|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
8-309 |
0e+00 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 600.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 8 LPPDPFMCSSDEKQSRSPLALYSEYQRMDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACT 87
Cdd:PRK10371 1 MNTDTFMCSSDEKQTRSPLSLYSEYQRLEIEFRPPHIMPTSHWHGQVEVNVPFDGDVEYLINNEKVQINQGHITLFWACT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 88 PHQLTRPGDCQQMAIFNLPMHLFLSWPLDRELINHVTHGMVIKSLAAQQLSAFEVRRWQQELNHDNEQIRQLAIDEIALM 167
Cdd:PRK10371 81 PHQLTDPGNCRSMAIFNLPMHLFLSWPLDKDLINHVTHGMVIKSLATQQLSPFEVRRWQQELNSPNEQIRQLAIDEIGLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 168 LKRLSLSGWQPILVNKTSRTHKNSVSRHAQFYVSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYI 247
Cdd:PRK10371 161 LKRFSLSGWEPILVNKTSRTHKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082732 248 TAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQRRHGLAL 309
Cdd:PRK10371 241 TAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQRRQTFPG 302
|
|
| cupin_MelR-like_N |
cd06997 |
AraC/XylS family transcriptional regulators similar to Escherichia coli MelR, N-terminal cupin ... |
35-112 |
5.22e-43 |
|
AraC/XylS family transcriptional regulators similar to Escherichia coli MelR, N-terminal cupin domain; This family contains 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, including Escherichia coli MelR, a transcription factor that controls melibiose utilization. MelR is encoded by the melR gene and is essential for melibiose-dependent triggering of the melAB operon that encodes products needed for melibiose catabolism and transport. Expression of melR is autoregulated by MelR, which represses the melR promoter by binding to a target that overlaps the transcript start. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380401 Cd Length: 78 Bit Score: 142.52 E-value: 5.22e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082732 35 MDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIFNLPMHLFLS 112
Cdd:cd06997 1 LQIEHRQPHIMPTPHWHGQVEVNIPFDGDVEYLINEHAVSLNAGHIGLFWGGLPHQLTDTGDCAIMAIFNLPLHHFFS 78
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
215-297 |
5.74e-25 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 95.70 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 215 LTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQ 294
Cdd:smart00342 2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81
|
...
gi 496082732 295 QYR 297
Cdd:smart00342 82 EYR 84
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
200-311 |
3.98e-23 |
|
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: 97.82 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 200 VSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLsDTDKTILDIALTAGFRSSS 279
Cdd:COG2169 86 VARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLS 164
|
90 100 110
....*....|....*....|....*....|..
gi 496082732 280 RFYSTFTRYVGMPPQQYRKLSQQRRHGLALPE 311
Cdd:COG2169 165 RFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTP 196
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
220-298 |
2.69e-17 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 75.32 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 220 VAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALL-SDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRK 298
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
8-309 |
0e+00 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 600.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 8 LPPDPFMCSSDEKQSRSPLALYSEYQRMDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACT 87
Cdd:PRK10371 1 MNTDTFMCSSDEKQTRSPLSLYSEYQRLEIEFRPPHIMPTSHWHGQVEVNVPFDGDVEYLINNEKVQINQGHITLFWACT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 88 PHQLTRPGDCQQMAIFNLPMHLFLSWPLDRELINHVTHGMVIKSLAAQQLSAFEVRRWQQELNHDNEQIRQLAIDEIALM 167
Cdd:PRK10371 81 PHQLTDPGNCRSMAIFNLPMHLFLSWPLDKDLINHVTHGMVIKSLATQQLSPFEVRRWQQELNSPNEQIRQLAIDEIGLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 168 LKRLSLSGWQPILVNKTSRTHKNSVSRHAQFYVSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYI 247
Cdd:PRK10371 161 LKRFSLSGWEPILVNKTSRTHKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082732 248 TAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQRRHGLAL 309
Cdd:PRK10371 241 TAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQRRQTFPG 302
|
|
| cupin_MelR-like_N |
cd06997 |
AraC/XylS family transcriptional regulators similar to Escherichia coli MelR, N-terminal cupin ... |
35-112 |
5.22e-43 |
|
AraC/XylS family transcriptional regulators similar to Escherichia coli MelR, N-terminal cupin domain; This family contains 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, including Escherichia coli MelR, a transcription factor that controls melibiose utilization. MelR is encoded by the melR gene and is essential for melibiose-dependent triggering of the melAB operon that encodes products needed for melibiose catabolism and transport. Expression of melR is autoregulated by MelR, which represses the melR promoter by binding to a target that overlaps the transcript start. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380401 Cd Length: 78 Bit Score: 142.52 E-value: 5.22e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082732 35 MDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIFNLPMHLFLS 112
Cdd:cd06997 1 LQIEHRQPHIMPTPHWHGQVEVNIPFDGDVEYLINEHAVSLNAGHIGLFWGGLPHQLTDTGDCAIMAIFNLPLHHFFS 78
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
215-297 |
5.74e-25 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 95.70 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 215 LTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQ 294
Cdd:smart00342 2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81
|
...
