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Conserved domains on  [gi|1750994941|gb|QET56401|]
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AraC family transcriptional regulator [Citrobacter portucalensis]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 12093096)

AraC family transcriptional regulator controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence; contains an N-terminal PAS domain which functions as a signal sensor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
184-266 3.14e-23

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 90.30  E-value: 3.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  184 PIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTPITDIALQCGYTDHSAFSRQFKAMTGSTP 262
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRdTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1750994941  263 RDFR 266
Cdd:smart00342  81 SEYR 84
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 49-162 2.50e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 67.44  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  49 LNAIPnVVFFIKDVQARYLMVNmTLARRCGFKTVVSLLGKTSADVFPSALGLGYTEQDMRVLREGVTLRDQLEMHLyNGR 128
Cdd:pfam08448   1 LDSLP-DALAVLDPDGRVRYAN-AAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLL-NGE 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1750994941 129 ERgWCLTQKLALRDAQGQVIGMAGISHDLQEAQA 162
Cdd:pfam08448  78 ER-HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
184-266 3.14e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 90.30  E-value: 3.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  184 PIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTPITDIALQCGYTDHSAFSRQFKAMTGSTP 262
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRdTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1750994941  263 RDFR 266
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
156-266 1.62e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 93.31  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 156 DLQEAQARHPAWQRLAIVDDHIRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTP 234
Cdd:COG2207   140 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAeTDLS 219

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1750994941 235 ITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:COG2207   220 ISEIAYELGFSSQSHFSRAFKKRFGVTPSEYR 251
HTH_18 pfam12833
Helix-turn-helix domain;
190-266 6.29e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 86.87  E-value: 6.29e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750994941 190 LTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA--GDTPITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 49-162 2.50e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 67.44  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  49 LNAIPnVVFFIKDVQARYLMVNmTLARRCGFKTVVSLLGKTSADVFPSALGLGYTEQDMRVLREGVTLRDQLEMHLyNGR 128
Cdd:pfam08448   1 LDSLP-DALAVLDPDGRVRYAN-AAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLL-NGE 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1750994941 129 ERgWCLTQKLALRDAQGQVIGMAGISHDLQEAQA 162
Cdd:pfam08448  78 ER-HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 165-271 1.91e-11

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 62.85  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 165 PAWQRLAIVDDHIRNHYHRPiAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKA-TELLAGDTPITDIALQCG 243
Cdd:PRK10296  170 PQWLKATVEKMHDKEQFSES-ALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAkKQLEMTNYSVTDIAFEAG 248

                          90       100
                  ....*....|....*....|....*...
gi 1750994941 244 YTDHSAFSRQFKAMTGSTPRDFRITLAG 271
Cdd:PRK10296  249 YSSPSLFIKTFKKLTSFTPGSYRKKLTE 276
PAS COG2202
PAS domain [Signal transduction mechanisms];
36-194 1.85e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.79  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  36 QTLLHAMALIAPLLNAIPNVVFfIKDVQARYLMVNMTLARRCGFkTVVSLLGKTSADVFPSALGLGYTEQDMRVLREGVT 115
Cdd:COG2202     4 EALEESERRLRALVESSPDAII-ITDLDGRILYVNPAFERLTGY-SAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 116 LRDQLEMHLYNGRERgWCLTQKLALRDAQGQVIGMAGISHD----------LQEAQAR-----HPAWQRLAIVDDHIRNH 180
Cdd:COG2202    82 WRGELRNRRKDGSLF-WVELSISPVRDEDGEITGFVGIARDiterkraeeaLRESEERlrllvENAPDGIFVLDLDGRIL 160

                         170
                  ....*....|....
gi 1750994941 181 YHRPiAMEELTALS 194
Cdd:COG2202   161 YVNP-AAEELLGYS 173
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
184-266 3.14e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 90.30  E-value: 3.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  184 PIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTPITDIALQCGYTDHSAFSRQFKAMTGSTP 262
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRdTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1750994941  263 RDFR 266
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
156-266 1.62e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 93.31  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 156 DLQEAQARHPAWQRLAIVDDHIRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTP 234
Cdd:COG2207   140 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAeTDLS 219

