QIAHAISGTMRVTVHDFVWF-VPTGRALWIPAMTLHAIDCVGPVDMRTAYLS 76
Cdd:cd02208     7 PPGTSSPPHWHPEQdEIFYVLSGEGELTLDDGETVeLKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
 
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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