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Conserved domains on  [gi|1176858758|ref|WP_082615536|]
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AraC family transcriptional regulator [Acidovorax sp. Root267]

Protein Classification

helix-turn-helix domain-containing protein( domain architecture ID 11454391)

helix-turn-helix (HTH) domain-containing protein with an AraC family HTH domain, binds DNA and may function as a transcriptional regulator

CATH:  1.10.10.60
Gene Ontology:  GO:0003700|GO:0003677
PubMed:  10473770|15808743|8831795

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
59-304 1.06e-19

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 86.76  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  59 LIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLDGLPTAWALG 138
Cdd:COG2207    11 LLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 139 SDSAPVIAHAIAQMHQDTQTHAASLHAHALLRYQLYAL-LTRLRMAHEQQSAQSVPPGRALQRFKAFELLVEKHFATWHQ 217
Cdd:COG2207    91 LVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLaLLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 218 LPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEF 297
Cdd:COG2207   171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250


                  ....*..
gi 1176858758 298 RCRQTAN 304
Cdd:COG2207   251 RKRLRAR 257
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
59-304 1.06e-19

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 86.76  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  59 LIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLDGLPTAWALG 138
Cdd:COG2207    11 LLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 139 SDSAPVIAHAIAQMHQDTQTHAASLHAHALLRYQLYAL-LTRLRMAHEQQSAQSVPPGRALQRFKAFELLVEKHFATWHQ 217
Cdd:COG2207    91 LVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLaLLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 218 LPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEF 297
Cdd:COG2207   171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250


                  ....*..
gi 1176858758 298 RCRQTAN 304
Cdd:COG2207   251 RKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
221-298 1.08e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.87  E-value: 1.08e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176858758 221 YAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTT-WPVARIAEGLGYSDLANFAKFFKREAGCTPTEFR 298
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
218-298 1.26e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.83  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  218 LPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEF 297
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 1176858758  298 R 298
Cdd:smart00342  84 R 84
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
50-298 1.77e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 67.05  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  50 STYRYAFPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLD 129
Cdd:PRK13500   62 AEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIPGFSASA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 130 GLPtAWALGSDSAPVIAHAIAQMHQDTQTHAASLHAHA-LLRYQLYALLTRLRMaheqqSAQSVPPGRALQRFKAFELLV 208
Cdd:PRK13500  142 GQP-HWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAeLLFGQLVMLLNRHRY-----TSDSLPPTSSETLLDKLITRL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 209 EKHFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKR 288
Cdd:PRK13500  216 AASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTR 295

                         250
                  ....*....|
gi 1176858758 289 EAGCTPTEFR 298
Cdd:PRK13500  296 ETGMTPSQWR 305
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 56-181 2.34e-04

HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380382 [Multi-domain]  Cd Length: 147  Bit Score: 40.71  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  56 FPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAApaaqaqapvDGLDGLPTA- 134
Cdd:cd06977    22 FHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFLFL---------DWLDTLPGYl 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1176858758 135 -------WALGSDSAPVIAHAIAQM-HQDTQTHAASLHAHALLRYQLYALLTRLR 181
Cdd:cd06977    93 ahqfqshWRLNSSTLREIRQLIDQLeSELEERDAGSELMAEALFLQLLVLLSRHR 147
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
59-304 1.06e-19

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 86.76  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  59 LIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLDGLPTAWALG 138
Cdd:COG2207    11 LLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 139 SDSAPVIAHAIAQMHQDTQTHAASLHAHALLRYQLYAL-LTRLRMAHEQQSAQSVPPGRALQRFKAFELLVEKHFATWHQ 217
Cdd:COG2207    91 LVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLaLLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 218 LPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEF 297
Cdd:COG2207   171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250


                  ....*..
gi 1176858758 298 RCRQTAN 304
Cdd:COG2207   251 RKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
221-298 1.08e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.87  E-value: 1.08e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176858758 221 YAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTT-WPVARIAEGLGYSDLANFAKFFKREAGCTPTEFR 298
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
218-298 1.26e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.83  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  218 LPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEF 297
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 1176858758  298 R 298
Cdd:smart00342  84 R 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 186-298 5.20e-14

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: 71.34  E-value: 5.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 186 QQSAQSVPPGRALQRFKAFELLVEKHFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTW 265
Cdd:COG4977   197 QFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDL 276

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1176858758 266 PVARIAEGLGYSDLANFAKFFKREAGCTPTEFR 298
Cdd:COG4977   277 SIEEIAAACGFGSASHFRRAFRRRFGVSPSAYR 309
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
50-298 1.77e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 67.05  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  50 STYRYAFPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLD 129
Cdd:PRK13500   62 AEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIPGFSASA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 130 GLPtAWALGSDSAPVIAHAIAQMHQDTQTHAASLHAHA-LLRYQLYALLTRLRMaheqqSAQSVPPGRALQRFKAFELLV 208
Cdd:PRK13500  142 GQP-HWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAeLLFGQLVMLLNRHRY-----TSDSLPPTSSETLLDKLITRL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 209 EKHFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKR 288
Cdd:PRK13500  216 AASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTR 295

