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Conserved domains on  [gi|507052278|ref|WP_016123262|]
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MULTISPECIES: bifunctional transcriptional activator/DNA repair enzyme AdaA [Bacillus]

Protein Classification

bifunctional transcriptional activator/DNA repair enzyme AdaA( domain architecture ID 11450612)

bifunctional transcriptional activator/DNA repair enzyme AdaA repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues; the methylation of AdaA by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of the ada operon which consists of adaA and adaB, and of the adjacent gene alkA

CATH:  1.10.10.10
EC:  2.1.1.-
Gene Ontology:  GO:0006281|GO:0032259|GO:0008168|GO:0003677|GO:0003700
PubMed:  1744039|2120677|8831795|2644244|10473770|15808743

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 9-191 2.58e-81

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: 245.73  E-value: 2.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   9 TNEYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRCKPNGITL--PNEEWVE 86
Cdd:COG2169    8 DDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGspPRADLVA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  87 QIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEyLLQTNQSIKEISTAVGIENPEYF 166
Cdd:COG2169   88 RACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQ-LLQTGLSVTDAAYAAGFGSLSRF 166

                        170       180
                 ....*....|....*....|....*
gi 507052278 167 ATLFKKKTGFTPTEYRKKNEMKEGY 191
Cdd:COG2169  167 YEAFKKLLGMTPSAYRRGGAGAAIR 191
 
Name Accession Description Interval E-value
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 9-191 2.58e-81

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: 245.73  E-value: 2.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   9 TNEYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRCKPNGITL--PNEEWVE 86
Cdd:COG2169    8 DDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGspPRADLVA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  87 QIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEyLLQTNQSIKEISTAVGIENPEYF 166
Cdd:COG2169   88 RACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQ-LLQTGLSVTDAAYAAGFGSLSRF 166

                        170       180
                 ....*....|....*....|....*
gi 507052278 167 ATLFKKKTGFTPTEYRKKNEMKEGY 191
Cdd:COG2169  167 YEAFKKLLGMTPSAYRRGGAGAAIR 191
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
1-186 1.84e-38

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 135.31  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   1 MHNEGVTLTNEYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRCKPNGITlP 80
Cdd:PRK15435   1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKAN-P 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  81 NEEWVEQIK---DYIEKhyDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNqSIKEISTA 157
Cdd:PRK15435  80 QQHRLDKIThacRLLEQ--ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILN 156

                        170       180
                 ....*....|....*....|....*....
gi 507052278 158 VGIENPEYFATLFKKKTGFTPTEYRKKNE 186
Cdd:PRK15435 157 AGFPDSSSYYRKADETLGMTAKQFRHGGE 185
Ada_Zn_binding pfam02805
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ...
 11-72 2.30e-36

Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.


Pssm-ID: 460701 [Multi-domain]  Cd Length: 62  Bit Score: 121.40  E-value: 2.30e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507052278   11 EYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRC 72
Cdd:pfam02805   1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
100-182 2.18e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.48  E-value: 2.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   100 LTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPEYFATLFKKKTGFTPT 179
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ...
gi 507052278   180 EYR 182
Cdd:smart00342  82 EYR 84
 
Name Accession Description Interval E-value
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 9-191 2.58e-81

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: 245.73  E-value: 2.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   9 TNEYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRCKPNGITL--PNEEWVE 86
Cdd:COG2169    8 DDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAPGspPRADLVA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  87 QIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEyLLQTNQSIKEISTAVGIENPEYF 166
Cdd:COG2169   88 RACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQ-LLQTGLSVTDAAYAAGFGSLSRF 166

                        170       180
                 ....*....|....*....|....*
gi 507052278 167 ATLFKKKTGFTPTEYRKKNEMKEGY 191
Cdd:COG2169  167 YEAFKKLLGMTPSAYRRGGAGAAIR 191
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
1-186 1.84e-38

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 135.31  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   1 MHNEGVTLTNEYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRCKPNGITlP 80
Cdd:PRK15435   1 MKNATCLTDDQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPDKAN-P 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  81 NEEWVEQIK---DYIEKhyDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNqSIKEISTA 157
Cdd:PRK15435  80 QQHRLDKIThacRLLEQ--ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILN 156

                        170       180
                 ....*....|....*....|....*....
gi 507052278 158 VGIENPEYFATLFKKKTGFTPTEYRKKNE 186
Cdd:PRK15435 157 AGFPDSSSYYRKADETLGMTAKQFRHGGE 185
Ada_Zn_binding pfam02805
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ...
 11-72 2.30e-36

Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.