gi 496082732 295 QYR 297
Cdd:smart00342 82 EYR 84
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
200-311 |
3.98e-23 |
|
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: 97.82 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 200 VSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLsDTDKTILDIALTAGFRSSS 279
Cdd:COG2169 86 VARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLS 164
|
90 100 110
....*....|....*....|....*....|..
gi 496082732 280 RFYSTFTRYVGMPPQQYRKLSQQRRHGLALPE 311
Cdd:COG2169 165 RFYEAFKKLLGMTPSAYRRGGAGAAIRFAPTP 196
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
65-304 |
3.75e-20 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 87.91 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 65 EYLINNEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIFNLPMHLFLSWPLDRELINHVTHGMVIKSLAAQQLSAFEVRR 144
Cdd:COG2207 19 LLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 145 WQQELNHDNEQIRQLAIDEIALMLKRLSLSGWQPILVNKTSRTHKNSVSRHAQFYVSQMLEFIAAHYDQALTVNAVAEHV 224
Cdd:COG2207 99 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELAREL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 225 KLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQRR 304
Cdd:COG2207 179 GLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
200-304 |
1.91e-19 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 86.75 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 200 VSQMLEFIAAHYDQALTVNAVAEHVklnpnyAMGV------FQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTA 273
Cdd:COG4977 212 LARAQAWMEANLEEPLSVDELARRA------GMSPrtlerrFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAAC 285
|
90 100 110
....*....|....*....|....*....|.
gi 496082732 274 GFRSSSRFYSTFTRYVGMPPQQYRKLSQQRR 304
Cdd:COG4977 286 GFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
220-298 |
2.69e-17 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 75.32 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 220 VAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALL-SDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRK 298
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
|
| PRK13500 |
PRK13500 |
HTH-type transcriptional activator RhaR; |
30-303 |
6.97e-10 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184091 [Multi-domain] Cd Length: 312 Bit Score: 58.96 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 30 SEYQRMDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIFNLP--M 107
Cdd:PRK13500 45 SDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPerL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 108 HLFLSWPLDRELINhVTHGMVIKSLAAQQLSafEVRRWQQELNHDNEQIRQLAIDEIALMLKRLSLsgwqpiLVNKTSRT 187
Cdd:PRK13500 125 KLNLDWQGAIPGFS-ASAGQPHWRLGSVGMA--QARQVIGQLEHESSQHVPFANEMAELLFGQLVM------LLNRHRYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 188 HKNSVSRHAQFYVSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTIL 267
Cdd:PRK13500 196 SDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLIS 275
|
250 260 270
....*....|....*....|....*....|....*.
gi 496082732 268 DIALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQR 303
Cdd:PRK13500 276 DISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQK 311
|
|
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
192-298 |
2.24e-09 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 57.67 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 192 VSRHAQFYVSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIAL 271
Cdd:PRK09393 212 VASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAE 291
|
90 100
....*....|....*....|....*..
gi 496082732 272 TAGFRSSSRFYSTFTRYVGMPPQQYRK 298
Cdd:PRK09393 292 RAGFGSEESLRHHFRRRAATSPAAYRK 318
|
|
| PRK10219 |
PRK10219 |
superoxide response transcriptional regulator SoxS; |
200-297 |
9.75e-09 |
|
superoxide response transcriptional regulator SoxS;
Pssm-ID: 182314 [Multi-domain] Cd Length: 107 Bit Score: 52.23 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 200 VSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSS 279
Cdd:PRK10219 7 IQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQ 86
|
90
....*....|....*...
gi 496082732 280 RFYSTFTRYVGMPPQQYR 297
Cdd:PRK10219 87 TFSRVFRRQFDRTPSDYR 104
|
|
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
31-303 |
2.99e-08 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 53.90 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 31 EYQRMDIELRPPHAMPTSHWHGQVEVNVPFDGDVEYLINNEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIFNLP--MH 108
Cdd:PRK13502 16 EQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVLQNIIYCPerLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 109 LFLSWpldRELINHVTHGMVIKSLAAQQLSAFEVRRWQQELNHDNEQIRQLAIDEIALMLKRLSLSgwqpiLVNKTSRTH 188
Cdd:PRK13502 96 LNVNW---QAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMT-----LKRHRYATD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 189 KNSVSRHAQFyVSQMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILD 268
Cdd:PRK13502 168 DLPATSRETL-LDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISE 246
|
250 260 270
....*....|....*....|....*....|....*
gi 496082732 269 IALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQR 303
Cdd:PRK13502 247 ISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQS 281
|
|
| PRK15435 |
PRK15435 |
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada; |
212-298 |
1.02e-07 |
|
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
Pssm-ID: 185333 [Multi-domain] Cd Length: 353 Bit Score: 52.49 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 212 DQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDkTILDIALTAGFRSSSRFYSTFTRYVGM 291
Cdd:PRK15435 97 ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGFPDSSSYYRKADETLGM 175
|
....*..
