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Conserved domains on  [gi|446196781|ref|WP_000274636|]
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MULTISPECIES: AraC family transcriptional regulator [Enterobacteriaceae]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 13462103)

AraC family transcriptional regulator controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

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;
186-268 1.65e-27

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.86  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781   186 LTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPS 265
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ...
gi 446196781   266 EYR 268
Cdd:smart00342  82 EYR 84
PRK09685 super family cl35885
DNA-binding transcriptional activator FeaR; Provisional
 55-271 3.99e-08

DNA-binding transcriptional activator FeaR; Provisional


The actual alignment was detected with superfamily member PRK09685:

Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 53.50  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781  55 GAGATLVPGDVLYVPAGGWNFPQWQAPATTFSVLFGK----QQLGFSVVQWDGKQYQNLAKQHVARRgprigsFLLQTLN 130
Cdd:PRK09685  88 DRQVQLAAGDITLIDASRPCSIYPQGLSEQISLLLPRelveQYFPGQKPACAGRLSASLPMVQLSHR------LLQQSMN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 131 EMQMQPQEQQTARLIVASLLshcRDLLGSQIQTASRSQALFEAIRDYIDERYAS-ALTRESVAQAFYISPNYLSHLFQKT 209
Cdd:PRK09685 162 GPALSETESEALLEALIALL---RPALHQRESVQPRRERQFQKVVALIDQSIQEeILRPEWIAGELGISVRSLYRLFAEQ 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446196781 210 GAIgFNEYLNHTRLEHAKTLLKGY--DLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09685 239 GLV-VAQYIRNRRLDRCADDLRPAadDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
186-268 1.65e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.86  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781   186 LTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPS 265
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ...
gi 446196781   266 EYR 268
Cdd:smart00342  82 EYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
142-274 1.66e-23

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 96.39  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 142 ARLIVASLLSHCRDLLGSQIQTASRSQALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHT 221
Cdd:COG2207  125 LLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLREL 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446196781 222 RLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG2207  205 RLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
191-270 1.52e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.41  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781  191 VAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGY-DLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 446196781  270 Q 270
Cdd:pfam12833  81 R 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
176-271 7.74e-13

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 67.31  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 176 DYIDERYASALTRESVAQAFYISPNYLSHLF-QKTGaIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCR 254
Cdd:PRK10572 190 QYISDHLASEFDIESVAQHVCLSPSRLAHLFrQQLG-ISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSR 268

                         90
                 ....*....|....*..
gi 446196781 255 LFRKNTERSPSEYRRQY 271
Cdd:PRK10572 269 VFKKCTGASPSEFRARC 285
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 55-271 3.99e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 53.50  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781  55 GAGATLVPGDVLYVPAGGWNFPQWQAPATTFSVLFGK----QQLGFSVVQWDGKQYQNLAKQHVARRgprigsFLLQTLN 130
Cdd:PRK09685  88 DRQVQLAAGDITLIDASRPCSIYPQGLSEQISLLLPRelveQYFPGQKPACAGRLSASLPMVQLSHR------LLQQSMN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 131 EMQMQPQEQQTARLIVASLLshcRDLLGSQIQTASRSQALFEAIRDYIDERYAS-ALTRESVAQAFYISPNYLSHLFQKT 209
Cdd:PRK09685 162 GPALSETESEALLEALIALL---RPALHQRESVQPRRERQFQKVVALIDQSIQEeILRPEWIAGELGISVRSLYRLFAEQ 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446196781 210 GAIgFNEYLNHTRLEHAKTLLKGY--DLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09685 239 GLV-VAQYIRNRRLDRCADDLRPAadDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 45-71 1.51e-03

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 36.72  E-value: 1.51e-03
                         10        20
                 ....*....|....*....|....*....
gi 446196781  45 IVLEGEF--VDTGAGATLVPGDVLYVPAG 71
Cdd:cd02228   38 YVLEGELeiTDDGQTVTAKPGDVLFIPKG 66
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 45-71 3.55e-03

