|
Name |
Accession |
Description |
Interval |
E-value |
| GlpR |
COG1349 |
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ... |
1-253 |
3.91e-110 |
|
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: 317.46 E-value: 3.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYTVDRPVNEKEKMQSSEKN 80
Cdd:COG1349 1 MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVSSAAAEPPFAERETLNAEEKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 81 RIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQV 160
Cdd:COG1349 81 AIARAAASLIEDGDTIFLDAGTTTLALARALPDRRNLTVVTNSLNIANELAERPNIEVILLGGELRPSSGSLVGPLAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 161 LQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMI 240
Cdd:COG1349 161 LRRFRADKAFLGASGIDAEGGLTTFDEEEAEVKRAMIEAARRVILLADSSKFGRRALARVAPLSEIDVLITDAGPPPELL 240
|
250
....*....|...
gi 2536568968 241 NHLEGLGVTVTVV 253
Cdd:COG1349 241 EALEEAGVEVIVA 253
|
|
| AgaR |
NF040755 |
transcriptional repressor AgaR; |
4-253 |
4.33e-75 |
|
transcriptional repressor AgaR;
Pssm-ID: 468715 [Multi-domain] Cd Length: 256 Bit Score: 228.69 E-value: 4.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 4 AERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYT--VDRPVNEKEKMQSSEKNR 81
Cdd:NF040755 5 SERREQIIQRLRQQGSVQVEDLSALFGVSTVTIRNDLAFLEKQGIAVRAYGGALINDGFIpgAEPSVEDKSRLNTAVKRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 82 IGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVL 161
Cdd:NF040755 85 IAAAAAELIKPGDRVILDSGTTTYEIARHLKQHQDVVVMTNGLNVANELLEAEGVEVLMTGGHLRRQSLSFYGDQAEQSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 162 QDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMIN 241
Cdd:NF040755 165 QNYHFDKLFLGVDGFDLERGITTHNEDEARLNRRMCEVAERIIAVTDSSKFGRSSLHKIRDTGRIDTLITDSGIPEEYLQ 244
|
250
....*....|..
gi 2536568968 242 HLEGLGVTVTVV 253
Cdd:NF040755 245 GLRKLGVEVILV 256
|
|
| srlR |
PRK10434 |
DNA-binding transcriptional repressor; |
1-253 |
6.68e-63 |
|
DNA-binding transcriptional repressor;
Pssm-ID: 182457 [Multi-domain] Cd Length: 256 Bit Score: 197.60 E-value: 6.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLsNPYTVDRPVNEKEKMQSSEKN 80
Cdd:PRK10434 1 MKPRQRQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLVILEHAGTVIRTYGGVVL-NKEESDPPIDHKTLINTHKKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 81 RIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFL-RNPEVEVIQLGGLLRKSSSSVMGSYAEQ 159
Cdd:PRK10434 80 LIAEAAVSLIHDGDSIILDAGSTVLQMVPLLSRFNNITVMTNSLHIVNALSeLDNEQTILMPGGTFRKKSASFHGQLAEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 160 VLQDFYFNTLFLGVDGIDLEHGFTTTNamEAH-LNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQ 238
Cdd:PRK10434 160 AFEHFTFDKLFIGTDGIDLNAGVTTFN--EVYtVSKAMCNAAREIILMADSSKFGRKSPNVVCSLEKVDKLITDAGIDPA 237
|
250
....*....|....*
gi 2536568968 239 MINHLEGLGVTVTVV 253
Cdd:PRK10434 238 FRQALEEKGIEVIIT 252
|
|
| DeoRC |
pfam00455 |
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive ... |
75-233 |
2.19e-62 |
|
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: 192.73 E-value: 2.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 75 QSSEKNRIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMG 154
Cdd:pfam00455 2 NAEEKRRIAKAAASLIEDGDTIFLDAGTTTLELARALPDRRNLTVITNSLNIANELSEKPDIEVILLGGEVRPKTGAFVG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536568968 155 SYAEQVLQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDK 233
Cdd:pfam00455 82 PLAEEFLRQFNVDKAFIGANGIDLEGGLTTSDEEEAEVKRAMIEAARRVILLADSSKFGKRAFARFAPLEDIDALITDK 160
|
|
| trans_reg_YciT |
NF040887 |
DNA-binding transcriptional regulator YciT; Involved in osmolarity control regulation |
6-253 |
5.33e-40 |
|
