|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10411 |
PRK10411 |
L-fucose operon activator; |
1-240 |
5.43e-177 |
|
L-fucose operon activator;
Pssm-ID: 236684 [Multi-domain] Cd Length: 240 Bit Score: 485.46 E-value: 5.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSGDPFHIRLKSHYAHK 80
Cdd:PRK10411 1 MKAARQQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSGDPFHIRLKSHYAHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLISQ 160
Cdd:PRK10411 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICQELGKRERIQLISSGGTLERKYGCYVNPSLISQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 161 LKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDERQVATSL 240
Cdd:PRK10411 161 LKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDERQVATSL 240
|
|
| GlpR |
COG1349 |
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ... |
1-233 |
2.36e-72 |
|
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];
Pssm-ID: 440960 [Multi-domain] Cd Length: 254 Bit Score: 221.16 E-value: 2.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSgdPFHIRLKSHYAHK 80
Cdd:COG1349 2 LAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVSSAAAEP--PFAERETLNAEEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPD-INIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLIS 159
Cdd:COG1349 80 RAIARAAASLIEDGDTIFLDAGTTTLALARALPDrRNLTVVTNSLNIANELAERPNIEVILLGGELRPSSGSLVGPLAEE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446564998 160 QLKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
Cdd:COG1349 160 ALRRFRADKAFLGASGIDAEGGLTTFDEEEAEVKRAMIEAARRVILLADSSKFGRRALARVAPLSEIDVLITDA 233
|
|
| DeoRC |
pfam00455 |
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive ... |
75-233 |
2.41e-57 |
|
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive versions of the ISOCOT fold, but retain the substrate binding site. DeorC senses diverse sugar derivatives such as deoxyribose nucleoside (DeoR), tagatose phosphate (LacR), galactosamine (AgaR), myo-inositol (Bacillus IolR) and L-ascorbate (UlaR). It can also bind L-ascorbate 6-phosphate, agrocinopines, sn-glycerol 3-phosphate, and sulfoquinovose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395365 Cd Length: 160 Bit Score: 179.63 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 75 SHYAHKADIAREALAWIEEGMVIALDASSTCWYLARQLPDI-NIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYV 153
Cdd:pfam00455 1 ENAEEKRRIAKAAASLIEDGDTIFLDAGTTTLELARALPDRrNLTVITNSLNIANELSEKPDIEVILLGGEVRPKTGAFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 154 NPSLISQLKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
Cdd:pfam00455 81 GPLAEEFLRQFNVDKAFIGANGIDLEGGLTTSDEEEAEVKRAMIEAARRVILLADSSKFGKRAFARFAPLEDIDALITDK 160
|
|
| HTH_DEOR |
smart00420 |
helix_turn_helix, Deoxyribose operon repressor; |
5-57 |
8.63e-17 |
|
helix_turn_helix, Deoxyribose operon repressor;
Pssm-ID: 197714 [Multi-domain] Cd Length: 53 Bit Score: 71.87 E-value: 8.63e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446564998 5 RQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKY 57
Cdd:smart00420 1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLTRVHGGAVS 53
|
|
| WHTH_GntR |
cd07377 |
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ... |
19-54 |
2.05e-03 |
|
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.