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 36.50  E-value: 3.55e-03
                         10        20
                 ....*....|....*....|....*....
gi 446196781  45 IVLEGEFVDTGAGATLV--PGDVLYVPAG 71
Cdd:COG4766   72 YVLEGTLTIEIDGETVTagPGDVIYIPKG 100
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
186-268 1.65e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.86  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781   186 LTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPS 265
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ...
gi 446196781   266 EYR 268
Cdd:smart00342  82 EYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
142-274 1.66e-23

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 96.39  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 142 ARLIVASLLSHCRDLLGSQIQTASRSQALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHT 221
Cdd:COG2207  125 LLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLREL 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446196781 222 RLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG2207  205 RLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
191-270 1.52e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.41  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781  191 VAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGY-DLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 446196781  270 Q 270
Cdd:pfam12833  81 R 81
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 146-274 2.12e-19

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: 85.98  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 146 VASLLSHCRDLLGSQIQTASRSQAL------FEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQK-TGaIGFNEYL 218
Cdd:COG4977  181 VARRLVVDPRRPGGQAQFSPLLVPLghrdprLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAaTG-TTPARYL 259

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446196781 219 NHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG4977  260 QRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 153-270 3.04e-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: 74.70  E-value: 3.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 153 CRDLLGSQiqtASRSQALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQK-TGaIGFNEYLNHTRLEHAKTLLK 231
Cdd:COG2169   71 CRPDLAPG---SPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAhTG-VTPKAYARARRLLRARQLLQ 146

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446196781 232 GyDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQ 270
Cdd:COG2169  147 T-GLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRG 184
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
176-271 7.74e-13

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 67.31  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 176 DYIDERYASALTRESVAQAFYISPNYLSHLF-QKTGaIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCR 254
Cdd:PRK10572 190 QYISDHLASEFDIESVAQHVCLSPSRLAHLFrQQLG-ISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSR 268

                         90
                 ....*....|....*..
gi 446196781 255 LFRKNTERSPSEYRRQY 271
Cdd:PRK10572 269 VFKKCTGASPSEFRARC 285
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
158-275 1.54e-12

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 66.24  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 158 GSQIQTASRSQALFEAIRDYIDERYASALTRESVAQAFYISPNYL-SHLFQKTGAIGFNeYLNHTRLEHAKTLLKGYDLK 236
Cdd:PRK13503 160 SSLQENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLhRQLKQQTGLTPQR-YLNRLRLLKARHLLRHSDAS 238

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446196781 237 VKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQYHSQL 275
Cdd:PRK13503 239 VTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQGRDGFL 277
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
197-271 2.20e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 65.70  E-value: 2.20e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446196781 197 ISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK13501 204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRF 278
PRK10371 PRK10371
transcriptional regulator MelR;
158-269 1.88e-11

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 63.30  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 158 GSQIQTASRSQALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKV 237
Cdd:PRK10371 180 THKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSI 259

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446196781 238 KEVAHACGFVDSNYFCRLFRKNTERSPSEYRR 269
Cdd:PRK10371 260 LDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
172-268 1.87e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 60.07  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 172 EAIRDYIDERYASALTRESVAQAF----YISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFV 247
Cdd:PRK13502 175 ETLLDKLITALANSLECPFALDAFcqqeQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFE 254

                         90       100
                 ....*....|....*....|.
gi 446196781 248 DSNYFCRLFRKNTERSPSEYR 268
Cdd:PRK13502 255 DSNYFSVVFTRETGMTPSQWR 275
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
172-268 1.48e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 54.72  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 172 EAIRDYIDERYASALTRESVAQAF----YISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFV 247
Cdd:PRK13500 205 ETLLDKLITRLAASLKSPFALDKFcdeaSCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFE 284

