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Conserved domains on  [gi|1693393703|ref|WP_140171708|]
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MULTISPECIES: AraC family transcriptional regulator [Providencia]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 1567310)

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
GlxA super family cl34854
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 119-226 3.54e-27

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


The actual alignment was detected with superfamily member COG4977:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 106.01  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 119 LLAQLKPENKWIDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL-SNKSIEQ 197
Cdd:COG4977   201 LLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLEtTDLSIEE 280

                          90       100
                  ....*....|....*....|....*....
gi 1693393703 198 IALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:COG4977   281 IAAACGFGSASHFRRAFRRRFGVSPSAYR 309
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 9-75 2.31e-09

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.


The actual alignment was detected with superfamily member cd07003:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 66  Bit Score: 52.01  E-value: 2.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693393703   9 RQYSDEVISHQHDGQwQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAFSGQLGNQNYVLEMP 75
Cdd:cd07003     1 RTYSHDQSSHSHEHA-QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 119-226 3.54e-27

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: 106.01  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 119 LLAQLKPENKWIDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL-SNKSIEQ 197
Cdd:COG4977   201 LLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLEtTDLSIEE 280

                          90       100
                  ....*....|....*....|....*....
gi 1693393703 198 IALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:COG4977   281 IAAACGFGSASHFRRAFRRRFGVSPSAYR 309
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
144-226 2.41e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 94.93  E-value: 2.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703  144 PISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL-SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTP 222
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRdTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1693393703  223 NEYR 226
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
150-226 3.09e-23

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 89.19  E-value: 3.09e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693393703 150 MATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL--SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
ftrA PRK09393
transcriptional activator FtrA; Provisional
 133-228 1.11e-14

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 71.53  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 133 LSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLLSNK-SIEQIALAVGYDSHSAFS 211
Cdd:PRK09393  223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSAlSIDQIAERAGFGSEESLR 302

                          90
                  ....*....|....*..
gi 1693393703 212 HAFRQFYSKTPNEYRLQ 228
Cdd:PRK09393  303 HHFRRRAATSPAAYRKR 319
cupin_YobQ-like_N cd07003
Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes ...
 9-75 2.31e-09

Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380407 [Multi-domain]  Cd Length: 66  Bit Score: 52.01  E-value: 2.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693393703   9 RQYSDEVISHQHDGQwQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAFSGQLGNQNYVLEMP 75
Cdd:cd07003     1 RTYSHDQSSHSHEHA-QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
18-61 4.54e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 38.29  E-value: 4.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1693393703  18 HQHDGQwQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAF 61
Cdd:COG1917    39 HSHPGE-ELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAF 81
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 17-61 7.06e-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: 34.16  E-value: 7.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1693393703  17 SHQHDGQWQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAF 61
Cdd:pfam07883  13 PHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 119-226 3.54e-27

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: 106.01  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 119 LLAQLKPENKWIDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL-SNKSIEQ 197
Cdd:COG4977   201 LLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLEtTDLSIEE 280

                          90       100
                  ....*....|....*....|....*....
gi 1693393703 198 IALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:COG4977   281 IAAACGFGSASHFRRAFRRRFGVSPSAYR 309
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
144-226 2.41e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 94.93  E-value: 2.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703  144 PISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL-SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTP 222
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRdTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1693393703  223 NEYR 226
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
105-233 2.05e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 97.54  E-value: 2.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 105 FPQAPEHNFTVARLLLAQLKPENKWIDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEA 184
Cdd:COG2207   129 ALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLER 208

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1693393703 185 AGRLLL-SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYRLQGSHLR 233
Cdd:COG2207   209 AKRLLAeTDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
150-226 3.09e-23

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 89.19  E-value: 3.09e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693393703 150 MATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLL--SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 129-229 1.29e-17

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: 80.48  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 129 WIDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLLSNKSIEQIALAVGYDSHS 208
Cdd:COG2169    85 LVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGFGSLS 164

                          90       100
                  ....*....|....*....|.
gi 1693393703 209 AFSHAFRQFYSKTPNEYRLQG 229
Cdd:COG2169   165 RFYEAFKKLLGMTPSAYRRGG 185
ftrA PRK09393
transcriptional activator FtrA; Provisional
 133-228 1.11e-14