DNA-binding transcriptional regulator YciT; Involved in osmolarity control regulation
Pssm-ID: 468823 [Multi-domain] Cd Length: 246 Bit Score: 138.47 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 6 RHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYTVDrpvnekEKMQS--SEKNRIG 83
Cdd:NF040887 4 RQQQILQLVNDRGRVSVSELAQLTGVSEVTIRQDLNLLEKQSYLKRVHGSAVALDSDDVD------TRMMTnfPLKQKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 84 AAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISiEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVLQD 163
Cdd:NF040887 78 EYAASLVEDGETVFIEGGSTNALLARYLAERKDITIITVSHYIA-HLLKDSACEVILLGGLYQKSSESVVGPLTRLCIQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 164 FYFNTLFLGVDGIDLEHGFTTTNAMEAHL-NRQMIKVSQKVVvLADSTKFGK---RGFGKICGFEDVdyiITDKGISQQM 239
Cdd:NF040887 157 VHFSKAFIGIDGWHPETGFTGRDMMRADVvNAVLAKGAENIV-LTDSSKFGQihpYPLGPLHQFSRV---ITDDGLPADY 232
|
250
....*....|....
gi 2536568968 240 INHLEGLGVTVTVV 253
Cdd:NF040887 233 RQQLEEQGIRVDLV 246
|
|
| HTH_DEOR |
smart00420 |
helix_turn_helix, Deoxyribose operon repressor; |
6-58 |
8.59e-13 |
|
helix_turn_helix, Deoxyribose operon repressor;
Pssm-ID: 197714 [Multi-domain] Cd Length: 53 Bit Score: 61.47 E-value: 8.59e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 6 RHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATL 58
Cdd:smart00420 1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLTRVHGGAVS 53
|
|
| hrcA |
TIGR00331 |
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; ... |
5-145 |
8.11e-05 |
|
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; overproduction prevents induction of these operons by heat shock while deletion allows constitutive expression even at low temperatures. In Bacillus subtilis, hrcA is the first gene of the dnaK operon and so is itself a heat shock gene. [Regulatory functions, DNA interactions]
Pssm-ID: 273017 [Multi-domain] Cd Length: 337 Bit Score: 43.04 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 5 ERHQFILNRIQQDqYIN---------VVELCkQLKVSSVTIRKDLKLLEDKHLLFRTH--GG---ATLSNPYTVDRPVnE 70
Cdd:TIGR00331 2 ERQRKILKAIVEE-YIKtgqpvgsktLLEKY-NLGLSSATIRNDMADLEDLGFIEKPHtsSGripTDKGYRYYVDHLL-K 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536568968 71 KEKMQSSEKNRIGAAAAKLLKENDSIvvasgttLLYFVKSIPNGLNLTVVTSSLNISIEFLRNpeVEVIQLGGLL 145
Cdd:TIGR00331 79 VDSLTEEEKRRIQNQFLQRRFYLEKV-------LQLAASLLSELTNYTAVVLGPRLSQDKLKH--IELIPLDPNL 144
|
|
| WHTH_GntR |
cd07377 |
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ... |
10-57 |
1.05e-04 |
|
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: 39.35 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2536568968 10 ILNRIQQDQY------INVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGAT 57
Cdd:cd07377 10 LREAILSGELkpgdrlPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGT 63
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GlpR |
COG1349 |
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ... |
1-253 |
3.91e-110 |
|
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: 317.46 E-value: 3.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYTVDRPVNEKEKMQSSEKN 80
Cdd:COG1349 1 MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVHGGAVLVSSAAAEPPFAERETLNAEEKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 81 RIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQV 160
Cdd:COG1349 81 AIARAAASLIEDGDTIFLDAGTTTLALARALPDRRNLTVVTNSLNIANELAERPNIEVILLGGELRPSSGSLVGPLAEEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 161 LQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMI 240
Cdd:COG1349 161 LRRFRADKAFLGASGIDAEGGLTTFDEEEAEVKRAMIEAARRVILLADSSKFGRRALARVAPLSEIDVLITDAGPPPELL 240
|
250
....*....|...
