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Conserved domains on  [gi|503995461|ref|WP_014229455|]
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MULTISPECIES: AraC family transcriptional regulator [Klebsiella]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 12123318)

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;
227-310 4.72e-26

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.78  E-value: 4.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   227 NWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 503995461   307 GALR 310
Cdd:smart00342  81 SEYR 84
Cupin_6 pfam12852
Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin ...
 7-195 9.98e-25

Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin superfamily. Some of the proteins in this family are annotated as being members of the AraC family of transcription factors, in which case this domain corresponds to the ligand binding domain.


:

Pssm-ID: 432833  Cd Length: 184  Bit Score: 98.53  E-value: 9.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461    7 DLTSELLRGMRLSGVNYRRIETSRPFGVEFGFVPGkAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGHVLLSDDQ 86
Cdd:pfam12852   1 DVLSDLLAGLRLRGAVFFRGVLRAPWALRFPAGDG-ATFHVVLRGSCWLRLPGGEPVRLRAGDLVLLPRGDPHVLADDPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   87 ATVVNVSRLPSEPVCGSVSCVKNACDDAksdsAIIFSACMDFELGGMQPLVKAMPEVMLVSSLLTSRPEIPPMLAAMERE 166
Cdd:pfam12852  80 TPPVPVDPLSRAPRPGEGEPVVGGGGAA----TVLLCGAFQFDGEAANPLLAALPPVLHVPADEAAAPWLRALLELLAAE 155

                         170       180
                  ....*....|....*....|....*....
gi 503995461  167 SLTRQAGYAGILARLADVVAALIVRGWVE 195
Cdd:pfam12852 156 LAEDRPGSQAVLDRLLDLLLVQALRAWLA 184
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 4.72e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.78  E-value: 4.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   227 NWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 503995461   307 GALR 310
Cdd:smart00342  81 SEYR 84
Cupin_6 pfam12852
Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin ...
 7-195 9.98e-25

Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin superfamily. Some of the proteins in this family are annotated as being members of the AraC family of transcription factors, in which case this domain corresponds to the ligand binding domain.


Pssm-ID: 432833  Cd Length: 184  Bit Score: 98.53  E-value: 9.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461    7 DLTSELLRGMRLSGVNYRRIETSRPFGVEFGFVPGkAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGHVLLSDDQ 86
Cdd:pfam12852   1 DVLSDLLAGLRLRGAVFFRGVLRAPWALRFPAGDG-ATFHVVLRGSCWLRLPGGEPVRLRAGDLVLLPRGDPHVLADDPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   87 ATVVNVSRLPSEPVCGSVSCVKNACDDAksdsAIIFSACMDFELGGMQPLVKAMPEVMLVSSLLTSRPEIPPMLAAMERE 166
Cdd:pfam12852  80 TPPVPVDPLSRAPRPGEGEPVVGGGGAA----TVLLCGAFQFDGEAANPLLAALPPVLHVPADEAAAPWLRALLELLAAE 155

                         170       180
                  ....*....|....*....|....*....
gi 503995461  167 SLTRQAGYAGILARLADVVAALIVRGWVE 195
Cdd:pfam12852 156 LAEDRPGSQAVLDRLLDLLLVQALRAWLA 184
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
229-317 2.85e-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: 2.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 229 KVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAPGA 308
Cdd:COG2207  170 TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                 ....*....
gi 503995461 309 LRDLSREEG 317
Cdd:COG2207  250 YRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
233-310 1.18e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 1.18e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995461  233 LAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHE-GQALEKVAFRLGYSSHAAFSRAFKRIIGKAPGALR 310
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
ftrA PRK09393
transcriptional activator FtrA; Provisional
 213-310 2.46e-16

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 78.08  E-value: 2.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 213 LAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHA 292
Cdd:PRK09393 220 LGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEE 299

                         90
                 ....*....|....*...
gi 503995461 293 AFSRAFKRIIGKAPGALR 310
Cdd:PRK09393 300 SLRHHFRRRAATSPAAYR 317
cupin_YkgD-like_N cd06995
AraC/XylS family transcriptional regulators similar to Escherichia coli YkgD, N-terminal cupin ...
 40-98 1.33e-06