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 71.53  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 133 LSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLLLSNK-SIEQIALAVGYDSHSAFS 211
Cdd:PRK09393  223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSAlSIDQIAERAGFGSEESLR 302

                          90
                  ....*....|....*..
gi 1693393703 212 HAFRQFYSKTPNEYRLQ 228
Cdd:PRK09393  303 HHFRRRAATSPAAYRKR 319
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
130-226 2.41e-11

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 58.78  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 130 IDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKR-MEAAGRLLLSNKSIEQIALAVGYDSHS 208
Cdd:PRK10219    7 IQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRlLLAAVELRTTERPIFDIAMDLGYVSQQ 86

                          90
                  ....*....|....*...
gi 1693393703 209 AFSHAFRQFYSKTPNEYR 226
Cdd:PRK10219   87 TFSRVFRRQFDRTPSDYR 104
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 137-228 3.63e-10

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 58.17  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 137 VELRLHHPISCEDMATAFCMSVSTLQRKIKAEtQLTAMQFLLQKRMEAAGRLLLSNKSIEQIALAVGYDSHSAFSHAFRQ 216
Cdd:PRK09940  143 VNMKLAHPWKLKDICDCLYISESLLKKKLKQE-QTTFSQILLDARMQHAKNLIRVEGSVNKIAEQCGYASTSYFIYAFRK 221

                          90
                  ....*....|....*.
gi 1693393703 217 FYSKTP----NEYRLQ 228
Cdd:PRK09940  222 HFGNSPkrvsKEYRCQ 237
cupin_YobQ-like_N cd07003
Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes ...
 9-75 2.31e-09

Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380407 [Multi-domain]  Cd Length: 66  Bit Score: 52.01  E-value: 2.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693393703   9 RQYSDEVISHQHDGQwQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAFSGQLGNQNYVLEMP 75
Cdd:cd07003     1 RTYSHDQSSHSHEHA-QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 148-231 4.04e-09

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 55.77  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 148 EDMATAFCMSVSTLQRKIkAETQLTAMQFLLQKRMEAAGRLL-LSNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:PRK15185  226 TDVADHIFMSTSTLKRKL-AEEGTSFSDIYLSARMNQAAKLLrIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTFI 304


                  ....*
gi 1693393703 227 LQGSH 231
Cdd:PRK15185  305 KMANH 309
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 150-231 1.21e-08

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 54.16  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 150 MATAFCMSVSTLQRKIKAEtQLTAMQFLLQKRMEAAGRLL-LSNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYRLQ 228
Cdd:PRK09978  164 IASELLMSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIvIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQER 242


                  ...
gi 1693393703 229 GSH 231
Cdd:PRK09978  243 SAQ 245
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
130-231 3.67e-08

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 50.49  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 130 IDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRM-EAAGRLLLSNKSIEQIALAVGYDSHS 208
Cdd:PRK11511   11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMtEIAQKLKESNEPILYLAERYGFESQQ 90

                          90       100
                  ....*....|....*....|...
gi 1693393703 209 AFSHAFRQFYSKTPNEYRLQGSH 231
Cdd:PRK11511   91 TLTRTFKNYFDVPPHKYRMTNMQ 113
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
130-228 4.20e-08

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 52.37  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 130 IDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKR-MEAAGRLLLSNKSIEQIALAVGYDSHS 208
Cdd:PRK13503  173 LNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRlLKARHLLRHSDASVTDIAYRCGFGDSN 252

                          90       100
                  ....*....|....*....|
gi 1693393703 209 AFSHAFRQFYSKTPNEYRLQ 228
Cdd:PRK13503  253 HFSTLFRREFSWSPRDIRQG 272
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 148-225 2.09e-07

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 50.45  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693393703 148 EDMATAFCMSVSTLQRKIKAEtQLTAMQFLLQKRMEAAGRLLL-SNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEY 225
Cdd:PRK15186  201 KDISDSLYMSCSTLKRKLKQE-NTSFSEVYLNARMNKATKLLRnSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
130-226 6.68e-06

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 45.77  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 130 IDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRM-EAAGRLLLSNKSIEQIALAVGYDSHS 208
Cdd:PRK15121    7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLsKAAVALRLTSRPILDIALQYRFDSQQ 86

