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Conserved domains on  [gi|501083655|ref|WP_012134174|]
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MULTISPECIES: MDR efflux pump AcrAB transcriptional activator RobA [Citrobacter]

Protein Classification

MDR efflux pump AcrAB transcriptional activator RobA( domain architecture ID 11487664)

MDR efflux pump AcrAB transcriptional activator RobA confers antimicrobial resistance through upregulation of acrAB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
1-289 0e+00

MDR efflux pump AcrAB transcriptional activator RobA;


:

Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 649.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   1 MDQAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  81 RFDSQQTFTRAFKKQFSQTPALYRRSPEWSAFGIRPPMRLGEFAMPEHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 161 VQFWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEHANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121 161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 501083655 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTGGRPINLRCEFLIPVRR 289
Cdd:PRK15121 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCEYLIPIRR 289
 
Name Accession Description Interval E-value
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
1-289 0e+00

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 649.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   1 MDQAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  81 RFDSQQTFTRAFKKQFSQTPALYRRSPEWSAFGIRPPMRLGEFAMPEHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 161 VQFWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEHANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121 161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 501083655 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTGGRPINLRCEFLIPVRR 289
Cdd:PRK15121 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCEYLIPIRR 289
RobA_TF NF012228
MDR efflux pump AcrAB transcriptional activator RobA; The original characterization of RobA as ...
 3-288 0e+00

MDR efflux pump AcrAB transcriptional activator RobA; The original characterization of RobA as a Right side Origin of replication Binding protein A (robA) may be misleading. Characterizations in large numbers of papers since then treat RobA as a transcriptional activator of the AcrAB antibiotic efflux pump.


Pssm-ID: 467958 [Multi-domain]  Cd Length: 286  Bit Score: 618.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   3 QAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRF 82
Cdd:NF012228   1 QAGIIRDLLVWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGQAIGAYIRARRLSKAAVALRLTSRPILDIALQYRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  83 DSQQTFTRAFKKQFSQTPALYRRSPEWSAFGIRPPMRLGEFAMPEHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMRVQ 162
Cdd:NF012228  81 DSQQTFTRAFKKQFNQTPALYRRSEDWNAFGICPPIRLGKFTLPEPEFVTLPEQHLVGITQSYSCTLEQISDFRTEMRVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 163 FWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEHANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFILT 242
Cdd:NF012228 161 FWRQYLGNTPTIPPVLYGLHHSRPSKEKDDEQEVLYTTALEPEHAPEGVQEGQPVVLEGGEYVQFTYEGPPEGLQDFILT 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 501083655 243 VYGTCMPMLNLTRRKGQDIERYYPAEDAKTGGRPINLRCEFLIPVR 288
Cdd:NF012228 241 VYGTCMPTLNLTRRKGQDIERFYPHGDKKRDEPPTHIRCEYLIPIR 286
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
21-104 5.57e-29

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 105.71  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655    21 PLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFTRAFKKQFSQTP 100
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 501083655   101 ALYR 104
Cdd:smart00342  81 SEYR 84
YdeE COG3708
Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription] ...
 126-288 3.56e-26

Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription];


Pssm-ID: 442922  Cd Length: 157  Bit Score: 100.87  E-value: 3.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 126 PEHQFVTLEDTQLLGTTQSYSCSLEQisdfRHEMRVQFWQDFLSQAP-TIPPL-----LYGLNETrpslEKDDEQEVFYT 199
Cdd:COG3708    1 MEYRIVEKPAFKLVGLSARTSNSDEE----ANEEIPALWQRFLPEGLaEIPNLsnpggLYGVCTD----YESDEGEFDYL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 200 TALPQEHANGYVPSAQPVTLQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTggrpiN 278
Cdd:COG3708   73 AGVEVSSFDEVPEGLETLEIPAGTYAVFTHKGpMPEALQETWQYIYSEWLPSSGYERADGPDFEVYDERDDPSP-----D 147

                        170
                 ....*....|
gi 501083655 279 LRCEFLIPVR 288
Cdd:COG3708  148 SEVEIWIPIK 157
GyrI-like pfam06445
GyrI-like small molecule binding domain; This family contains the small molecule binding ...
 127-287 7.16e-23

GyrI-like small molecule binding domain; This family contains the small molecule binding domain of a number of different bacterial transcription activators. This family also contains DNA gyrase inhibitors. The GyrI superfamily contains a diad of the SHS2 module, adapted for small-molecule binding. The GyrI superfamily includes a family of secreted forms that is found only in animals and the bacterial pathogen Leptospira.