AraC/XylS family transcriptional regulators similar to Escherichia coli YkgD, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is YkgD, an uncharacterized Escherichia coli protein thought to be a transcriptional regulator. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380399  Cd Length: 114  Bit Score: 46.56  E-value: 1.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503995461  40 PGKAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGHVLLSDDQATVVNVSRLPSE 98
Cdd:cd06995   35 LGEARFHIVLQGECRLELPGGESLTLSPGDVVLLPQGSAHRLHSGSNKDAAVPPTLSSD 93
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 4.72e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 98.78  E-value: 4.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   227 NWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 503995461   307 GALR 310
Cdd:smart00342  81 SEYR 84
Cupin_6 pfam12852
Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin ...
 7-195 9.98e-25

Cupin; This is a family of bacterial and eukaryotic proteins that belong to the Cupin superfamily. Some of the proteins in this family are annotated as being members of the AraC family of transcription factors, in which case this domain corresponds to the ligand binding domain.


Pssm-ID: 432833  Cd Length: 184  Bit Score: 98.53  E-value: 9.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461    7 DLTSELLRGMRLSGVNYRRIETSRPFGVEFGFVPGkAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGHVLLSDDQ 86
Cdd:pfam12852   1 DVLSDLLAGLRLRGAVFFRGVLRAPWALRFPAGDG-ATFHVVLRGSCWLRLPGGEPVRLRAGDLVLLPRGDPHVLADDPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461   87 ATVVNVSRLPSEPVCGSVSCVKNACDDAksdsAIIFSACMDFELGGMQPLVKAMPEVMLVSSLLTSRPEIPPMLAAMERE 166
Cdd:pfam12852  80 TPPVPVDPLSRAPRPGEGEPVVGGGGAA----TVLLCGAFQFDGEAANPLLAALPPVLHVPADEAAAPWLRALLELLAAE 155

                         170       180
                  ....*....|....*....|....*....
gi 503995461  167 SLTRQAGYAGILARLADVVAALIVRGWVE 195
Cdd:pfam12852 156 LAEDRPGSQAVLDRLLDLLLVQALRAWLA 184
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
229-317 2.85e-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: 2.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 229 KVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAPGA 308
Cdd:COG2207  170 TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                 ....*....
gi 503995461 309 LRDLSREEG 317
Cdd:COG2207  250 YRKRLRARA 258
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 209-310 9.67e-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: 95.99  E-value: 9.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 209 RDPKLAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGY 288
Cdd:COG4977  208 RDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGF 287

                         90       100
                 ....*....|....*....|..
gi 503995461 289 SSHAAFSRAFKRIIGKAPGALR 310
Cdd:COG4977  288 GSASHFRRAFRRRFGVSPSAYR 309
HTH_18 pfam12833
Helix-turn-helix domain;
233-310 1.18e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 1.18e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995461  233 LAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHE-GQALEKVAFRLGYSSHAAFSRAFKRIIGKAPGALR 310
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
ftrA PRK09393
transcriptional activator FtrA; Provisional
 213-310 2.46e-16

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 78.08  E-value: 2.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 213 LAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHA 292
Cdd:PRK09393 220 LGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEE 299

                         90
                 ....*....|....*...
gi 503995461 293 AFSRAFKRIIGKAPGALR 310
Cdd:PRK09393 300 SLRHHFRRRAATSPAAYR 317
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 209-316 8.85e-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: 70.85  E-value: 8.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 209 RDPKLAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYIsHEGQALEKVAFRLGY 288
Cdd:COG2169   82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGF 160

                         90       100
                 ....*....|....*....|....*...
gi 503995461 289 SSHAAFSRAFKRIIGKAPGALRDLSREE 316
Cdd:COG2169  161 GSLSRFYEAFKKLLGMTPSAYRRGGAGA 188
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 222-310 2.70e-08

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 54.27  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 222 QQPGInwKVEDLAREAGIS-RSVFaeRFLSATGTTPARYLTELRMRLAVQYISH--EGQALEKVAFRLGYSSHAAFSRAF 298
Cdd:PRK09685 211 QEEIL--RPEWIAGELGISvRSLY--RLFAEQGLVVAQYIRNRRLDRCADDLRPaaDDEKITSIAYKWGFSDSSHFSTAF 286

                         90
                 ....*....|..
gi 503995461 299 KRIIGKAPGALR 310
Cdd:PRK09685 287 KQRFGVSPGEYR 298
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
230-310 5.68e-07

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 47.23  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 230 VEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAPGAL 309
Cdd:PRK10219  24 IDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFRRQFDRTPSDY 103