                          90
                  ....*....|....*...
gi 1693393703 209 AFSHAFRQFYSKTPNEYR 226
Cdd:PRK15121   87 TFTRAFKKQFAQTPALYR 104
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 189-226 7.87e-06

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 41.76  E-value: 7.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1693393703 189 LLSNKSIEQIALAVGYDShSAFSHAFRQFYSKTPNEYR 226
Cdd:pfam00165   5 LSTNLTIADIADELGFSR-SYFSRLFKKYTGVTPSQYR 41
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 18-226 1.50e-05

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 44.75  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703  18 HQHDG-QWQVVLSLSGQMEINMYRqhFLLNAGKGVVIPPSVSH--------------AFSGQLGNQNYVLEMPA--TAQW 80
Cdd:PRK10296   39 HQHDYyEFTLVLTGRYYQEINGKR--VLLERGDFVFIPLGSHHqsfyefgatrilnvGISKRFFEQHYLPLLPYcfVASQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703  81 ALNEKMTQFTLTPAAIGLLNWLQNfpQAPEHNFTVARLLLAQLK--PENKWIDELSQWVE--LRLHHPIS------CEDM 150
Cdd:PRK10296  117 VYRTNNAFLTYIETVISSLNFRET--GLDEFVELVTFYVINRLRhyREEQVIDDIPQWLKatVEKMHDKEqfsesaLENM 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693393703 151 ATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAGRLL-LSNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYR 226
Cdd:PRK10296  195 VRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLeMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYR 271
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
 146-222 6.35e-05

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 43.10  E-value: 6.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693393703 146 SCEDMATAFCMSVSTLQRKIKAEtQLTAMQFLLQKRMEAAGRLL-LSNKSIEQIALAVGYDSHSAFSHAFRQFYSKTP 222
Cdd:PRK15044  210 SQAEVAGKLFMSVSSLKRKLAAE-EVSFSKIYLDARMNQAIKLLrMGAGNISQVATMCGYDTPSYFIAIFKRHFKITP 286
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 18-61 7.60e-05

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: 39.77  E-value: 7.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1693393703  18 HQHDGQWQVVLSLSGQMEINMY-RQHFLLNAGKGVVIPPSVSHAF 61
Cdd:cd02208    15 HWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSF 59
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
130-226 1.27e-04

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 42.27  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 130 IDELSQWVELRLHHPISCEDMATAFCMSVSTLQRKIKAETQLTAMQFLLQKRMEAAgRLLLS--NKSIEQIALAVGYDSH 207
Cdd:PRK10572  185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRA-KLLLQttRMPIATIGRNVGYDDQ 263

                          90
                  ....*....|....*....
gi 1693393703 208 SAFSHAFRQFYSKTPNEYR 226
Cdd:PRK10572  264 LYFSRVFKKCTGASPSEFR 282
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 156-228 1.91e-04

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 41.56  E-value: 1.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693393703 156 MSVSTLQRkIKAETQLTAMQFLLQKRME---AAGRLLLSNKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYRLQ 228
Cdd:PRK09685  226 ISVRSLYR-LFAEQGLVVAQYIRNRRLDrcaDDLRPAADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRK 300
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
18-61 4.54e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 38.29  E-value: 4.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1693393703  18 HQHDGQwQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAF 61
Cdd:COG1917    39 HSHPGE-ELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAF 81
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
18-61 6.60e-04

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 38.20  E-value: 6.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1693393703  18 HQHDGQWQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAF 61
Cdd:COG0662    43 HVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRL 86
PRK10371 PRK10371
transcriptional regulator MelR;
170-227 2.63e-03

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 38.26  E-value: 2.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703 170 QLTAMQFLLQKRMEAAgRLLLS--NKSIEQIALAVGYDSHSAFSHAFRQFYSKTPNEYRL 227
Cdd:PRK10371  233 QLTMKQYITAMRINHV-RALLSdtDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 18-77 4.47e-03

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: 35.55  E-value: 4.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693393703  18 HQHDGQWQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAFSGQLGNQNYVLEMPAT 77
Cdd:cd06999    38 HRHADLFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHGFRFSPDTDGHVLTLADP 97
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 17-61 7.06e-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: 34.16  E-value: 7.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1693393703  17 SHQHDGQWQVVLSLSGQMEINMYRQHFLLNAGKGVVIPPSVSHAF 61
Cdd:pfam07883  13 PHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57
 
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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