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Conserved domains on  [gi|446457466|ref|WP_000535320|]
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AraC family transcriptional regulator [Acinetobacter baumannii]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 15746445)

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
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
91-281 1.25e-25

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.17  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466  91 QMLHLDLAWLNQLYSEFQEQGLDLHIPQHKPLIIKDESLYEAFTEMNETLFDAQKLIFEKEQSLLHCLIHLLLPHFILEE 170
Cdd:COG2207   65 LLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 171 IQKPQYLYKDFLNLIDVISSSEVFISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELA 249
Cdd:COG2207  145 LLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETdLSISEIA 224

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446457466 250 VNLGFSDQSHFHKAFKAHTGVTPRQFQLAAAQ 281
Cdd:COG2207  225 YELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 20-103 4.13e-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 pfam02311:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 134  Bit Score: 53.98  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466   20 PYVETRRSCFGRTCYKSHSHPTFSIGAIDEGNSVFQSSFGTaQKITAGTLVIVPAHVEHSCNPMPNQAWSYQMLHLDLAW 99
Cdd:pfam02311   2 PGLEGIEARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRT-YHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPEL 80


                  ....
gi 446457466  100 LNQL 103
Cdd:pfam02311  81 LERI 84
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
91-281 1.25e-25

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.17  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466  91 QMLHLDLAWLNQLYSEFQEQGLDLHIPQHKPLIIKDESLYEAFTEMNETLFDAQKLIFEKEQSLLHCLIHLLLPHFILEE 170
Cdd:COG2207   65 LLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 171 IQKPQYLYKDFLNLIDVISSSEVFISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELA 249
Cdd:COG2207  145 LLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETdLSISEIA 224

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446457466 250 VNLGFSDQSHFHKAFKAHTGVTPRQFQLAAAQ 281
Cdd:COG2207  225 YELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
195-275 2.37e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 96.08  E-value: 2.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466   195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTdLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ..
gi 446457466   274 QF 275
Cdd:smart00342  82 EY 83
HTH_18 pfam12833
Helix-turn-helix domain;
200-276 7.11e-23

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 89.57  E-value: 7.11e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446457466  200 LAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQ--GVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQFQ 276
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 194-276 7.28e-16

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 76.64  E-value: 7.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466  194 FISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:TIGR04094 301 PLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQIPVSEVSNELGFYDLSHFSRTFKKHTGVSPK 380


                  ...
gi 446457466  274 QFQ 276
Cdd:TIGR04094 381 QYQ 383
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
195-276 1.76e-12

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 66.74  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQ 274
Cdd:PRK15435 100 VTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQ 179


                 ..
gi 446457466 275 FQ 276
Cdd:PRK15435 180 FR 181
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 20-103 4.13e-09

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 53.98  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466   20 PYVETRRSCFGRTCYKSHSHPTFSIGAIDEGNSVFQSSFGTaQKITAGTLVIVPAHVEHSCNPMPNQAWSYQMLHLDLAW 99
Cdd:pfam02311   2 PGLEGIEARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRT-YHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPEL 80


                  ....
gi 446457466  100 LNQL 103
Cdd:pfam02311  81 LERI 84
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
91-281 1.25e-25

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 102.17  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466  91 QMLHLDLAWLNQLYSEFQEQGLDLHIPQHKPLIIKDESLYEAFTEMNETLFDAQKLIFEKEQSLLHCLIHLLLPHFILEE 170
Cdd:COG2207   65 LLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 171 IQKPQYLYKDFLNLIDVISSSEVFISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELA 249
Cdd:COG2207  145 LLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETdLSISEIA 224

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446457466 250 VNLGFSDQSHFHKAFKAHTGVTPRQFQLAAAQ 281
Cdd:COG2207  225 YELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
195-275 2.37e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 96.08  E-value: 2.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466   195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTdLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ..
gi 446457466   274 QF 275
Cdd:smart00342  82 EY 83
HTH_18 pfam12833
Helix-turn-helix domain;
200-276 7.11e-23

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 89.57  E-value: 7.11e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446457466  200 LAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQ--GVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQFQ 276
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 182-275 2.10e-22

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: 95.12  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 182 LNLIDviSSSEVFISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQGVPLAELAVNLGFSDQSHFH 261
Cdd:COG2169   90 CRLIE--AGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGFGSLSRFY 167

                         90
                 ....*....|....
gi 446457466 262 KAFKAHTGVTPRQF 275
Cdd:COG2169  168 EAFKKLLGMTPSAY 181
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 195-281 1.25e-21

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: 92.14  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELAVNLGFSDQSHFHKAFKAHTGVTP- 272
Cdd:COG4977  227 LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTdLSIEEIAAACGFGSASHFRRAFRRRFGVSPs 306

                         90
                 ....*....|..
gi 446457466 273 ---RQFQLAAAQ 281
Cdd:COG4977  307 ayrRRFRARAAA 318
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 194-276 7.28e-16