                 .
gi 503995461 310 R 310
Cdd:PRK10219 104 R 104
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 220-261 7.16e-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: 45.22  E-value: 7.16e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 503995461  220 MHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLT 261
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
cupin_YkgD-like_N cd06995
AraC/XylS family transcriptional regulators similar to Escherichia coli YkgD, N-terminal cupin ...
 40-98 1.33e-06

AraC/XylS family transcriptional regulators similar to Escherichia coli YkgD, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is YkgD, an uncharacterized Escherichia coli protein thought to be a transcriptional regulator. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380399  Cd Length: 114  Bit Score: 46.56  E-value: 1.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503995461  40 PGKAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGHVLLSDDQATVVNVSRLPSE 98
Cdd:cd06995   35 LGEARFHIVLQGECRLELPGGESLTLSPGDVVLLPQGSAHRLHSGSNKDAAVPPTLSSD 93
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 227-316 4.54e-06

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 47.23  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 227 NWKVEDLAREAGISRSVFAERfLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKAP 306
Cdd:PRK09978 158 EWTLARIASELLMSPSLLKKK-LREEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTP 236

                         90
                 ....*....|
gi 503995461 307 GALRDLSREE 316
Cdd:PRK09978 237 TEYQERSAQG 246
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
226-310 8.66e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 46.59  E-value: 8.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 226 INWkvEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGYSSHAAFSRAFKRIIGKA 305
Cdd:PRK13503 188 VNW--EALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWS 265


                 ....*
gi 503995461 306 PGALR 310
Cdd:PRK13503 266 PRDIR 270
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
205-315 8.73e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 43.42  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 205 VQVLRDPKLAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAF 284
Cdd:PRK10572 177 LHPPMDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGR 256

                         90       100       110
                 ....*....|....*....|....*....|.
gi 503995461 285 RLGYSSHAAFSRAFKRIIGKAPGALRDLSRE 315
Cdd:PRK10572 257 NVGYDDQLYFSRVFKKCTGASPSEFRARCEE 287
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 207-309 2.02e-04

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 42.29  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 207 VLRDPKLA---KAIYVMHQQPGINWKVEDLAREAGISRSVFaERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVA 283
Cdd:PRK15185 199 ILSSAQITlkeRVYNIISSSPSRQWKLTDVADHIFMSTSTL-KRKLAEEGTSFSDIYLSARMNQAAKLLRIGNHNVNAVA 277

                         90       100
                 ....*....|....*....|....*.
gi 503995461 284 FRLGYSSHAAFSRAFKRIIGKAPGAL 309
Cdd:PRK15185 278 LKCGYDSTSYFIQCFKKYFKTTPSTF 303
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
209-316 6.02e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 40.81  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503995461 209 RDPKLAKAIYVMHQQPGINWKVEDLAREAGISRSVFAERFLSATGTTPARYLTELRMRLAVQYISHEGQALEKVAFRLGY 288
Cdd:PRK13502 174 RETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGF 253

                         90       100
                 ....*....|....*....|....*...
gi 503995461 289 SSHAAFSRAFKRIIGKAPGALRDLSREE 316
Cdd:PRK13502 254 EDSNYFSVVFTRETGMTPSQWRHLSNQS 281
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 228-306 8.23e-04

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 40.45  E-value: 8.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503995461 228 WKVEDLAREAGISRSVFAERfLSATGTTPARYLTELRMRLAVQYISHEGqALEKVAFRLGYSSHAAFSRAFKRIIGKAP 306
Cdd:PRK09940 151 WKLKDICDCLYISESLLKKK-LKQEQTTFSQILLDARMQHAKNLIRVEG-SVNKIAEQCGYASTSYFIYAFRKHFGNSP 227
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 274-310 8.83e-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: 36.36  E-value: 8.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 503995461  274 HEGQALEKVAFRLGYSSHAaFSRAFKRIIGKAPGALR 310
Cdd:pfam00165   6 STNLTIADIADELGFSRSY-FSRLFKKYTGVTPSQYR 41
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 40-93 3.77e-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.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 35.54  E-value: 3.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503995461  40 PGKAQFHFISRGPVLLRMVSGQRLMLQSGDALFIPNGDGH--VLLSDDQATVVNVS 93
Cdd:cd02208   18 PEQDEIFYVLSGEGELTLDDGETVELKAGDIVLIPPGVPHsfVNTSDEPAVFLVVS 73
 
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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