gi 2536568968 241 NHLEGLGVTVTVV 253
Cdd:COG1349 241 EALEEAGVEVIVA 253
|
|
| AgaR |
NF040755 |
transcriptional repressor AgaR; |
4-253 |
4.33e-75 |
|
transcriptional repressor AgaR;
Pssm-ID: 468715 [Multi-domain] Cd Length: 256 Bit Score: 228.69 E-value: 4.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 4 AERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYT--VDRPVNEKEKMQSSEKNR 81
Cdd:NF040755 5 SERREQIIQRLRQQGSVQVEDLSALFGVSTVTIRNDLAFLEKQGIAVRAYGGALINDGFIpgAEPSVEDKSRLNTAVKRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 82 IGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVL 161
Cdd:NF040755 85 IAAAAAELIKPGDRVILDSGTTTYEIARHLKQHQDVVVMTNGLNVANELLEAEGVEVLMTGGHLRRQSLSFYGDQAEQSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 162 QDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMIN 241
Cdd:NF040755 165 QNYHFDKLFLGVDGFDLERGITTHNEDEARLNRRMCEVAERIIAVTDSSKFGRSSLHKIRDTGRIDTLITDSGIPEEYLQ 244
|
250
....*....|..
gi 2536568968 242 HLEGLGVTVTVV 253
Cdd:NF040755 245 GLRKLGVEVILV 256
|
|
| srlR |
PRK10434 |
DNA-binding transcriptional repressor; |
1-253 |
6.68e-63 |
|
DNA-binding transcriptional repressor;
Pssm-ID: 182457 [Multi-domain] Cd Length: 256 Bit Score: 197.60 E-value: 6.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLsNPYTVDRPVNEKEKMQSSEKN 80
Cdd:PRK10434 1 MKPRQRQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLVILEHAGTVIRTYGGVVL-NKEESDPPIDHKTLINTHKKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 81 RIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFL-RNPEVEVIQLGGLLRKSSSSVMGSYAEQ 159
Cdd:PRK10434 80 LIAEAAVSLIHDGDSIILDAGSTVLQMVPLLSRFNNITVMTNSLHIVNALSeLDNEQTILMPGGTFRKKSASFHGQLAEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 160 VLQDFYFNTLFLGVDGIDLEHGFTTTNamEAH-LNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQ 238
Cdd:PRK10434 160 AFEHFTFDKLFIGTDGIDLNAGVTTFN--EVYtVSKAMCNAAREIILMADSSKFGRKSPNVVCSLEKVDKLITDAGIDPA 237
|
250
....*....|....*
gi 2536568968 239 MINHLEGLGVTVTVV 253
Cdd:PRK10434 238 FRQALEEKGIEVIIT 252
|
|
| DeoRC |
pfam00455 |
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive ... |
75-233 |
2.19e-62 |
|
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: 192.73 E-value: 2.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 75 QSSEKNRIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMG 154
Cdd:pfam00455 2 NAEEKRRIAKAAASLIEDGDTIFLDAGTTTLELARALPDRRNLTVITNSLNIANELSEKPDIEVILLGGEVRPKTGAFVG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536568968 155 SYAEQVLQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDK 233
Cdd:pfam00455 82 PLAEEFLRQFNVDKAFIGANGIDLEGGLTTSDEEEAEVKRAMIEAARRVILLADSSKFGKRAFARFAPLEDIDALITDK 160
|
|
| PRK09802 |
PRK09802 |
DeoR family transcriptional regulator; |
4-253 |
7.61e-62 |
|
DeoR family transcriptional regulator;
Pssm-ID: 182086 [Multi-domain] Cd Length: 269 Bit Score: 195.46 E-value: 7.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 4 AERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATL--SNPYTVDRPVNEKEKMQSSEKNR 81
Cdd:PRK09802 16 SERREQIIQRLRQQGSVQVNDLSALYGVSTVTIRNDLAFLEKQGIAVRAYGGALIcdSTTPSVEPSVEDKSALNTAMKRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 82 IGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVL 161
Cdd:PRK09802 96 VAKAAVELIQPGHRVILDSGTTTFEIARLMRKHTDVIAMTNGMNVANALLEAEGVELLMTGGHLRRQSQSFYGDQAEQSL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 162 QDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMIN 241
Cdd:PRK09802 176 QNYHFDMLFLGVDAIDLERGVSTHNEDEARLNRRMCEVAERIIVVTDSSKFNRSSLHKIIDTQRIDMIIVDEGIPADSLE 255
|
250
....*....|..