Pssm-ID: 153418 [Multi-domain] Cd Length: 66 Bit Score: 35.89 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446564998 19 LTTE-ALSEQLKVSKETIRRDLNELQTQGKILRNHGR 54
Cdd:cd07377 25 LPSErELAEELGVSRTTVREALRELEAEGLVERRPGR 61
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10411 |
PRK10411 |
L-fucose operon activator; |
1-240 |
5.43e-177 |
|
L-fucose operon activator;
Pssm-ID: 236684 [Multi-domain] Cd Length: 240 Bit Score: 485.46 E-value: 5.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSGDPFHIRLKSHYAHK 80
Cdd:PRK10411 1 MKAARQQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSGDPFHIRLKSHYAHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLISQ 160
Cdd:PRK10411 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICQELGKRERIQLISSGGTLERKYGCYVNPSLISQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 161 LKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDERQVATSL 240
Cdd:PRK10411 161 LKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDERQVATSL 240
|
|
| GlpR |
COG1349 |
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ... |
1-233 |
2.36e-72 |
|
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];
Pssm-ID: 440960 [Multi-domain] Cd Length: 254 Bit Score: 221.16 E-value: 2.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSgdPFHIRLKSHYAHK 80
Cdd:COG1349 2 LAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVSSAAAEP--PFAERETLNAEEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPD-INIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLIS 159
Cdd:COG1349 80 RAIARAAASLIEDGDTIFLDAGTTTLALARALPDrRNLTVVTNSLNIANELAERPNIEVILLGGELRPSSGSLVGPLAEE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446564998 160 QLKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
Cdd:COG1349 160 ALRRFRADKAFLGASGIDAEGGLTTFDEEEAEVKRAMIEAARRVILLADSSKFGRRALARVAPLSEIDVLITDA 233
|
|
| DeoRC |
pfam00455 |
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive ... |
75-233 |
2.41e-57 |
|
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive versions of the ISOCOT fold, but retain the substrate binding site. DeorC senses diverse sugar derivatives such as deoxyribose nucleoside (DeoR), tagatose phosphate (LacR), galactosamine (AgaR), myo-inositol (Bacillus IolR) and L-ascorbate (UlaR). It can also bind L-ascorbate 6-phosphate, agrocinopines, sn-glycerol 3-phosphate, and sulfoquinovose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395365 Cd Length: 160 Bit Score: 179.63 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 75 SHYAHKADIAREALAWIEEGMVIALDASSTCWYLARQLPDI-NIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYV 153
Cdd:pfam00455 1 ENAEEKRRIAKAAASLIEDGDTIFLDAGTTTLELARALPDRrNLTVITNSLNIANELSEKPDIEVILLGGEVRPKTGAFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 154 NPSLISQLKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
Cdd:pfam00455 81 GPLAEEFLRQFNVDKAFIGANGIDLEGGLTTSDEEEAEVKRAMIEAARRVILLADSSKFGKRAFARFAPLEDIDALITDK 160
|
|
| PRK10906 |
PRK10906 |
DeoR/GlpR family transcriptional regulator; |
5-233 |
6.47e-25 |
|
DeoR/GlpR family transcriptional regulator;
Pssm-ID: 182827 [Multi-domain] Cd Length: 252 Bit Score: 98.78 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 5 RQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYihrQNQDSGDPFHIRLKSHYAHKADIA 84
Cdd:PRK10906 6 RHDAIIELVKQQGYVSTEELVEHFSVSPQTIRRDLNDLAEQNKILRHHGGAAL---PSSSVNTPWHDRKATQTEEKERIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 85 REALAWIEEGMVIALDASSTCWYLARQLPD-INIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLISQLKS 163
Cdd:PRK10906 83 RKVASQIPNGATLFIDIGTTPEAVAHALLNhSNLRIVTNNLNVANTLMAKEDFRIILAGGELRSRDGGIIGEATLDFISQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 164 LEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
Cdd:PRK10906 163 FRLDFGILGISGIDSDGSLLEFDYHEVRTKRAIIENSRHVMLVVDHSKFGRNAMVNMGSISMVDAVYTDQ 232
|
|
| srlR |
PRK10434 |
DNA-binding transcriptional repressor; |
1-233 |
2.54e-21 |
|
DNA-binding transcriptional repressor;
Pssm-ID: 182457 [Multi-domain] Cd Length: 256 Bit Score: 89.36 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKA-ARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYihrqNQDSGDPfHIRLKSHY-- 77
Cdd:PRK10434 1 MKPrQRQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLVILEHAGTVIRTYGGVVL----NKEESDP-PIDHKTLInt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 78 AHKADIAREALAWIEEGMVIALDASSTCW----YLARQlpdINIQVFTNSHPICHELGKRERIQ-LISSGGTLERKYGCY 152
Cdd:PRK10434 76 HKKELIAEAAVSLIHDGDSIILDAGSTVLqmvpLLSRF---NNITVMTNSLHIVNALSELDNEQtILMPGGTFRKKSASF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 153 VNPSLISQLKSLEID-LFIfSCEGIDSSGALWDSNAINADYKSMlLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIIS 231
Cdd:PRK10434 153 HGQLAENAFEHFTFDkLFI-GTDGIDLNAGVTTFNEVYTVSKAM-CNAAREIILMADSSKFGRKSPNVVCSLEKVDKLIT 230
|
..
