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Conserved domains on  [gi|2524318663|ref|WP_286500767|]
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AraC family transcriptional regulator [Citrobacter sp. Cf097]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 15747380)

AraC family transcriptional regulator containing a cupin domain as its effector domain and an AraC family helix-turn-helix (HTH) DNA binding domain, controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

CATH:  2.60.120.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0043565
PubMed:  11282467|33837749|9409145|12270809|19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
185-268 2.87e-27

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663  185 PLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSP 264
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2524318663  265 SEYR 268
Cdd:smart00342  81 SEYR 84
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 23-71 3.23e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member cd02228:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 84  Bit Score: 35.95  E-value: 3.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524318663  23 YFASTNSTTP-ELAYQvdfpRLEIVLEGEF--ADSGIDKVLTPGDVLFVPAG 71
Cdd:cd02228    19 FMELEKKSFPwTLTYD----EIKYVLEGELeiTDDGQTVTAKPGDVLFIPKG 66
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
185-268 2.87e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663  185 PLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSP 264
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2524318663  265 SEYR 268
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
121-274 5.26e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.15  E-value: 5.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 121 IGSFLLQTLHEMQMQPQEQQTAKLIVASLLSHCRDLLGSQIQTASRSQALFDAIRGY--IDERYASPLTRESVAQAFYIS 198
Cdd:COG2207   102 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLllLLLLLLLLLTLEELARELGLS 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524318663 199 PNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG2207   182 PRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
191-270 5.95e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.17  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 191 VAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGY-ELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2524318663 270 Q 270
Cdd:pfam12833  81 R 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
177-271 3.01e-13

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 68.46  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 177 YIDERYASPLTRESVAQAFYISPNYLSHLF-QKTGaIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRL 255
Cdd:PRK10572  191 YISDHLASEFDIESVAQHVCLSPSRLAHLFrQQLG-ISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRV 269

                          90
                  ....*....|....*.
gi 2524318663 256 FRKNTERSPSEYRRQY 271
Cdd:PRK10572  270 FKKCTGASPSEFRARC 285
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 23-71 3.23e-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: 35.95  E-value: 3.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524318663  23 YFASTNSTTP-ELAYQvdfpRLEIVLEGEF--ADSGIDKVLTPGDVLFVPAG 71
Cdd:cd02228    19 FMELEKKSFPwTLTYD----EIKYVLEGELeiTDDGQTVTAKPGDVLFIPKG 66
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
185-268 2.87e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663  185 PLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSP 264
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2524318663  265 SEYR 268
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
121-274 5.26e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.15  E-value: 5.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 121 IGSFLLQTLHEMQMQPQEQQTAKLIVASLLSHCRDLLGSQIQTASRSQALFDAIRGY--IDERYASPLTRESVAQAFYIS 198
Cdd:COG2207   102 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLllLLLLLLLLLTLEELARELGLS 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524318663 199 PNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG2207   182 PRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
191-270 5.95e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.17  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 191 VAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGY-ELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2524318663 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 2.56e-18

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: 82.90  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 146 VASLLSHCRDLLGSQIQTASRSQAL------FDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQK-TGaIGFNEYL 218
Cdd:COG4977   181 VARRLVVDPRRPGGQAQFSPLLVPLghrdprLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAaTG-TTPARYL 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524318663 219 NHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQYHSQ 274
Cdd:COG4977   260 QRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 153-270 3.40e-14

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: 71.62  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 153 CRDLLGSQiqtASRSQALFDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQK-TGaIGFNEYLNHTRLEHAKTLLK 231
Cdd:COG2169    71 CRPDLAPG---SPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAhTG-VTPKAYARARRLLRARQLLQ 146

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2524318663 232 GyELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQ 270
Cdd:COG2169   147 T-GLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRG 184
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
177-271 3.01e-13

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 68.46  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 177 YIDERYASPLTRESVAQAFYISPNYLSHLF-QKTGaIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRL 255
Cdd:PRK10572  191 YISDHLASEFDIESVAQHVCLSPSRLAHLFrQQLG-ISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRV 269

                          90
                  ....*....|....*.
gi 2524318663 256 FRKNTERSPSEYRRQY 271
Cdd:PRK10572  270 FKKCTGASPSEFRARC 285
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
164-271 4.97e-13

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 67.62  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 164 ASRSQAL-----FDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIK 238
Cdd:PRK13501  166 AEQAHLLpdgeqLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRIS 245

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2524318663 239 DVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK13501  246 DIAARCGFEDSNYFSAVFTREAGMTPRDYRQRF 278
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
158-275 3.68e-12

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 65.08  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 158 GSQIQTASRSQALFDAIRGYIDERYASPLTRESVAQAFYISPNYL-SHLFQKTGAIGFNeYLNHTRLEHAKTLLKGYELK 236
Cdd:PRK13503  160 SSLQENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLhRQLKQQTGLTPQR-YLNRLRLLKARHLLRHSDAS 238