Pssm-ID: 460701 [Multi-domain]  Cd Length: 62  Bit Score: 121.40  E-value: 2.30e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507052278   11 EYWQAIIHNDSSYDSKFFYAVKSTGIFCRPSCKSRIPNRNNVRIFHHAEQALSENFRPCKRC 72
Cdd:pfam02805   1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
77-189 1.11e-30

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 112.95  E-value: 1.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  77 ITLPNEEWVEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEIST 156
Cdd:COG2207  146 LLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAY 225

                         90       100       110
                 ....*....|....*....|....*....|...
gi 507052278 157 AVGIENPEYFATLFKKKTGFTPTEYRKKNEMKE 189
Cdd:COG2207  226 ELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
100-182 2.18e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.48  E-value: 2.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278   100 LTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPEYFATLFKKKTGFTPT 179
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81


                   ...
gi 507052278   180 EYR 182
Cdd:smart00342  82 EYR 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 85-184 7.39e-28

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: 106.40  E-value: 7.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  85 VEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPE 164
Cdd:COG4977  212 LARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSAS 291

                         90       100
                 ....*....|....*....|
gi 507052278 165 YFATLFKKKTGFTPTEYRKK 184
Cdd:COG4977  292 HFRRAFRRRFGVSPSAYRRR 311
HTH_18 pfam12833
Helix-turn-helix domain;
105-184 2.75e-24

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 91.11  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  105 LAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQ-TNQSIKEISTAVGIENPEYFATLFKKKTGFTPTEYRK 183
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEdTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 507052278  184 K 184
Cdd:pfam12833  81 R 81
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
81-182 9.89e-15

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 66.87  E-value: 9.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  81 NEEWVEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGI 160
Cdd:PRK10219   3 HQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGY 82

                         90       100
                 ....*....|....*....|..
gi 507052278 161 ENPEYFATLFKKKTGFTPTEYR 182
Cdd:PRK10219  83 VSQQTFSRVFRRQFDRTPSDYR 104
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
85-186 7.17e-14

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 68.08  E-value: 7.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  85 VEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPE 164
Cdd:PRK10572 185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264

                         90       100
                 ....*....|....*....|..
gi 507052278 165 YFATLFKKKTGFTPTEYRKKNE 186
Cdd:PRK10572 265 YFSRVFKKCTGASPSEFRARCE 286
PRK10371 PRK10371
transcriptional regulator MelR;
84-183 7.09e-13

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 65.61  E-value: 7.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  84 WVEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENP 163
Cdd:PRK10371 192 YVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSS 271

                         90       100
                 ....*....|....*....|
gi 507052278 164 EYFATLFKKKTGFTPTEYRK 183
Cdd:PRK10371 272 SRFYSTFGKYVGMSPQQYRK 291
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
81-182 4.07e-11

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 60.46  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  81 NEEWVEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGI 160
Cdd:PRK13503 169 SDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGF 248

                         90       100
                 ....*....|....*....|..
gi 507052278 161 ENPEYFATLFKKKTGFTPTEYR 182
Cdd:PRK13503 249 GDSNHFSTLFRREFSWSPRDIR 270
ftrA PRK09393
transcriptional activator FtrA; Provisional
 90-184 1.71e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 58.82  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  90 DYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPEYFATL 169
Cdd:PRK09393 225 DWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHH 304

                         90
                 ....*....|....*
gi 507052278 170 FKKKTGFTPTEYRKK 184
Cdd:PRK09393 305 FRRRAATSPAAYRKR 319
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 92-133 2.27e-10