gi 446564998 232 DE 233
Cdd:PRK10434 231 DA 232
|
|
| PRK09802 |
PRK09802 |
DeoR family transcriptional regulator; |
5-240 |
1.46e-19 |
|
DeoR family transcriptional regulator;
Pssm-ID: 182086 [Multi-domain] Cd Length: 269 Bit Score: 84.91 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 5 RQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAkYIHRQNQDSGDPfHIRLKS--HYAHKAD 82
Cdd:PRK09802 18 RREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGIAVRAYGGA-LICDSTTPSVEP-SVEDKSalNTAMKRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 83 IAREALAWIEEGMVIALDASSTCWYLARQLPD-INIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSLISQL 161
Cdd:PRK09802 96 VAKAAVELIQPGHRVILDSGTTTFEIARLMRKhTDVIAMTNGMNVANALLEAEGVELLMTGGHLRRQSQSFYGDQAEQSL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446564998 162 KSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDERQVATSL 240
Cdd:PRK09802 176 QNYHFDMLFLGVDAIDLERGVSTHNEDEARLNRRMCEVAERIIVVTDSSKFNRSSLHKIIDTQRIDMIIVDEGIPADSL 254
|
|
| HTH_DeoR |
pfam08220 |
DeoR-like helix-turn-helix domain; |
5-61 |
9.20e-19 |
|
DeoR-like helix-turn-helix domain;
Pssm-ID: 285436 [Multi-domain] Cd Length: 57 Bit Score: 77.30 E-value: 9.20e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446564998 5 RQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYIHRQ 61
Cdd:pfam08220 1 RIQQILELLKQQGTLSVEELAELLGVSEMTIRRDLNELEEQGLLTRTHGGAVSNSST 57
|
|
| HTH_DEOR |
smart00420 |
helix_turn_helix, Deoxyribose operon repressor; |
5-57 |
8.63e-17 |
|
helix_turn_helix, Deoxyribose operon repressor;
Pssm-ID: 197714 [Multi-domain] Cd Length: 53 Bit Score: 71.87 E-value: 8.63e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446564998 5 RQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKY 57
Cdd:smart00420 1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLTRVHGGAVS 53
|
|
| PRK13509 |
PRK13509 |
HTH-type transcriptional regulator UlaR; |
3-211 |
1.45e-16 |
|
HTH-type transcriptional regulator UlaR;
Pssm-ID: 184100 [Multi-domain] Cd Length: 251 Bit Score: 76.20 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 3 AARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQGKI--LRNHgrAKYIHrQNQDSGDPFHIRLKSHYAHK 80
Cdd:PRK13509 4 AQRHQILLELLAQLGFVTVEKVIERLGISPATARRDINKLDESGKLkkVRNG--AEAIT-QQRPRWTPMNIHQAQNHDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 81 ADIAREALAWIEEGMVIALDASSTCWYLARQLPDINIQVFTNSHPICHELGKRERIQLISSGGTLERKYGCYVNPSliSQ 160
Cdd:PRK13509 81 VRIAKAASQLCNPGESVVINCGSTAFLLGRELCGKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQSITLSPQ--GS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446564998 161 LKSLEIDLFIF-SCEGIDSSGaLWDSNAINADYKSMLLKRAAQSLLLIDKSK 211
Cdd:PRK13509 159 ENSLYAGHWMFtSGKGLTADG-LYKTDMLTAMAEQKMLSVVGKLVVLVDSSK 209
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
1-46 |
5.38e-08 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 52.39 E-value: 5.38e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNELQTQG 46
Cdd:COG2378 2 SRLERLLALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELG 47
|
|
| HTH_GNTR |
smart00345 |
helix_turn_helix gluconate operon transcriptional repressor; |
7-58 |
2.22e-04 |
|
helix_turn_helix gluconate operon transcriptional repressor;
Pssm-ID: 197669 [Multi-domain] Cd Length: 60 Bit Score: 38.32 E-value: 2.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446564998 7 QAIVDLLLNH-TSLTTE-ALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYI 58
Cdd:smart00345 7 EDIVSGELRPgDKLPSErELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
7-49 |
2.35e-04 |
|
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
Pssm-ID: 429896 [Multi-domain] Cd Length: 52 Bit Score: 37.80 E-value: 2.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446564998 7 QAIVDLLLNHTS-LTTEALSEQLKVSKETIRRDLNELQTQGKIL 49
Cdd:pfam08279 1 LQILQLLLEARGpISGQELAEKLGVSRRTIRRDIKILEELGVPI 44
|
|
| ArgR |
COG1438 |
Arginine repressor [Transcription]; |
1-97 |
2.79e-04 |
|
Arginine repressor [Transcription];
Pssm-ID: 441047 Cd Length: 152 Bit Score: 40.11 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 1 MKAARQQAIVDLLLNHTSLTTEALSEQLK-----VSKETIRRDLNELQTqGKILRNHGRAKY-IHRQNQDSGDPfhiRLK 74
Cdd:COG1438 2 KKAARQAKIKEIISEEEIETQEELVELLKeegfnVTQATVSRDLKELGL-VKVPNADGGYVYaLPEEGGPNPEE---RLK 77
|
90 100
....*....|....*....|....*
gi 446564998 75 ShyahkadIAREALAWIE--EGMVI 97
Cdd:COG1438 78 R-------LLRELVVSIDhsGNLVV 95
|
|
| GntR |
pfam00392 |
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ... |
7-58 |
3.73e-04 |
|
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.