Pssm-ID: 428947  Cd Length: 153  Bit Score: 92.09  E-value: 7.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  127 EHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMRVQFWQDFLSQAPTIpplLYGLNETRPslEKDDEQEVFYTTALPQEH 206
Cdd:pfam06445   1 EVEIVELPAFRVAGLRHRGPYNEEGIGALWEELCAWASENGLSPAPSP---LIGVSYDDP--EVTEDEELRYDAGVAVPI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  207 ANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKtggRPINLRCEFLIP 286
Cdd:pfam06445  76 PVEGPEGVEELELPGGEYAVFRHKGPYDDLQETYAKIYGEWLPESGYERRDGPSFEIYLNDPREV---PEEELKTEIYIP 152


                  .
gi 501083655  287 V 287
Cdd:pfam06445 153 V 153
 
Name Accession Description Interval E-value
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
1-289 0e+00

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 649.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   1 MDQAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  81 RFDSQQTFTRAFKKQFSQTPALYRRSPEWSAFGIRPPMRLGEFAMPEHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 161 VQFWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEHANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121 161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 501083655 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTGGRPINLRCEFLIPVRR 289
Cdd:PRK15121 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCEYLIPIRR 289
RobA_TF NF012228
MDR efflux pump AcrAB transcriptional activator RobA; The original characterization of RobA as ...
 3-288 0e+00

MDR efflux pump AcrAB transcriptional activator RobA; The original characterization of RobA as a Right side Origin of replication Binding protein A (robA) may be misleading. Characterizations in large numbers of papers since then treat RobA as a transcriptional activator of the AcrAB antibiotic efflux pump.


Pssm-ID: 467958 [Multi-domain]  Cd Length: 286  Bit Score: 618.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   3 QAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRF 82
Cdd:NF012228   1 QAGIIRDLLVWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGQAIGAYIRARRLSKAAVALRLTSRPILDIALQYRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  83 DSQQTFTRAFKKQFSQTPALYRRSPEWSAFGIRPPMRLGEFAMPEHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMRVQ 162
Cdd:NF012228  81 DSQQTFTRAFKKQFNQTPALYRRSEDWNAFGICPPIRLGKFTLPEPEFVTLPEQHLVGITQSYSCTLEQISDFRTEMRVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 163 FWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEHANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFILT 242
Cdd:NF012228 161 FWRQYLGNTPTIPPVLYGLHHSRPSKEKDDEQEVLYTTALEPEHAPEGVQEGQPVVLEGGEYVQFTYEGPPEGLQDFILT 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 501083655 243 VYGTCMPMLNLTRRKGQDIERYYPAEDAKTGGRPINLRCEFLIPVR 288
Cdd:NF012228 241 VYGTCMPTLNLTRRKGQDIERFYPHGDKKRDEPPTHIRCEYLIPIR 286
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
1-106 1.76e-45

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 149.30  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   1 MDQAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK10219   1 MSHQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDL 80

                         90       100
                 ....*....|....*....|....*.
gi 501083655  81 RFDSQQTFTRAFKKQFSQTPALYRRS 106
Cdd:PRK10219  81 GYVSQQTFSRVFRRQFDRTPSDYRHR 106
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
7-104 1.96e-33

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 118.67  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   7 IRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK11511  11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                         90
                 ....*....|....*...
gi 501083655  87 TFTRAFKKQFSQTPALYR 104
Cdd:PRK11511  91 TLTRTFKNYFDVPPHKYR 108
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
21-104 5.57e-29

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 105.71  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655    21 PLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFTRAFKKQFSQTP 100
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 501083655   101 ALYR 104
Cdd:smart00342  81 SEYR 84
YdeE COG3708
Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription] ...
 126-288 3.56e-26

Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription];


Pssm-ID: 442922  Cd Length: 157  Bit Score: 100.87  E-value: 3.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 126 PEHQFVTLEDTQLLGTTQSYSCSLEQisdfRHEMRVQFWQDFLSQAP-TIPPL-----LYGLNETrpslEKDDEQEVFYT 199
Cdd:COG3708    1 MEYRIVEKPAFKLVGLSARTSNSDEE----ANEEIPALWQRFLPEGLaEIPNLsnpggLYGVCTD----YESDEGEFDYL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655 200 TALPQEHANGYVPSAQPVTLQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTggrpiN 278
Cdd:COG3708   73 AGVEVSSFDEVPEGLETLEIPAGTYAVFTHKGpMPEALQETWQYIYSEWLPSSGYERADGPDFEVYDERDDPSP-----D 147

                        170
                 ....*....|
gi 501083655 279 LRCEFLIPVR 288
Cdd:COG3708  148 SEVEIWIPIK 157
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 7-105 2.82e-23

