MULTISPECIES: MerR family transcriptional regulator [Rhizobium/Agrobacterium group]
Protein Classification
MerR family transcriptional regulator( domain architecture ID 10140925)
MerR family transcriptional regulator activates transcription through protein-dependent DNA distortion and the majority of regulators in the family respond to environmental stimuli, such as oxidative stress, heavy metals or antibiotics; similar to Rhodobacter capsulatus HTH-type transcriptional regulator in himA 3'region
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HTH_MlrA-like_sg2 | cd04765 | Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ... |
11-86 | 7.17e-43 | ||
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. : Pssm-ID: 133393 Cd Length: 99 Bit Score: 138.54 E-value: 7.17e-43
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| HTH_MlrA-like_sg2 | cd04765 | Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ... |
11-86 | 7.17e-43 | ||
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133393 Cd Length: 99 Bit Score: 138.54 E-value: 7.17e-43
|
||||||
| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
12-78 | 1.53e-21 | ||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 82.99 E-value: 1.53e-21
|
||||||
| SoxR | COG0789 | DNA-binding transcriptional regulator, MerR family [Transcription]; |
13-79 | 2.10e-15 | ||
DNA-binding transcriptional regulator, MerR family [Transcription]; Pssm-ID: 440552 [Multi-domain] Cd Length: 100 Bit Score: 68.01 E-value: 2.10e-15
|
||||||
| HTH_MERR | smart00422 | helix_turn_helix, mercury resistance; |
12-79 | 8.38e-09 | ||
helix_turn_helix, mercury resistance; Pssm-ID: 197716 Cd Length: 70 Bit Score: 49.83 E-value: 8.38e-09
|
||||||
| PRK15043 | PRK15043 | HTH-type transcriptional regulator MlrA; |
9-78 | 5.31e-06 | ||
HTH-type transcriptional regulator MlrA; Pssm-ID: 185003 [Multi-domain] Cd Length: 243 Bit Score: 45.31 E-value: 5.31e-06
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| HTH_MlrA-like_sg2 | cd04765 | Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ... |
11-86 | 7.17e-43 | ||
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133393 Cd Length: 99 Bit Score: 138.54 E-value: 7.17e-43
|
||||||
| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
12-78 | 1.53e-21 | ||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 82.99 E-value: 1.53e-21
|
||||||
| HTH_MlrA-like | cd04763 | Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix ... |
12-79 | 3.01e-17 | ||
Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A) and related proteins, N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins. Pssm-ID: 133391 Cd Length: 68 Bit Score: 72.18 E-value: 3.01e-17
|
||||||
| SoxR | COG0789 | DNA-binding transcriptional regulator, MerR family [Transcription]; |
13-79 | 2.10e-15 | ||
DNA-binding transcriptional regulator, MerR family [Transcription]; Pssm-ID: 440552 [Multi-domain] Cd Length: 100 Bit Score: 68.01 E-value: 2.10e-15
|
||||||
| HTH_MlrA-like_sg1 | cd04764 | Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative ... |
12-79 | 9.91e-12 | ||
Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators; Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 1). The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins. Pssm-ID: 133392 Cd Length: 67 Bit Score: 57.73 E-value: 9.91e-12
|
||||||
| HTH_MlrA-CarA | cd01104 | Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; ... |
12-79 | 7.14e-11 | ||
Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA- and CarA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins. Pssm-ID: 133379 Cd Length: 68 Bit Score: 55.32 E-value: 7.14e-11
|
||||||
| HTH_MerR-SF | cd04761 | Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ... |
12-60 | 3.73e-10 | ||
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133389 [Multi-domain] Cd Length: 49 Bit Score: 52.98 E-value: 3.73e-10
|
||||||
| HTH_MerR-like | cd00592 | Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix ... |
12-79 | 1.16e-09 | ||
Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators; Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133378 [Multi-domain] Cd Length: 100 Bit Score: 53.02 E-value: 1.16e-09
|
||||||