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1750994941 235 ITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:COG2207   220 ISEIAYELGFSSQSHFSRAFKKRFGVTPSEYR 251
HTH_18 pfam12833
Helix-turn-helix domain;
190-266 6.29e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 86.87  E-value: 6.29e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1750994941 190 LTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA--GDTPITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 175-266 6.15e-20

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: 87.14  E-value: 6.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 175 DHIRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELL-AGDTPITDIALQCGYTDHSAFSRQ 253
Cdd:COG4977   217 AWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLeTTDLSIEEIAAACGFGSASHFRRA 296

                          90
                  ....*....|...
gi 1750994941 254 FKAMTGSTPRDFR 266
Cdd:COG4977   297 FRRRFGVSPSAYR 309
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 156-266 2.82e-18

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: 83.18  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 156 DLQEAQARHPAWQRLAIvdDHIRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLAGDTPI 235
Cdd:COG2169    74 DLAPGSPPRADLVARAC--RLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSV 151

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1750994941 236 TDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:COG2169   152 TDAAYAAGFGSLSRFYEAFKKLLGMTPSAYR 182
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 49-162 2.50e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 67.44  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  49 LNAIPnVVFFIKDVQARYLMVNmTLARRCGFKTVVSLLGKTSADVFPSALGLGYTEQDMRVLREGVTLRDQLEMHLyNGR 128
Cdd:pfam08448   1 LDSLP-DALAVLDPDGRVRYAN-AAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLL-NGE 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1750994941 129 ERgWCLTQKLALRDAQGQVIGMAGISHDLQEAQA 162
Cdd:pfam08448  78 ER-HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 165-271 1.91e-11

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 62.85  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 165 PAWQRLAIVDDHIRNHYHRPiAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKA-TELLAGDTPITDIALQCG 243
Cdd:PRK10296  170 PQWLKATVEKMHDKEQFSES-ALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAkKQLEMTNYSVTDIAFEAG 248

                          90       100
                  ....*....|....*....|....*...
gi 1750994941 244 YTDHSAFSRQFKAMTGSTPRDFRITLAG 271
Cdd:PRK10296  249 YSSPSLFIKTFKKLTSFTPGSYRKKLTE 276
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
179-267 4.96e-11

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 61.62  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 179 NHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTPITDIALQCGYTDHSAFSRQFKAM 257
Cdd:PRK13503  182 DHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRhSDASVTDIAYRCGFGDSNHFSTLFRRE 261

                          90
                  ....*....|
gi 1750994941 258 TGSTPRDFRI 267
Cdd:PRK13503  262 FSWSPRDIRQ 271
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
177-269 4.35e-10

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 55.70  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 177 IRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELL-AGDTPITDIALQCGYTDHSAFSRQFK 255
Cdd:PRK10219   14 IDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELrTTERPIFDIAMDLGYVSQQTFSRVFR 93

                          90
                  ....*....|....
gi 1750994941 256 AMTGSTPRDFRITL 269
Cdd:PRK10219   94 RQFDRTPSDYRHRL 107
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 155-266 7.21e-09

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 55.42  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 155 HDLQEAQARHPA--WQRLAIVDDHIRNHYHRPiamEELTALSGMSVaqieRYCKRIFH---LTPRQMIHKVRLEKATELL 229
Cdd:PRK09685  186 HQRESVQPRRERqfQKVVALIDQSIQEEILRP---EWIAGELGISV----RSLYRLFAeqgLVVAQYIRNRRLDRCADDL 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1750994941 230 ---AGDTPITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:PRK09685  259 rpaADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298
ftrA PRK09393
transcriptional activator FtrA; Provisional
 162-266 9.95e-09