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: 96.77  E-value: 2.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   7 IRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:COG4977  212 LARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSAS 291

                         90
                 ....*....|....*....
gi 501083655  87 TFTRAFKKQFSQTPALYRR 105
Cdd:COG4977  292 HFRRAFRRRFGVSPSAYRR 310
GyrI-like pfam06445
GyrI-like small molecule binding domain; This family contains the small molecule binding ...
 127-287 7.16e-23

GyrI-like small molecule binding domain; This family contains the small molecule binding domain of a number of different bacterial transcription activators. This family also contains DNA gyrase inhibitors. The GyrI superfamily contains a diad of the SHS2 module, adapted for small-molecule binding. The GyrI superfamily includes a family of secreted forms that is found only in animals and the bacterial pathogen Leptospira.


Pssm-ID: 428947  Cd Length: 153  Bit Score: 92.09  E-value: 7.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  127 EHQFVTLEDTQLLGTTQSYSCSLEQISDFRHEMRVQFWQDFLSQAPTIpplLYGLNETRPslEKDDEQEVFYTTALPQEH 206
Cdd:pfam06445   1 EVEIVELPAFRVAGLRHRGPYNEEGIGALWEELCAWASENGLSPAPSP---LIGVSYDDP--EVTEDEELRYDAGVAVPI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  207 ANGYVPSAQPVTLQGGEYVMFTYEGLGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKtggRPINLRCEFLIP 286
Cdd:pfam06445  76 PVEGPEGVEELELPGGEYAVFRHKGPYDDLQETYAKIYGEWLPESGYERRDGPSFEIYLNDPREV---PEEELKTEIYIP 152


                  .
gi 501083655  287 V 287
Cdd:pfam06445 153 V 153
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
8-106 8.28e-23

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 94.46  E-value: 8.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   8 RDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQT 87
Cdd:COG2207  155 LLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSH 234

                         90
                 ....*....|....*....
gi 501083655  88 FTRAFKKQFSQTPALYRRS 106
Cdd:COG2207  235 FSRAFKKRFGVTPSEYRKR 253
HTH_18 pfam12833
Helix-turn-helix domain;
27-106 6.10e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.17  E-value: 6.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   27 VAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVAL-RLTARPILDIALQYRFDSQQTFTRAFKKQFSQTPALYRR 105
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 501083655  106 S 106
Cdd:pfam12833  81 R 81
AraC_E_bind smart00871
Bacterial transcription activator, effector binding domain; This domain is found in the ...
 127-288 2.92e-18

Bacterial transcription activator, effector binding domain; This domain is found in the probable effector binding domain of a number of different bacterial transcription activators.and is also present in some DNA gyrase inhibitors. The absence of a HTH motif in the DNA gyrase inhibitors is thought to indicate the fact that these do not bind DNA.


Pssm-ID: 214874 [Multi-domain]  Cd Length: 158  Bit Score: 79.83  E-value: 2.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   127 EHQFVTLEDTQLLGTTQSYSCSLEQISDFrhEMRVQFWQDFLSQAPTIPP-LLYGLNETRPSLEKDDEQEVFYTTALPQE 205
Cdd:smart00871   1 EVRIVELPAFKVAGLRHRGPNEDEKIPEL--WQRLIQWAKELGLLPVGNSgEPYGVYYDDPDDTPDGEFRYDAGVEVSDE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   206 HANGYVPsaQPVTLQGGEYVMFTYEGL-GTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKTGgrPINLRCEFL 284
Cdd:smart00871  79 VEAPEGV--ETKTIPAGKYAVFTHKGGsYDEIQEAWEAIYGEWLPNSGYELRDAGPDFEVYLNDPPDTD--PEELVTEIY 154


                   ....
gi 501083655   285 IPVR 288
Cdd:smart00871 155 IPVK 158
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 3-105 7.41e-16

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: 76.63  E-value: 7.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   3 QAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRlTARPILDIALQYRF 82
Cdd:COG2169   82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAGF 160

                         90       100
                 ....*....|....*....|...
gi 501083655  83 DSQQTFTRAFKKQFSQTPALYRR 105
Cdd:COG2169  161 GSLSRFYEAFKKLLGMTPSAYRR 183
ftrA PRK09393
transcriptional activator FtrA; Provisional
 10-106 2.75e-14

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 71.92  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  10 LLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFT 89
Cdd:PRK09393 223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLR 302

                         90
                 ....*....|....*..
gi 501083655  90 RAFKKQFSQTPALYRRS 106
Cdd:PRK09393 303 HHFRRRAATSPAAYRKR 319
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 17-106 3.37e-13