gi 496082732 292 PPQQYRK 298
Cdd:PRK15435 176 TAKQFRH 182
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
206-301 |
6.61e-07 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 49.97 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 206 FIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTF 285
Cdd:PRK10572 191 YISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVF 270
|
90
....*....|....*.
gi 496082732 286 TRYVGMPPQQYRKLSQ 301
Cdd:PRK10572 271 KKCTGASPSEFRARCE 286
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
185-297 |
1.22e-06 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 47.02 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 185 SRTHKNSVSRHAqfyvsqMLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDK 264
Cdd:PRK11511 2 SRRNTDAITIHS------ILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNE 75
|
90 100 110
....*....|....*....|....*....|...
gi 496082732 265 TILDIALTAGFRSSSRFYSTFTRYVGMPPQQYR 297
Cdd:PRK11511 76 PILYLAERYGFESQQTLTRTFKNYFDVPPHKYR 108
|
|
| PRK10296 |
PRK10296 |
DNA-binding transcriptional regulator ChbR; Provisional |
236-298 |
1.80e-06 |
|
DNA-binding transcriptional regulator ChbR; Provisional
Pssm-ID: 182362 [Multi-domain] Cd Length: 278 Bit Score: 48.60 E-value: 1.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082732 236 QRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRK 298
Cdd:PRK10296 210 RRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRK 272
|
|
| PRK13501 |
PRK13501 |
HTH-type transcriptional activator RhaR; |
124-303 |
2.18e-06 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184092 [Multi-domain] Cd Length: 290 Bit Score: 48.36 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 124 THGMVIKSLAAQQLsafevrrwQQELNHDNEQIRQLA---IDEIALMLKRLSLSGwqpilvnktSRTHKNSVSRHAQFYV 200
Cdd:PRK13501 120 TQGMAQARPIIQQL--------AQESRKTDSWSIQLTevlLLQLAIVLKRHRYRA---------EQAHLLPDGEQLDLIM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 201 SQMLEFIAAHYDQAltvnAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSR 280
Cdd:PRK13501 183 SALQQSLGAYFDMA----DFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNY 258
|
170 180
....*....|....*....|...
gi 496082732 281 FYSTFTRYVGMPPQQYRKLSQQR 303
Cdd:PRK13501 259 FSAVFTREAGMTPRDYRQRFIRS 281
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
207-248 |
4.77e-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: 42.91 E-value: 4.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 496082732 207 IAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYIT 248
Cdd:pfam00165 1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
261-298 |
1.07e-05 |
|
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: 41.76 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....*...
gi 496082732 261 DTDKTILDIALTAGFrSSSRFYSTFTRYVGMPPQQYRK 298
Cdd:pfam00165 6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
202-303 |
7.80e-05 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 43.51 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 202 QMLEFIAAHYDQALTVNAVAEHVKLnpnyAMGVFQRVMQQ----TMKQYITAMRINHVRALLSDTDKTILDIALTAGFRS 277
Cdd:PRK13503 175 QLLAWLEDHFAEEVNWEALADQFSL----SLRTLHRQLKQqtglTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGD 250
|
90 100
....*....|....*....|....*.
gi 496082732 278 SSRFYSTFTRYVGMPPqqyRKLSQQR 303
Cdd:PRK13503 251 SNHFSTLFRREFSWSP---RDIRQGR 273
|
|
| PRK09978 |
PRK09978 |
DNA-binding transcriptional regulator GadX; Provisional |
237-302 |
1.34e-03 |
|
DNA-binding transcriptional regulator GadX; Provisional
Pssm-ID: 137624 [Multi-domain] Cd Length: 274 Bit Score: 39.91 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082732 237 RVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFYSTFTRYVGMPPQQYRKLSQQ 302
Cdd:PRK09978 180 REEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQ 245
|
|
| cupin_RmlC-like |
cd02208 |
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
41-103 |
3.73e-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: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082732 41 PPHAMPTSHWHG-QVEVNVPFDGDVEYLIN-NEVVRIEKGYITLFWACTPHQLTRPGDCQQMAIF 103
Cdd:cd02208 7 PPGTSSPPHWHPeQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLV 71
|
|
| PRK15121 |
PRK15121 |
MDR efflux pump AcrAB transcriptional activator RobA; |
203-298 |
9.92e-03 |
|
MDR efflux pump AcrAB transcriptional activator RobA;
Pssm-ID: 185076 [Multi-domain] Cd Length: 289 Bit Score: 36.91 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082732 203 MLEFIAAHYDQALTVNAVAEHVKLNPNYAMGVFQRVMQQTMKQYITAMRINHVRALLSDTDKTILDIALTAGFRSSSRFY 282
Cdd:PRK15121 10 LLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFT 89
|
90
....*....|....*.
gi 496082732 283 STFTRYVGMPPQQYRK 298
Cdd:PRK15121 90 RAFKKQFAQTPALYRR 105
|
|
| |
