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Conserved domains on  [gi|1314862259|gb|AUG19073|]
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right origin-binding protein [Escherichia coli str. K-12 substr. MG1655]

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: 649.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121    1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPLRLGEFTMPEHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121   81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 161 YQFWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTALAQDQADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121  161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862259 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCELLIPIRR 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: 649.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121    1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPLRLGEFTMPEHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121   81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 161 YQFWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTALAQDQADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121  161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862259 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCELLIPIRR 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: 621.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   3 QAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRF 82
Cdd:NF012228    1 QAGIIRDLLVWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGQAIGAYIRARRLSKAAVALRLTSRPILDIALQYRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  83 DSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPLRLGEFTMPEHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMRYQ 162
Cdd:NF012228   81 DSQQTFTRAFKKQFNQTPALYRRSEDWNAFGICPPIRLGKFTLPEPEFVTLPEQHLVGITQSYSCTLEQISDFRTEMRVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 163 FWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTALAQDQADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFILT 242
Cdd:NF012228  161 FWRQYLGNTPTIPPVLYGLHHSRPSKEKDDEQEVLYTTALEPEHAPEGVQEGQPVVLEGGEYVQFTYEGPPEGLQDFILT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1314862259 243 VYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCELLIPIR 288
Cdd:NF012228  241 VYGTCMPTLNLTRRKGQDIERFYPHGDKKRDEPPTHIRCEYLIPIR 286
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
21-104 3.31e-29

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 106.48  E-value: 3.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   21 PLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFTRAFKKQFAQTP 100
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 1314862259  101 ALYR 104
Cdd:smart00342  81 SEYR 84
YdeE COG3708
Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription] ...
126-288 9.44e-27

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


Pssm-ID: 442922  Cd Length: 157  Bit Score: 102.41  E-value: 9.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 126 PEHKFVTLEDTPLIGVTQSYSCSLEQisdfRHEMRYQFWHDFLGNAP-TIP-----PVLYGLNetrpSQDKDDEQEVFYT 199
Cdd:COG3708     1 MEYRIVEKPAFKLVGLSARTSNSDEE----ANEEIPALWQRFLPEGLaEIPnlsnpGGLYGVC----TDYESDEGEFDYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 200 TALAQDQADGYVLTGHPVMLQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAgdrpiN 278
Cdd:COG3708    73 AGVEVSSFDEVPEGLETLEIPAGTYAVFTHKGpMPEALQETWQYIYSEWLPSSGYERADGPDFEVYDERDDPSP-----D 147
                         170
                  ....*....|
gi 1314862259 279 LRCELLIPIR 288
Cdd:COG3708   148 SEVEIWIPIK 157
GyrI-like pfam06445
GyrI-like small molecule binding domain; This family contains the small molecule binding ...
127-287 6.19e-26

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: 100.18  E-value: 6.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 127 EHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMRYQFWHDFLGNAPtipPVLYGLNETRPsqDKDDEQEVFYTTALAQDQ 206
Cdd:pfam06445   1 EVEIVELPAFRVAGLRHRGPYNEEGIGALWEELCAWASENGLSPAP---SPLIGVSYDDP--EVTEDEELRYDAGVAVPI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 207 ADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAkagDRPINLRCELLIP 286
Cdd:pfam06445  76 PVEGPEGVEELELPGGEYAVFRHKGPYDDLQETYAKIYGEWLPESGYERRDGPSFEIYLNDPRE---VPEEELKTEIYIP 152

                  .
gi 1314862259 287 I 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: 649.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK15121    1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPLRLGEFTMPEHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMR 160
Cdd:PRK15121   81 RFDSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPIRLGEFTLPEHEFVTLPETPLVGVTQSYSCSLEQISDFRHEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 161 YQFWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTALAQDQADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFI 240
Cdd:PRK15121  161 VQFWRDFLGNAPTIPPVLYGLHETRPSQEKDDEQEVFYTTALEPDQADGYVQTGHPVMLQGGEYVMFTYEGLGTGLQEFI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1314862259 241 LTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCELLIPIRR 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: 621.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   3 QAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRF 82
Cdd:NF012228    1 QAGIIRDLLVWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGQAIGAYIRARRLSKAAVALRLTSRPILDIALQYRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  83 DSQQTFTRAFKKQFAQTPALYRRSPEWSAFGIRPPLRLGEFTMPEHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMRYQ 162
Cdd:NF012228   81 DSQQTFTRAFKKQFNQTPALYRRSEDWNAFGICPPIRLGKFTLPEPEFVTLPEQHLVGITQSYSCTLEQISDFRTEMRVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 163 FWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTALAQDQADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFILT 242
Cdd:NF012228  161 FWRQYLGNTPTIPPVLYGLHHSRPSKEKDDEQEVLYTTALEPEHAPEGVQEGQPVVLEGGEYVQFTYEGPPEGLQDFILT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1314862259 243 VYGTCMPMLNLTRRKGQDIERYYPAEDAKAGDRPINLRCELLIPIR 288
Cdd:NF012228  241 VYGTCMPTLNLTRRKGQDIERFYPHGDKKRDEPPTHIRCEYLIPIR 286
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
1-106 5.79e-45