                         90       100
                 ....*....|....*....|.
gi 446196781 248 DSNYFCRLFRKNTERSPSEYR 268
Cdd:PRK13500 285 DSNYFSVVFTRETGMTPSQWR 305
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 55-271 3.99e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 53.50  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781  55 GAGATLVPGDVLYVPAGGWNFPQWQAPATTFSVLFGK----QQLGFSVVQWDGKQYQNLAKQHVARRgprigsFLLQTLN 130
Cdd:PRK09685  88 DRQVQLAAGDITLIDASRPCSIYPQGLSEQISLLLPRelveQYFPGQKPACAGRLSASLPMVQLSHR------LLQQSMN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 131 EMQMQPQEQQTARLIVASLLshcRDLLGSQIQTASRSQALFEAIRDYIDERYAS-ALTRESVAQAFYISPNYLSHLFQKT 209
Cdd:PRK09685 162 GPALSETESEALLEALIALL---RPALHQRESVQPRRERQFQKVVALIDQSIQEeILRPEWIAGELGISVRSLYRLFAEQ 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446196781 210 GAIgFNEYLNHTRLEHAKTLLKGY--DLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09685 239 GLV-VAQYIRNRRLDRCADDLRPAadDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
ftrA PRK09393
transcriptional activator FtrA; Provisional
 143-271 7.55e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 52.66  E-value: 7.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 143 RLIVASllsHcRDllGSQIQTASRSQALFEAIR-----DYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEY 217
Cdd:PRK09393 193 RLVVPP---H-RD--GGQAQFVPRPVASRESDRlgpliDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEW 266

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446196781 218 LNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09393 267 LLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 234-269 1.65e-07

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 46.76  E-value: 1.65e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446196781  234 DLKVKEVAHACGFvDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam00165   8 NLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
168-270 3.07e-07

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 48.00  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 168 QALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFV 247
Cdd:PRK10219   4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                         90       100
                 ....*....|....*....|...
gi 446196781 248 DSNYFCRLFRKNTERSPSEYRRQ 270
Cdd:PRK10219  84 SQQTFSRVFRRQFDRTPSDYRHR 106
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 178-272 5.94e-07

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 49.54  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 178 IDERYASALTRESVAQAFYISPNYLSHLFQKTGAiGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYFCRLFR 257
Cdd:PRK09978 151 INNNIAHEWTLARIASELLMSPSLLKKKLREEET-SYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFR 229

                         90
                 ....*....|....*..
gi 446196781 258 KNTERSPSEY--RRQYH 272
Cdd:PRK09978 230 NYYGMTPTEYqeRSAQG 246
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 174-274 7.04e-07

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 49.31  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 174 IRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIgFNEYLNHTRLEHAKTLLKgYDLKVKEVAHACGFVDSNYFC 253
Cdd:PRK09940 139 VRNIVNMKLAHPWKLKDICDCLYISESLLKKKLKQEQTT-FSQILLDARMQHAKNLIR-VEGSVNKIAEQCGYASTSYFI 216

                         90       100
                 ....*....|....*....|.
gi 446196781 254 RLFRKNTERSPSEYRRQYHSQ 274
Cdd:PRK09940 217 YAFRKHFGNSPKRVSKEYRCQ 237
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 169-267 6.05e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.52  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 169 ALFEAIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAiGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVD 248
Cdd:PRK15186 181 TLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENT-SFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDS 259

                         90
                 ....*....|....*....
gi 446196781 249 SNYFCRLFRKNTERSPSEY 267
Cdd:PRK15186 260 ASYFTCVFKKHFKTTPSEF 278
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 45-71 1.51e-03

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 36.72  E-value: 1.51e-03
                         10        20
                 ....*....|....*....|....*....
gi 446196781  45 IVLEGEF--VDTGAGATLVPGDVLYVPAG 71
Cdd:cd02228   38 YVLEGELeiTDDGQTVTAKPGDVLFIPKG 66
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 178-219 3.00e-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: 34.82  E-value: 3.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446196781  178 IDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLN 219
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 45-71 3.55e-03

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 36.50  E-value: 3.55e-03
                         10        20
                 ....*....|....*....|....*....
gi 446196781  45 IVLEGEFVDTGAGATLV--PGDVLYVPAG 71
Cdd:COG4766   72 YVLEGTLTIEIDGETVTagPGDVIYIPKG 100
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
173-268 6.65e-03

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 35.85  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446196781 173 AIRDYIDERYASALTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYDLKVKEVAHACGFVDSNYF 252
Cdd:PRK11511  13 SILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTL 92

                         90
                 ....*....|....*.
gi 446196781 253 CRLFRKNTERSPSEYR 268
Cdd:PRK11511  93 TRTFKNYFDVPPHKYR 108
 
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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