gi 2536568968 242 HLEGLGVTVTVV 253
Cdd:PRK09802 256 GLRKAGVEVILV 267
|
|
| trans_reg_YciT |
NF040887 |
DNA-binding transcriptional regulator YciT; Involved in osmolarity control regulation |
6-253 |
5.33e-40 |
|
DNA-binding transcriptional regulator YciT; Involved in osmolarity control regulation
Pssm-ID: 468823 [Multi-domain] Cd Length: 246 Bit Score: 138.47 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 6 RHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYTVDrpvnekEKMQS--SEKNRIG 83
Cdd:NF040887 4 RQQQILQLVNDRGRVSVSELAQLTGVSEVTIRQDLNLLEKQSYLKRVHGSAVALDSDDVD------TRMMTnfPLKQKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 84 AAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISiEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVLQD 163
Cdd:NF040887 78 EYAASLVEDGETVFIEGGSTNALLARYLAERKDITIITVSHYIA-HLLKDSACEVILLGGLYQKSSESVVGPLTRLCIQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 164 FYFNTLFLGVDGIDLEHGFTTTNAMEAHL-NRQMIKVSQKVVvLADSTKFGK---RGFGKICGFEDVdyiITDKGISQQM 239
Cdd:NF040887 157 VHFSKAFIGIDGWHPETGFTGRDMMRADVvNAVLAKGAENIV-LTDSSKFGQihpYPLGPLHQFSRV---ITDDGLPADY 232
|
250
....*....|....
gi 2536568968 240 INHLEGLGVTVTVV 253
Cdd:NF040887 233 RQQLEEQGIRVDLV 246
|
|
| PRK10906 |
PRK10906 |
DeoR/GlpR family transcriptional regulator; |
1-233 |
2.63e-31 |
|
DeoR/GlpR family transcriptional regulator;
Pssm-ID: 182827 [Multi-domain] Cd Length: 252 Bit Score: 116.11 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPyTVDRPVNEKEKMQSSEKN 80
Cdd:PRK10906 1 MKQTQRHDAIIELVKQQGYVSTEELVEHFSVSPQTIRRDLNDLAEQNKILRHHGGAALPSS-SVNTPWHDRKATQTEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 81 RIGAAAAKLLKENDSIVVASGTTLLYFVKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQV 160
Cdd:PRK10906 80 RIARKVASQIPNGATLFIDIGTTPEAVAHALLNHSNLRIVTNNLNVANTLMAKEDFRIILAGGELRSRDGGIIGEATLDF 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 161 LQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDK 233
Cdd:PRK10906 160 ISQFRLDFGILGISGIDSDGSLLEFDYHEVRTKRAIIENSRHVMLVVDHSKFGRNAMVNMGSISMVDAVYTDQ 232
|
|
| PRK13509 |
PRK13509 |
HTH-type transcriptional regulator UlaR; |
1-253 |
1.46e-30 |
|
HTH-type transcriptional regulator UlaR;
Pssm-ID: 184100 [Multi-domain] Cd Length: 251 Bit Score: 113.95 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 1 MTLAERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGA-TLSNPYTVDRPVNEKEKMQSSEK 79
Cdd:PRK13509 1 MTEAQRHQILLELLAQLGFVTVEKVIERLGISPATARRDINKLDESGKLKKVRNGAeAITQQRPRWTPMNIHQAQNHDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 80 NRIGAAAAKLLKENDSIVVASGTTLLYFVKSIPnGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSsVMGSYAEQ 159
Cdd:PRK13509 81 VRIAKAASQLCNPGESVVINCGSTAFLLGRELC-GKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQS-ITLSPQGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 160 VLQDFYFNTLFLGVDGIDLEhGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQM 239
Cdd:PRK13509 159 ENSLYAGHWMFTSGKGLTAD-GLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKIGERAGMLFSRADQIDMLITGKNADPEV 237
|
250
....*....|....