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: 53.70  E-value: 2.27e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 507052278   92 IEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQ 133
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
100-189 2.93e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 58.19  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278 100 LTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKAtEYLLQTNQS-IKEISTAVGIENPEYFATLFKKKTGFTP 178
Cdd:PRK13500 223 FALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHA-QYLLQHSRLlISDISTECGFEDSNYFSVVFTRETGMTP 301

                         90
                 ....*....|.
gi 507052278 179 TEYRKKNEMKE 189
Cdd:PRK13500 302 SQWRHLNSQKD 312
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
105-184 3.33e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 57.99  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278 105 LAEMCHG---SPFHLQRTFKRIIGLTPIEYIQQFRVLKAtEYLLQTNQS-IKEISTAVGIENPEYFATLFKKKTGFTPTE 180
Cdd:PRK13501 195 MADFCHKnqlVERSLKQLFRQQTGMSISHYLRQIRLCHA-KCLLRGSEHrISDIAARCGFEDSNYFSAVFTREAGMTPRD 273


                 ....
gi 507052278 181 YRKK 184
Cdd:PRK13501 274 YRQR 277
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
116-182 1.68e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 53.13  E-value: 1.68e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507052278 116 LQRTFKRIIGLTPIEYIQQFRVLKAtEYLLQTNQ-SIKEISTAVGIENPEYFATLFKKKTGFTPTEYR 182
Cdd:PRK13502 209 LRQQFRAQTGMTINQYLRQVRICHA-QYLLQHSPlMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
88-186 8.85e-08

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 50.78  E-value: 8.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  88 IKD---YIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPE 164
Cdd:PRK15121   7 IRDlliWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQ 86

                         90       100
                 ....*....|....*....|..
gi 507052278 165 YFATLFKKKTGFTPTEYRKKNE 186
Cdd:PRK15121  87 TFTRAFKKQFAQTPALYRRSPE 108
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
85-190 8.97e-08

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 48.94  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  85 VEQIKDYIEKHYDESLTLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPE 164
Cdd:PRK11511  11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                         90       100
                 ....*....|....*....|....*.
gi 507052278 165 YFATLFKKKTGFTPTEYRKKNEMKEG 190
Cdd:PRK11511  91 TLTRTFKNYFDVPPHKYRMTNMQGES 116
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 88-184 5.65e-07

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 48.60  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  88 IKDYIEKHYDESL----TLDMLAEMCHGSPFHLQRTFKRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENP 163
Cdd:PRK10296 173 LKATVEKMHDKEQfsesALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSP 252

                         90       100
                 ....*....|....*....|.
gi 507052278 164 EYFATLFKKKTGFTPTEYRKK 184
Cdd:PRK10296 253 SLFIKTFKKLTSFTPGSYRKK 273
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 91-184 1.44e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 47.33  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278  91 YIEKHYDES-----LTLDMLAEMCHGSPFHLQRTFKRIiGLTPIEYIQQFRVLKATEYL--LQTNQSIKEISTAVGIENP 163
Cdd:PRK09685 201 KVVALIDQSiqeeiLRPEWIAGELGISVRSLYRLFAEQ-GLVVAQYIRNRRLDRCADDLrpAADDEKITSIAYKWGFSDS 279

                         90       100
                 ....*....|....*....|.
gi 507052278 164 EYFATLFKKKTGFTPTEYRKK 184
Cdd:PRK09685 280 SHFSTAFKQRFGVSPGEYRRK 300
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 145-183 3.87e-06

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: 42.14  E-value: 3.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 507052278  145 LQTNQSIKEISTAVGIeNPEYFATLFKKKTGFTPTEYRK 183
Cdd:pfam00165   5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 101-193 7.65e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 36.44  E-value: 7.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052278 101 TLDMLAEMCHGSPFHLQRTFkRIIGLTPIEYIQQFRVLKATEYLLQTNQSIKEISTAVGIENPEYFATLFKKKTGFTPTE 180
Cdd:PRK09978 160 TLARIASELLMSPSLLKKKL-REEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTE 238

                         90
                 ....*....|...
gi 507052278 181 YRKKNEmkEGYDN 193
Cdd:PRK09978 239 YQERSA--QGLPN 249
 
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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