Pssm-ID: 306822 [Multi-domain] Cd Length: 64 Bit Score: 37.59 E-value: 3.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446564998 7 QAIVDLLLN-----HTSLTTE-ALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYI 58
Cdd:pfam00392 7 ARLREDILSgrlrpGDKLPSErELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
|
|
| PRK04424 |
PRK04424 |
transcription factor FapR; |
2-42 |
1.24e-03 |
|
transcription factor FapR;
Pssm-ID: 179847 [Multi-domain] Cd Length: 185 Bit Score: 38.65 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446564998 2 KAARQQAIVDLLLNHTSLTTEALSEQLKVSKETIRRDLNEL 42
Cdd:PRK04424 5 KKERQKALQELIEENPFITDEELAEKFGVSIQTIRLDRMEL 45
|
|
| MngR |
COG2188 |
DNA-binding transcriptional regulator, GntR family [Transcription]; |
23-54 |
1.60e-03 |
|
DNA-binding transcriptional regulator, GntR family [Transcription];
Pssm-ID: 441791 [Multi-domain] Cd Length: 238 Bit Score: 38.69 E-value: 1.60e-03
10 20 30
....*....|....*....|....*....|..
gi 446564998 23 ALSEQLKVSKETIRRDLNELQTQGKILRNHGR 54
Cdd:COG2188 34 ELAEEFGVSRMTVRKALDELVEEGLLERRQGR 65
|
|
| WHTH_GntR |
cd07377 |
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ... |
19-54 |
2.05e-03 |
|
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.
Pssm-ID: 153418 [Multi-domain] Cd Length: 66 Bit Score: 35.89 E-value: 2.05e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446564998 19 LTTE-ALSEQLKVSKETIRRDLNELQTQGKILRNHGR 54
Cdd:cd07377 25 LPSErELAEELGVSRTTVREALRELEAEGLVERRPGR 61
|
|
| HTH_ICLR |
smart00346 |
helix_turn_helix isocitrate lyase regulation; |
4-93 |
4.29e-03 |
|
helix_turn_helix isocitrate lyase regulation;
Pssm-ID: 214629 [Multi-domain] Cd Length: 91 Bit Score: 35.64 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446564998 4 ARQQAIVDLLLN-HTSLTTEALSEQLKVSKETIRRDLNELQTQGKILRNHGRAKYihrqnqdSGDPFHIRLKSHYAHKAD 82
Cdd:smart00346 5 ERGLAVLRALAEePGGLTLAELAERLGLSKSTAHRLLNTLQELGYVEQDGQNGRY-------RLGPKVLELGQSYLSSLD 77
|
90
....*....|.
gi 446564998 83 IAREALAWIEE 93
Cdd:smart00346 78 LREVAKPVLEE 88
|
|
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
12-53 |
4.61e-03 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 37.92 E-value: 4.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446564998 12 LLLNHTSLTTEALSEQLKVSKETIRRDLNELqtqGKILRNHG 53
Cdd:COG3711 5 LLKNNNVVTAKELAKKLNVSERTIRYDIKKI---NEWLKKNG 43
|
|
| Tau138_eWH |
cd16169 |
extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits ... |
5-48 |
4.87e-03 |
|
extended winged-helix domain of tau138 and related proteins; Tau138 is one of three subunits of the tauB subcomplex of yeast transcription factor IIIC. This extended winged-helix domain of tau138 appears to interact with the TPR (tetratricopeptide repeat) array of tauA subunit tau131, and may therefore play a role in linking tauA, tauB, and TFIIIB to regulate the formation of the RNA polymerase III pre-initiation complex.
Pssm-ID: 320085 Cd Length: 97 Bit Score: 35.64 E-value: 4.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446564998 5 RQQAIVDLL------LNHTSLTTEALSEQLKVS----KETIRRDLNELQTQGKI 48
Cdd:cd16169 7 RENEILEVLkelggvVNLEKKFLEEHEKLLGSLtrmdKKTLKRDLNKLEEEGKL 60
|
|
| |