                         250
                  ....*....|
gi 1176858758 289 EAGCTPTEFR 298
Cdd:PRK13500  296 ETGMTPSQWR 305
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
50-298 8.90e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 64.69  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  50 STYRYAFPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAAPAAQAQAPVDGLD 129
Cdd:PRK13502   32 AEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVLQNIIYCPERLKLNVNWQAMIPGFQGAQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 130 GLPtAWALGSDSAPVIAHAIAQM-HQDTQTHAASLHAHALLRYQLYALLTRLRMAHEQQSAQSvppgRALQRFKAFELL- 207
Cdd:PRK13502  112 WHP-HWRLGSMGMNQARQVINQLeHESNGRDPLANEMAELLFGQLVMTLKRHRYATDDLPATS----RETLLDKLITALa 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 208 --VEKHFAtwhqLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKF 285
Cdd:PRK13502  187 nsLECPFA----LDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVV 262

                         250
                  ....*....|...
gi 1176858758 286 FKREAGCTPTEFR 298
Cdd:PRK13502  263 FTRETGMTPSQWR 275
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
52-300 1.96e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 57.61  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  52 YRYAFPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFL-----WAAAPAAQAQAPVD 126
Cdd:PRK13501   34 HTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVHDLVLDNIIYCPERLhlnaqWHKLLPPLGPEQNQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 127 GldglptAWALGSDSAPVIAHAIAQMHQDT-QTHAASLHAHALLRYQLYALLTRLRMAHEqqSAQSVPPGRALQRFKAfe 205
Cdd:PRK13501  114 G------YWRLTTQGMAQARPIIQQLAQESrKTDSWSIQLTEVLLLQLAIVLKRHRYRAE--QAHLLPDGEQLDLIMS-- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 206 lLVEKHFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKF 285
Cdd:PRK13501  184 -ALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAV 262

                         250
                  ....*....|....*
gi 1176858758 286 FKREAGCTPTEFRCR 300
Cdd:PRK13501  263 FTREAGMTPRDYRQR 277
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 207-298 1.41e-07

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: 52.36  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 207 LVEKHFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLaHTTWPVARIAEGLGYSDLANFAKFF 286
Cdd:COG2169    92 LIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLSRFYEAF 170

                          90
                  ....*....|..
gi 1176858758 287 KREAGCTPTEFR 298
Cdd:COG2169   171 KKLLGMTPSAYR 182
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 58-169 2.52e-07

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 48.97  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  58 TLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSF--GDTQDWDGWMVLFRPEFLWAAAPAAQaqapvdGLDGLPTAW 135
Cdd:pfam02311  25 VIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYepESEDGWRYRWLYFEPELLERILADIS------ILAGGPLPL 98

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1176858758 136 ALGSDSAPVIAHAIAQM--HQDTQTHAASLHAHALL 169
Cdd:pfam02311  99 LRDPELAALLRALFRLLeeAGRSDDLLAEALLYQLL 134
ftrA PRK09393
transcriptional activator FtrA; Provisional
 211-300 2.12e-06

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 48.81  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758 211 HFATWHQLPRYAQQLGCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREA 290
Cdd:PRK09393  230 HLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRA 309

                          90
                  ....*....|
gi 1176858758 291 GCTPTEFRCR 300
Cdd:PRK09393  310 ATSPAAYRKR 319
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
253-300 7.87e-06

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 46.89  E-value: 7.87e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1176858758 253 VLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEFRCR 300
Cdd:PRK10572  237 ISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRAR 284
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 56-181 2.34e-04

HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380382 [Multi-domain]  Cd Length: 147  Bit Score: 40.71  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176858758  56 FPTLIFVTQGTCLHLVDFEHVRCGPGSVLVLRPGKAHSFGDTQDWDGWMVLFRPEFLWAAApaaqaqapvDGLDGLPTA- 134
Cdd:cd06977    22 FHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFLFL---------DWLDTLPGYl 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1176858758 135 -------WALGSDSAPVIAHAIAQM-HQDTQTHAASLHAHALLRYQLYALLTRLR 181
Cdd:cd06977    93 ahqfqshWRLNSSTLREIRQLIDQLeSELEERDAGSELMAEALFLQLLVLLSRHR 147
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 261-298 5.99e-04

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 37.13  E-value: 5.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1176858758 261 AHTTWPVARIAEGLGYSdLANFAKFFKREAGCTPTEFR 298
Cdd:pfam00165   5 LSTNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQYR 41
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 226-302 3.35e-03

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 38.58  E-value: 3.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176858758 226 GCSEKSLVRASLEAAGVTPKAFISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEFRCRQT 302
Cdd:PRK10296  199 GKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLT 275
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
247-298 6.63e-03

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 35.67  E-value: 6.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176858758 247 FISARIVLEAKRLLAHTTWPVARIAEGLGYSDLANFAKFFKREAGCTPTEFR 298
Cdd:PRK10219   53 YIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFRRQFDRTPSDYR 104
 
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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