gi 2536568968 240 INHLEGLGVTVTVV 253
Cdd:PRK13509 238 LQQLEAQGVSILLV 251
|
|
| PRK10681 |
PRK10681 |
DNA-binding transcriptional repressor DeoR; Provisional |
29-250 |
5.03e-22 |
|
DNA-binding transcriptional repressor DeoR; Provisional
Pssm-ID: 182644 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 29 LKVSSVTIRKDLKLLEDKHLLFrthGGATLSNPYTVDRP-VNEKEKMQSSEKNRIGAAAAKLLKENDSIVVASGTTLLYF 107
Cdd:PRK10681 31 LGVSEMTIRRDLNAHSAPVVLL---GGYIVLEPRSASHYlLSDQKSRLVEEKRRAAQLAATLVEPNQTLFFDCGTTTPWI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 108 VKSIPNGLNLTVVTSSLNISIEFLRNPEVEVIQLGGLLRKSSSSVMGSYAEQVLQDFYFNTLFLGVDGIDLEHGFTTTNA 187
Cdd:PRK10681 108 IEAIDNELPFTAVCYSLNTFLALQEKPHCRAILCGGEFHASNAIFKPLDFQQTLDNICPDIAFYSAAGVHVSKGATCFNL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 188 MEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDKGISQQMINHLEGLGVTV 250
Cdd:PRK10681 188 EELPVKHWAMAMAQKHVLVVDHSKFGKVRPARMGDLTRFDTVVSDRCPDDEFVKYAQAQRIKL 250
|
|
| PRK10411 |
PRK10411 |
L-fucose operon activator; |
4-233 |
1.98e-17 |
|
L-fucose operon activator;
Pssm-ID: 236684 [Multi-domain] Cd Length: 240 Bit Score: 78.69 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 4 AERHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNPYTVDR--PVNEKEKMQSSEKNR 81
Cdd:PRK10411 3 AARQQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNHGRAKYIHRQNQDSgdPFHIRLKSHYAHKAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 82 IGAAAAKLLKENDSIVVASGTTLLYFVKSIPNgLNLTVVTSSLNISIEFLRNPEVEVIQLGGLL-RKSSSSVMGSYAEQv 160
Cdd:PRK10411 83 IAREALAWIEEGMVIALDASSTCWYLARQLPD-INIQVFTNSHPICQELGKRERIQLISSGGTLeRKYGCYVNPSLISQ- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 161 LQDFYFNTLFLGVDGIDLEHGFTTTNAMEAHLNRQMIKVSQKVVVLADSTKFGKRGFGKICGFEDVDYIITDK 233
Cdd:PRK10411 161 LKSLEIDLFIFSCEGIDSSGALWDSNAINADYKSMLLKRAAQSLLLIDKSKFNRSGEARIGHLDEVTHIISDE 233
|
|
| HTH_DEOR |
smart00420 |
helix_turn_helix, Deoxyribose operon repressor; |
6-58 |
8.59e-13 |
|
helix_turn_helix, Deoxyribose operon repressor;
Pssm-ID: 197714 [Multi-domain] Cd Length: 53 Bit Score: 61.47 E-value: 8.59e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 6 RHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATL 58
Cdd:smart00420 1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLTRVHGGAVS 53
|
|
| HTH_DeoR |
pfam08220 |
DeoR-like helix-turn-helix domain; |
6-61 |
8.88e-12 |
|
DeoR-like helix-turn-helix domain;
Pssm-ID: 285436 [Multi-domain] Cd Length: 57 Bit Score: 58.81 E-value: 8.88e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2536568968 6 RHQFILNRIQQDQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGATLSNP 61
Cdd:pfam08220 1 RIQQILELLKQQGTLSVEELAELLGVSEMTIRRDLNELEEQGLLTRTHGGAVSNSS 56
|
|
| MngR |
COG2188 |
DNA-binding transcriptional regulator, GntR family [Transcription]; |
8-54 |
8.01e-05 |
|
DNA-binding transcriptional regulator, GntR family [Transcription];
Pssm-ID: 441791 [Multi-domain] Cd Length: 238 Bit Score: 42.54 E-value: 8.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 8 QFILNRIQQDQYI------NVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHG 54
Cdd:COG2188 12 DALRERIESGELPpgdrlpSERELAEEFGVSRMTVRKALDELVEEGLLERRQG 64
|
|
| hrcA |
TIGR00331 |
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; ... |
5-145 |
8.11e-05 |
|