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 147.76  E-value: 5.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   1 MDQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQY 80
Cdd:PRK10219    1 MSHQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDL 80
                          90       100
                  ....*....|....*....|....*.
gi 1314862259  81 RFDSQQTFTRAFKKQFAQTPALYRRS 106
Cdd:PRK10219   81 GYVSQQTFSRVFRRQFDRTPSDYRHR 106
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
7-104 3.84e-33

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 117.90  E-value: 3.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK11511   11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90
                          90
                  ....*....|....*...
gi 1314862259  87 TFTRAFKKQFAQTPALYR 104
Cdd:PRK11511   91 TLTRTFKNYFDVPPHKYR 108
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
21-104 3.31e-29

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 106.48  E-value: 3.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   21 PLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFTRAFKKQFAQTP 100
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 1314862259  101 ALYR 104
Cdd:smart00342  81 SEYR 84
YdeE COG3708
Predicted transcriptional regulator YdeE, contains AraC-type DNA-binding domain [Transcription] ...
126-288 9.44e-27

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


Pssm-ID: 442922  Cd Length: 157  Bit Score: 102.41  E-value: 9.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 126 PEHKFVTLEDTPLIGVTQSYSCSLEQisdfRHEMRYQFWHDFLGNAP-TIP-----PVLYGLNetrpSQDKDDEQEVFYT 199
Cdd:COG3708     1 MEYRIVEKPAFKLVGLSARTSNSDEE----ANEEIPALWQRFLPEGLaEIPnlsnpGGLYGVC----TDYESDEGEFDYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 200 TALAQDQADGYVLTGHPVMLQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAKAgdrpiN 278
Cdd:COG3708    73 AGVEVSSFDEVPEGLETLEIPAGTYAVFTHKGpMPEALQETWQYIYSEWLPSSGYERADGPDFEVYDERDDPSP-----D 147
                         170
                  ....*....|
gi 1314862259 279 LRCELLIPIR 288
Cdd:COG3708   148 SEVEIWIPIK 157
GyrI-like pfam06445
GyrI-like small molecule binding domain; This family contains the small molecule binding ...
127-287 6.19e-26

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: 100.18  E-value: 6.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 127 EHKFVTLEDTPLIGVTQSYSCSLEQISDFRHEMRYQFWHDFLGNAPtipPVLYGLNETRPsqDKDDEQEVFYTTALAQDQ 206
Cdd:pfam06445   1 EVEIVELPAFRVAGLRHRGPYNEEGIGALWEELCAWASENGLSPAP---SPLIGVSYDDP--EVTEDEELRYDAGVAVPI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 207 ADGYVLTGHPVMLQGGEYVMFTYEGLGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAkagDRPINLRCELLIP 286
Cdd:pfam06445  76 PVEGPEGVEELELPGGEYAVFRHKGPYDDLQETYAKIYGEWLPESGYERRDGPSFEIYLNDPRE---VPEEELKTEIYIP 152

                  .
gi 1314862259 287 I 287
Cdd:pfam06445 153 V 153
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
7-105 7.09e-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: 95.61  E-value: 7.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:COG4977   212 LARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSAS 291
                          90
                  ....*....|....*....
gi 1314862259  87 TFTRAFKKQFAQTPALYRR 105
Cdd:COG4977   292 HFRRAFRRRFGVSPSAYRR 310
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
8-106 8.11e-23

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 94.85  E-value: 8.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   8 RDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQT 87
Cdd:COG2207   155 LLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSH 234
                          90
                  ....*....|....*....
gi 1314862259  88 FTRAFKKQFAQTPALYRRS 106
Cdd:COG2207   235 FSRAFKKRFGVTPSEYRKR 253
AraC_E_bind smart00871
Bacterial transcription activator, effector binding domain; This domain is found in the ...
127-288 4.96e-21

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: 87.15  E-value: 4.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  127 EHKFVTLEDTPLIGVTQSYSCSLEQISDFrhEMRYQFWHDFLGNAPTIPP-VLYGLNETRPSQDKDDEQEVFYTTALAQD 205
Cdd:smart00871   1 EVRIVELPAFKVAGLRHRGPNEDEKIPEL--WQRLIQWAKELGLLPVGNSgEPYGVYYDDPDDTPDGEFRYDAGVEVSDE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  206 QADGYVLtgHPVMLQGGEYVMFTYEGL-GTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDakAGDRPINLRCELL 284
Cdd:smart00871  79 VEAPEGV--ETKTIPAGKYAVFTHKGGsYDEIQEAWEAIYGEWLPNSGYELRDAGPDFEVYLNDP--PDTDPEELVTEIY 154

                   ....
gi 1314862259  285 IPIR 288
Cdd:smart00871 155 IPVK 158
HTH_18 pfam12833
Helix-turn-helix domain;
27-106 1.88e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 80.71  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  27 VAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVAL-RLTARPILDIALQYRFDSQQTFTRAFKKQFAQTPALYRR 105
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80

                  .
gi 1314862259 106 S 106
Cdd:pfam12833  81 R 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
3-105 1.62e-15