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 76.64  E-value: 7.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466  194 FISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:TIGR04094 301 PLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQIPVSEVSNELGFYDLSHFSRTFKKHTGVSPK 380


                  ...
gi 446457466  274 QFQ 276
Cdd:TIGR04094 381 QYQ 383
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
195-276 1.76e-12

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 66.74  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQ 274
Cdd:PRK15435 100 VTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFPDSSSYYRKADETLGMTAKQ 179


                 ..
gi 446457466 275 FQ 276
Cdd:PRK15435 180 FR 181
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
195-275 3.96e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 56.14  E-value: 3.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQL-KQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:PRK10572 200 FDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLqTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPS 279


                 ..
gi 446457466 274 QF 275
Cdd:PRK10572 280 EF 281
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 20-103 4.13e-09

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 53.98  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466   20 PYVETRRSCFGRTCYKSHSHPTFSIGAIDEGNSVFQSSFGTaQKITAGTLVIVPAHVEHSCNPMPNQAWSYQMLHLDLAW 99
Cdd:pfam02311   2 PGLEGIEARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRT-YHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPEL 80


                  ....
gi 446457466  100 LNQL 103
Cdd:pfam02311  81 LERI 84
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 232-278 2.67e-07

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: 51.21  E-value: 2.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446457466 232 INQAREQLKQGV----PLAELAVNLGFSDqSHFHKAFKAHTGVTPRQFQLA 278
Cdd:COG2169   86 VARACRLIEAGAedrpSLEDLAARLGLSP-RHLRRLFKAHTGVTPKAYARA 135
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 236-275 3.50e-07

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: 45.99  E-value: 3.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 446457466  236 REQLKQGVPLAELAVNLGFSdQSHFHKAFKAHTGVTPRQF 275
Cdd:pfam00165   2 RENLSTNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQY 40
ftrA PRK09393
transcriptional activator FtrA; Provisional
 196-275 9.61e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 49.19  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 196 SLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQL-KQGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQ 274
Cdd:PRK09393 236 TVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLeSSALSIDQIAERAGFGSEESLRHHFRRRAATSPAA 315


                 .
gi 446457466 275 F 275
Cdd:PRK09393 316 Y 316
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 198-275 3.54e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 47.33  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 198 EELAQRVGLSRYAIIRLFkANVGLTPHAFQINLKINQAREQLK---QGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQ 274
Cdd:PRK09685 218 EWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDRCADDLRpaaDDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGE 296


                 .
gi 446457466 275 F 275
Cdd:PRK09685 297 Y 297
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
195-277 5.53e-06

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 44.71  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:PRK11511  26 LSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESnEPILYLAERYGFESQQTLTRTFKNYFDVPPH 105


                 ....
gi 446457466 274 QFQL 277
Cdd:PRK11511 106 KYRM 109
PRK10371 PRK10371
transcriptional regulator MelR;
195-281 5.90e-06

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 46.74  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQ-GVPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:PRK10371 208 LTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDtDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQ 287


                 ....*...
gi 446457466 274 QFQLAAAQ 281
Cdd:PRK10371 288 QYRKLSQQ 295
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
195-273 8.29e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 46.21  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLKQG-VPLAELAVNLGFSDQSHFHKAFKAHTGVTPR 273
Cdd:PRK13503 188 VNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSdASVTDIAYRCGFGDSNHFSTLFRREFSWSPR 267
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
184-281 5.89e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 43.50  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 184 LIDVISSS-EVFISLEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQArEQLKQGVPL--AELAVNLGFSDQSHF 260
Cdd:PRK13502 181 LITALANSlECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHA-QYLLQHSPLmiSEISMQCGFEDSNYF 259

                         90       100
                 ....*....|....*....|.
gi 446457466 261 HKAFKAHTGVTPRQFQLAAAQ 281
Cdd:PRK13502 260 SVVFTRETGMTPSQWRHLSNQ 280
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
220-279 2.29e-04

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 42.09  E-value: 2.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446457466 220 GLTPHAFQINlKINQAREQLKQGVP--LAELAVNLGFSdQSHFHKAFKAHTGVTPRQFQLAA 279
Cdd:PRK15435  76 KANPQQHRLD-KITHACRLLEQETPvtLEALADQVAMS-PFHLHRLFKATTGMTPKAWQQAW 135
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
197-276 2.79e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 41.81  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457466 197 LEELAQRVGLSRYAIIRLFKANVGLTPHAFQINLKINQAREQLK-QGVPLAELAVNLGFSDQSHFHKAFKAHTGVTPRQF 275
Cdd:PRK13501 195 MADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRgSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDY 274


                 .
gi 446457466 276 Q 276
Cdd:PRK13501 275 R 275
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 195-226 7.64e-04

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: 36.36  E-value: 7.64e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446457466  195 ISLEELAQRVGLSRYAIIRLFKANVGLTPHAF 226
Cdd:pfam00165   9 LTIADIADELGFSRSYFSRLFKKYTGVTPSQY 40
 
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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