| HTH_MERR | smart00422 | helix_turn_helix, mercury resistance; |
12-79 | 8.38e-09 | ||
helix_turn_helix, mercury resistance; Pssm-ID: 197716 Cd Length: 70 Bit Score: 49.83 E-value: 8.38e-09
|
||||||
| HTH_YyaN | cd01109 | Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; ... |
12-63 | 3.27e-08 | ||
Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133384 [Multi-domain] Cd Length: 113 Bit Score: 49.38 E-value: 3.27e-08
|
||||||
| HTH_GlnR-like | cd01105 | Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix ... |
12-84 | 4.02e-08 | ||
Helix-Turn-Helix DNA binding domain of GlnR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator GlnR and related proteins, N-terminal domain. The GlnR and TnrA (also known as ScgR) proteins have been shown to regulate expression of glutamine synthetase as well as several genes involved in nitrogen metabolism. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133380 Cd Length: 88 Bit Score: 48.77 E-value: 4.02e-08
|
||||||
| HTH_HspR-like_MBC | cd04767 | Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators; Putative ... |
13-78 | 9.44e-07 | ||
Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators; Putative helix-turn-helix (HTH) transcription regulator HspR-like proteins. Unlike the characterized HspR, these proteins have a C-terminal domain with putative metal binding cysteines (MBC). Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133395 Cd Length: 120 Bit Score: 45.56 E-value: 9.44e-07
|
||||||
| HTH_HspR-like | cd01279 | Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix ... |
13-78 | 1.09e-06 | ||
Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix (HTH) transcription regulator HspR and related proteins, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133387 Cd Length: 98 Bit Score: 44.90 E-value: 1.09e-06
|
||||||
| PRK15043 | PRK15043 | HTH-type transcriptional regulator MlrA; |
9-78 | 5.31e-06 | ||
HTH-type transcriptional regulator MlrA; Pssm-ID: 185003 [Multi-domain] Cd Length: 243 Bit Score: 45.31 E-value: 5.31e-06
|
||||||
| MerR | pfam00376 | MerR family regulatory protein; |
12-49 | 1.19e-04 | ||
MerR family regulatory protein; Pssm-ID: 425647 [Multi-domain] Cd Length: 38 Bit Score: 37.78 E-value: 1.19e-04
|
||||||
| HTH_MerR-like_sg6 | cd04781 | Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR ... |
12-78 | 7.05e-04 | ||
Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 6) with at least two conserved cysteines present in the C-terminal portion of the protein. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133408 Cd Length: 120 Bit Score: 37.65 E-value: 7.05e-04
|
||||||
| HTH_HMRTR | cd04770 | Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; ... |
12-62 | 7.56e-03 | ||
Helix-Turn-Helix DNA binding domain of Heavy Metal Resistance transcription regulators; Helix-turn-helix (HTH) heavy metal resistance transcription regulators (HMRTR): MerR1 (mercury), CueR (copper), CadR (cadmium), PbrR (lead), ZntR (zinc), and other related proteins. These transcription regulators mediate responses to heavy metal stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates. Pssm-ID: 133398 [Multi-domain] Cd Length: 123 Bit Score: 34.85 E-value: 7.56e-03
|
||||||
| HTH_YfmP | cd04774 | Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) ... |
12-80 | 8.84e-03 | ||
Helix-Turn-Helix DNA binding domain of the YfmP transcription regulator; Helix-turn-helix (HTH) transcription regulator, YfmP, and related proteins; N-terminal domain. YfmP regulates the multidrug efflux protein, YfmO, and indirectly regulates the expression of the Bacillus subtilis copZA operon encoding a metallochaperone, CopZ, and a CPx-type ATPase efflux protein, CopA. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Pssm-ID: 133401 [Multi-domain] Cd Length: 96 Bit Score: 34.41 E-value: 8.84e-03
|
||||||
| HTH_TioE_rpt2 | cd04773 | Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative ... |
11-80 | 9.23e-03 | ||
Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD mainly contains the C-terminal or second repeat (rpt2) of these tandem MerR-like domain proteins. Pssm-ID: 133400 Cd Length: 108 Bit Score: 34.26 E-value: 9.23e-03
|
||||||
| Blast search parameters | ||||
|