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 68.52  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  17 HLDQP-LSLDNVAAKAGYSKWHLQRMFKDvTGHAIGAYIRARRLSKSAVALR--LTARPILDIALQYRFDSQQTFTRAFK 93
Cdd:PRK09685 209 SIQEEiLRPEWIAGELGISVRSLYRLFAE-QGLVVAQYIRNRRLDRCADDLRpaADDEKITSIAYKWGFSDSSHFSTAFK 287

                         90
                 ....*....|...
gi 501083655  94 KQFSQTPALYRRS 106
Cdd:PRK09685 288 QRFGVSPGEYRRK 300
PRK10371 PRK10371
transcriptional regulator MelR;
7-107 1.09e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 58.29  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   7 IRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK10371 193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272

                         90       100
                 ....*....|....*....|.
gi 501083655  87 TFTRAFKKQFSQTPALYRRSP 107
Cdd:PRK10371 273 RFYSTFGKYVGMSPQQYRKLS 293
Cass2 pfam14526
Integron-associated effector binding protein; This family contains Cass2 from Vibrio cholerae, ...
 131-287 1.16e-07

Integron-associated effector binding protein; This family contains Cass2 from Vibrio cholerae, an integron-associated protein that has been shown to bind cationic drug compounds with submicromolar affinity. Cass2 has been proposed to be representative of a larger family of independent effector-binding proteins associated with lateral gene transfer within Vibrio and other closely-related species.


Pssm-ID: 434016 [Multi-domain]  Cd Length: 149  Bit Score: 50.05  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  131 VTLEDTQLLG----TTQSYSCSLEQISDFRHEmrvqFWQDFLSQAPTIPPLLYGLNETRPSLEKDDEQEVFYTTALPQEH 206
Cdd:pfam14526   3 VELPSFTVAGiryeGPNEYEDHNKEIGKFWEE----FNEDGRLPNIKKDDKSYGIYVDYEDEENEFDYYAGVEVPSFSEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  207 ANGYVPsaqpVTLQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAktggrpiNLRCEFLI 285
Cdd:pfam14526  79 PEGLVV----IEIPGGKYAVFTIEGdFPDAIAEAWTRIYGWLLPNSGYERAGGPDFEVYKENGDE-------NMKIELYI 147


                  ..
gi 501083655  286 PV 287
Cdd:pfam14526 148 PV 149
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
2-100 2.38e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 50.83  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   2 DQAGIIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYR 81
Cdd:PRK13503 168 NSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCG 247

                         90
                 ....*....|....*....
gi 501083655  82 FDSQQTFTRAFKKQFSQTP 100
Cdd:PRK13503 248 FGDSNHFSTLFRREFSWSP 266
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
7-108 6.14e-07

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 49.59  E-value: 6.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   7 IRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK10572 185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264

                         90       100
                 ....*....|....*....|..
gi 501083655  87 TFTRAFKKQFSQTPALYRRSPE 108
Cdd:PRK10572 265 YFSRVFKKCTGASPSEFRARCE 286
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
10-105 1.45e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 48.75  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  10 LLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFT 89
Cdd:PRK13501 181 IMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFS 260

                         90
                 ....*....|....*.
gi 501083655  90 RAFKKQFSQTPALYRR 105
Cdd:PRK13501 261 AVFTREAGMTPRDYRQ 276
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
6-104 4.85e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 47.02  E-value: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   6 IIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQ 85
Cdd:PRK13500 207 LLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDS 286

                         90
                 ....*....|....*....
gi 501083655  86 QTFTRAFKKQFSQTPALYR 104
Cdd:PRK13500 287 NYFSVVFTRETGMTPSQWR 305
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
6-104 1.28e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 45.82  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655   6 IIRDLLTWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQ 85
Cdd:PRK13502 177 LLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDS 256

                         90
                 ....*....|....*....
gi 501083655  86 QTFTRAFKKQFSQTPALYR 104
Cdd:PRK13502 257 NYFSVVFTRETGMTPSQWR 275
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
19-108 3.90e-05

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 44.40  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501083655  19 DQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRlTARPILDIALQYRFDSQQTFTRAFKKQFSQ 98
Cdd:PRK15435  97 ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALA-KGESVTTSILNAGFPDSSSYYRKADETLGM 175

                         90
                 ....*....|
gi 501083655  99 TPALYRRSPE 108
Cdd:PRK15435 176 TAKQFRHGGE 185
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 73-105 4.02e-05

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: 40.21  E-value: 4.02e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 501083655   73 ILDIALQYRFdSQQTFTRAFKKQFSQTPALYRR 105
Cdd:pfam00165  11 IADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 14-55 3.65e-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: 37.52  E-value: 3.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 501083655   14 LEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIR 55
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
 
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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