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2524318663 237 IKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQYHSQL 275
Cdd:PRK13503  239 VTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQGRDGFL 277
PRK10371 PRK10371
transcriptional regulator MelR;
158-269 7.26e-12

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 64.46  E-value: 7.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 158 GSQIQTASRSQALFDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKI 237
Cdd:PRK10371  180 THKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSI 259

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2524318663 238 KDVAHTCGFIDSNYFCRLFRKNTERSPSEYRR 269
Cdd:PRK10371  260 LDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
164-268 1.04e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 60.84  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 164 ASRSQALFDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHT 243
Cdd:PRK13502  171 ATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQ 250

                          90       100
                  ....*....|....*....|....*
gi 2524318663 244 CGFIDSNYFCRLFRKNTERSPSEYR 268
Cdd:PRK13502  251 CGFEDSNYFSVVFTRETGMTPSQWR 275
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
165-268 1.19e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 60.89  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 165 SRSQALFDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTC 244
Cdd:PRK13500  202 TSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTEC 281

                          90       100
                  ....*....|....*....|....
gi 2524318663 245 GFIDSNYFCRLFRKNTERSPSEYR 268
Cdd:PRK13500  282 GFEDSNYFSVVFTRETGMTPSQWR 305
ftrA PRK09393
transcriptional activator FtrA; Provisional
 154-271 1.11e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 54.97  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 154 RDllGSQIQTASRSQA---------LFDAIRgyidERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLE 224
Cdd:PRK09393  200 RD--GGQAQFVPRPVAsresdrlgpLIDWMR----AHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLA 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2524318663 225 HAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09393  274 RARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 156-271 6.33e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 52.73  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 156 LLGSQIQ----TASRSQALFDAIRGYIDERYASP-LTRESVAQAFYISPNYLSHLFQKTGAIgFNEYLNHTRLEHAKTLL 230
Cdd:PRK09685  180 LLRPALHqresVQPRRERQFQKVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLFAEQGLV-VAQYIRNRRLDRCADDL 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2524318663 231 KGY--ELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSEYRRQY 271
Cdd:PRK09685  259 RPAadDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
168-270 8.35e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 49.54  E-value: 8.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 168 QALFDAIRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFI 247
Cdd:PRK10219    4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                          90       100
                  ....*....|....*....|...
gi 2524318663 248 DSNYFCRLFRKNTERSPSEYRRQ 270
Cdd:PRK10219   84 SQQTFSRVFRRQFDRTPSDYRHR 106
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 174-280 9.04e-08

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 52.01  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 174 IRGYIDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIgFNEYLNHTRLEHAKTLLKgYELKIKDVAHTCGFIDSNYFC 253
Cdd:PRK09940  139 VRNIVNMKLAHPWKLKDICDCLYISESLLKKKLKQEQTT-FSQILLDARMQHAKNLIR-VEGSVNKIAEQCGYASTSYFI 216

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2524318663 254 RLFRKNTERSP----SEYRRQYHSQLTEKKT 280
Cdd:PRK09940  217 YAFRKHFGNSPkrvsKEYRCQRHTGMNTGNT 247
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 234-269 1.12e-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: 47.15  E-value: 1.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2524318663 234 ELKIKDVAHTCGFiDSNYFCRLFRKNTERSPSEYRR 269
Cdd:pfam00165   8 NLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 178-272 4.21e-06

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 47.23  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 178 IDERYASPLTRESVAQAFYISPNYLSHLFQKTGAiGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFR 257
Cdd:PRK09978  151 INNNIAHEWTLARIASELLMSPSLLKKKLREEET-SYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFR 229

                          90
                  ....*....|....*..
gi 2524318663 258 KNTERSPSEY--RRQYH 272
Cdd:PRK09978  230 NYYGMTPTEYqeRSAQG 246
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 187-267 7.53e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.52  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524318663 187 TRESVAQAFYISPNYLSHLFQKTGAiGFNEYLNHTRLEHAKTLLKGYELKIKDVAHTCGFIDSNYFCRLFRKNTERSPSE 266
Cdd:PRK15186  199 ALKDISDSLYMSCSTLKRKLKQENT-SFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSE 277


                  .
gi 2524318663 267 Y 267
Cdd:PRK15186  278 F 278
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 178-219 1.50e-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: 35.59  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2524318663 178 IDERYASPLTRESVAQAFYISPNYLSHLFQKTGAIGFNEYLN 219
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 23-71 3.23e-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: 35.95  E-value: 3.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524318663  23 YFASTNSTTP-ELAYQvdfpRLEIVLEGEF--ADSGIDKVLTPGDVLFVPAG 71
Cdd:cd02228    19 FMELEKKSFPwTLTYD----EIKYVLEGELeiTDDGQTVTAKPGDVLFIPKG 66
 
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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