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; overproduction prevents induction of these operons by heat shock while deletion allows constitutive expression even at low temperatures. In Bacillus subtilis, hrcA is the first gene of the dnaK operon and so is itself a heat shock gene. [Regulatory functions, DNA interactions]
Pssm-ID: 273017 [Multi-domain] Cd Length: 337 Bit Score: 43.04 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 5 ERHQFILNRIQQDqYIN---------VVELCkQLKVSSVTIRKDLKLLEDKHLLFRTH--GG---ATLSNPYTVDRPVnE 70
Cdd:TIGR00331 2 ERQRKILKAIVEE-YIKtgqpvgsktLLEKY-NLGLSSATIRNDMADLEDLGFIEKPHtsSGripTDKGYRYYVDHLL-K 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536568968 71 KEKMQSSEKNRIGAAAAKLLKENDSIvvasgttLLYFVKSIPNGLNLTVVTSSLNISIEFLRNpeVEVIQLGGLL 145
Cdd:TIGR00331 79 VDSLTEEEKRRIQNQFLQRRFYLEKV-------LQLAASLLSELTNYTAVVLGPRLSQDKLKH--IELIPLDPNL 144
|
|
| WHTH_GntR |
cd07377 |
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ... |
10-57 |
1.05e-04 |
|
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: 39.35 E-value: 1.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2536568968 10 ILNRIQQDQY------INVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGAT 57
Cdd:cd07377 10 LREAILSGELkpgdrlPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGT 63
|
|
| HTH_GNTR |
smart00345 |
helix_turn_helix gluconate operon transcriptional repressor; |
10-57 |
6.65e-04 |
|
helix_turn_helix gluconate operon transcriptional repressor;
Pssm-ID: 197669 [Multi-domain] Cd Length: 60 Bit Score: 37.17 E-value: 6.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2536568968 10 ILNRIQQ------DQYINVVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGAT 57
Cdd:smart00345 5 LREDIVSgelrpgDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGT 58
|
|
| PRK13029 |
PRK13029 |
indolepyruvate ferredoxin oxidoreductase family protein; |
80-172 |
2.78e-03 |
|
indolepyruvate ferredoxin oxidoreductase family protein;
Pssm-ID: 237278 [Multi-domain] Cd Length: 1186 Bit Score: 39.00 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536568968 80 NRIGAAAAKLLKENDSIVVASGTTLlyfvKSIPNGLNLTVVTSSLNISIEFLRNPE--VEVIQLGGLLRKSS--SSVMGS 155
Cdd:PRK13029 806 TRIDTGEADLVIACDLVVAASGEAL----AAMRPGRTRAAANSHETPTAAFVRNPDwsFPVDQTVALLRDSIgaDQCAFF 881
|
90 100
....*....|....*....|..
gi 2536568968 156 YAEQVL-----QDFYFNTLFLG 172
Cdd:PRK13029 882 DANALAlallgDSIYANPLLLG 903
|
|
| LexA |
COG1974 |
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ... |
1-56 |
3.44e-03 |
|
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];
Pssm-ID: 441577 [Multi-domain] Cd Length: 199 Bit Score: 37.59 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536568968 1 MTLAERHQFILNRIQQdqYIN-------VVELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGA 56
Cdd:COG1974 2 KKLTKRQREILDFIKE--YIRergyppsQREIAEALGLSSSAVHRHLKALEKKGYLRRDPGKS 62
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
14-46 |
6.04e-03 |
|
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: 33.95 E-value: 6.04e-03
10 20 30
....*....|....*....|....*....|...
gi 2536568968 14 IQQDQYINVVELCKQLKVSSVTIRKDLKLLEDK 46
Cdd:pfam08279 8 LEARGPISGQELAEKLGVSRRTIRRDIKILEEL 40
|
|
| GntR |
pfam00392 |
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ... |
24-57 |
8.94e-03 |
|
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: 34.13 E-value: 8.94e-03
10 20 30
....*....|....*....|....*....|....
gi 2536568968 24 ELCKQLKVSSVTIRKDLKLLEDKHLLFRTHGGAT 57
Cdd:pfam00392 29 ELAAEFGVSRTTVREALRRLEAEGLVERRQGRGT 62
|
|
|