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 54.97  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 162 ARHPAwQRLAIVDDHIRNHYHRPIAMEELTALSGMSvaqiERYCKRIFH----LTPRQMIHKVRLEKATELL-AGDTPIT 236
Cdd:PRK09393  213 ASRES-DRLGPLIDWMRAHLAEPHTVASLAARAAMS----PRTFLRRFEaatgMTPAEWLLRERLARARDLLeSSALSID 287

                          90       100       110
                  ....*....|....*....|....*....|
gi 1750994941 237 DIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:PRK09393  288 QIAERAGFGSEESLRHHFRRRAATSPAAYR 317
PAS COG2202
PAS domain [Signal transduction mechanisms];
36-194 1.85e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.79  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941  36 QTLLHAMALIAPLLNAIPNVVFfIKDVQARYLMVNMTLARRCGFkTVVSLLGKTSADVFPSALGLGYTEQDMRVLREGVT 115
Cdd:COG2202     4 EALEESERRLRALVESSPDAII-ITDLDGRILYVNPAFERLTGY-SAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 116 LRDQLEMHLYNGRERgWCLTQKLALRDAQGQVIGMAGISHD----------LQEAQAR-----HPAWQRLAIVDDHIRNH 180
Cdd:COG2202    82 WRGELRNRRKDGSLF-WVELSISPVRDEDGEITGFVGIARDiterkraeeaLRESEERlrllvENAPDGIFVLDLDGRIL 160

                         170
                  ....*....|....
gi 1750994941 181 YHRPiAMEELTALS 194
Cdd:COG2202   161 YVNP-AAEELLGYS 173
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
202-266 2.69e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 47.59  E-value: 2.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 202 ERYCKRIFH----LTPRQMIHKVRLEKATELLAG-DTPITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:PRK13501  206 ERSLKQLFRqqtgMSISHYLRQIRLCHAKCLLRGsEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYR 275
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
184-266 3.01e-05

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 44.78  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 184 PIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLAGDTPITDIALQCGYTDHSAFSRQFKAMTGSTPR 263
Cdd:PRK15435   99 PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILNAGFPDSSSYYRKADETLGMTAK 178


                  ...
gi 1750994941 264 DFR 266
Cdd:PRK15435  179 QFR 181
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
175-268 5.63e-05

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 42.01  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 175 DHIRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRL-EKATELLAGDTPITDIALQCGYTDHSAFSRQ 253
Cdd:PRK11511   16 DWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMtEIAQKLKESNEPILYLAERYGFESQQTLTRT 95

                          90
                  ....*....|....*
gi 1750994941 254 FKAMTGSTPRDFRIT 268
Cdd:PRK11511   96 FKNYFDVPPHKYRMT 110
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
234-266 7.55e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 43.42  E-value: 7.55e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750994941 234 PITDIALQCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:PRK10572  250 PIATIGRNVGYDDQLYFSRVFKKCTGASPSEFR 282
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 227-266 9.86e-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: 9.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1750994941 227 ELLAGDTPITDIALQCGYtDHSAFSRQFKAMTGSTPRDFR 266
Cdd:pfam00165   3 ENLSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
165-266 6.98e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 40.42  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750994941 165 PAWQRLAIVDDHIR---NHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIHKVRLEKATELLA-GDTPITDIAL 240
Cdd:PRK13502  170 PATSRETLLDKLITalaNSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQhSPLMISEISM 249

                          90       100
                  ....*....|....*....|....*.
gi 1750994941 241 QCGYTDHSAFSRQFKAMTGSTPRDFR 266
Cdd:PRK13502  250 QCGFEDSNYFSVVFTRETGMTPSQWR 275
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 177-218 7.92e-03

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: 33.67  E-value: 7.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1750994941 177 IRNHYHRPIAMEELTALSGMSVAQIERYCKRIFHLTPRQMIH 218
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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