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: 75.48  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   3 QAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRlTARPILDIALQYRF 82
Cdd:COG2169    82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAGF 160
                          90       100
                  ....*....|....*....|...
gi 1314862259  83 DSQQTFTRAFKKQFAQTPALYRR 105
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAYRR 183
ftrA PRK09393
transcriptional activator FtrA; Provisional
10-106 1.70e-14

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 72.30  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  10 LLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQTFT 89
Cdd:PRK09393  223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLR 302
                          90
                  ....*....|....*..
gi 1314862259  90 RAFKKQFAQTPALYRRS 106
Cdd:PRK09393  303 HHFRRRAATSPAAYRKR 319
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
17-106 2.11e-13

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 68.90  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  17 HLDQP-LSLDNVAAKAGYSKWHLQRMFKDvTGHAIGAYIRARRLSKSAVALR--LTARPILDIALQYRFDSQQTFTRAFK 93
Cdd:PRK09685  209 SIQEEiLRPEWIAGELGISVRSLYRLFAE-QGLVVAQYIRNRRLDRCADDLRpaADDEKITSIAYKWGFSDSSHFSTAFK 287
                          90
                  ....*....|...
gi 1314862259  94 KQFAQTPALYRRS 106
Cdd:PRK09685  288 QRFGVSPGEYRRK 300
PRK10371 PRK10371
transcriptional regulator MelR;
7-107 3.99e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 56.37  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK10371  193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272
                          90       100
                  ....*....|....*....|.
gi 1314862259  87 TFTRAFKKQFAQTPALYRRSP 107
Cdd:PRK10371  273 RFYSTFGKYVGMSPQQYRKLS 293
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
7-108 1.02e-06

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 49.20  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQ 86
Cdd:PRK10572  185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264
                          90       100
                  ....*....|....*....|..
gi 1314862259  87 TFTRAFKKQFAQTPALYRRSPE 108
Cdd:PRK10572  265 YFSRVFKKCTGASPSEFRARCE 286
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
2-100 1.50e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 48.52  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   2 DQAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYR 81
Cdd:PRK13503  168 NSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCG 247
                          90
                  ....*....|....*....
gi 1314862259  82 FDSQQTFTRAFKKQFAQTP 100
Cdd:PRK13503  248 FGDSNHFSTLFRREFSWSP 266
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
9-105 1.88e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 48.36  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   9 DLLI-WLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQQT 87
Cdd:PRK13501  179 DLIMsALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNY 258
                          90
                  ....*....|....*...
gi 1314862259  88 FTRAFKKQFAQTPALYRR 105
Cdd:PRK13501  259 FSAVFTREAGMTPRDYRQ 276
Cass2 pfam14526
Integron-associated effector binding protein; This family contains Cass2 from Vibrio cholerae, ...
131-287 3.52e-06

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: 45.81  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 131 VTLEDTPLIGV----TQSYSCSLEQISDFRHEmryqFWHDFLGNAPTIPPVLYGLNETRPSQDKDDEQEVFYTTalaqdQ 206
Cdd:pfam14526   3 VELPSFTVAGIryegPNEYEDHNKEIGKFWEE----FNEDGRLPNIKKDDKSYGIYVDYEDEENEFDYYAGVEV-----P 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259 207 ADGYVLTGHPVM-LQGGEYVMFTYEG-LGTGVQEFILTVYGTCMPMLNLTRRKGQDIERYYPAEDAkagdrpiNLRCELL 284
Cdd:pfam14526  74 SFSELPEGLVVIeIPGGKYAVFTIEGdFPDAIAEAWTRIYGWLLPNSGYERAGGPDFEVYKENGDE-------NMKIELY 146

                  ...
gi 1314862259 285 IPI 287
Cdd:pfam14526 147 IPV 149
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
6-104 1.74e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 45.48  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   6 IIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQ 85
Cdd:PRK13500  207 LLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDS 286
                          90
                  ....*....|....*....
gi 1314862259  86 QTFTRAFKKQFAQTPALYR 104
Cdd:PRK13500  287 NYFSVVFTRETGMTPSQWR 305
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
19-108 2.75e-05

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 45.17  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259  19 DQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRlTARPILDIALQYRFDSQQTFTRAFKKQFAQ 98
Cdd:PRK15435   97 ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALA-KGESVTTSILNAGFPDSSSYYRKADETLGM 175
                          90
                  ....*....|
gi 1314862259  99 TPALYRRSPE 108
Cdd:PRK15435  176 TAKQFRHGGE 185
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
6-104 5.33e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 43.89  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314862259   6 IIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKSAVALRLTARPILDIALQYRFDSQ 85
Cdd:PRK13502  177 LLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDS 256
                          90
                  ....*....|....*....
gi 1314862259  86 QTFTRAFKKQFAQTPALYR 104
Cdd:PRK13502  257 NYFSVVFTRETGMTPSQWR 275
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
73-105 9.85e-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: 39.06  E-value: 9.85e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1314862259  73 ILDIALQYRFdSQQTFTRAFKKQFAQTPALYRR 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 2.77e-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: 37.90  E-value: 2.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1314862259  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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