MULTISPECIES: MerR family transcriptional regulator [Streptomyces]
Protein Classification
MerR family transcriptional regulator( domain architecture ID 323)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HTH_MerR-SF super family | cl02600 | Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ... |
23-60 | 3.46e-03 | ||
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. The actual alignment was detected with superfamily member cd04766: Pssm-ID: 470628 [Multi-domain] Cd Length: 91 Bit Score: 33.01 E-value: 3.46e-03
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| Name | Accession | Description | Interval | E-value | ||
| HTH_HspR | cd04766 | Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) ... |
23-60 | 3.46e-03 | ||
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) transcription regulator HspR, 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 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: 133394 [Multi-domain] Cd Length: 91 Bit Score: 33.01 E-value: 3.46e-03
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| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
23-60 | 3.67e-03 | ||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 32.53 E-value: 3.67e-03
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| Name | Accession | Description | Interval | E-value | ||
| HTH_HspR | cd04766 | Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) ... |
23-60 | 3.46e-03 | ||
Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) transcription regulator HspR, 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 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: 133394 [Multi-domain] Cd Length: 91 Bit Score: 33.01 E-value: 3.46e-03
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| MerR_1 | pfam13411 | MerR HTH family regulatory protein; |
23-60 | 3.67e-03 | ||
MerR HTH family regulatory protein; Pssm-ID: 463870 Cd Length: 66 Bit Score: 32.53 E-value: 3.67e-03
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| HTH_HspR-like | cd01279 | Helix-Turn-Helix DNA binding domain of HspR-like transcription regulators; Helix-turn-helix ... |
21-60 | 7.75e-03 | ||
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: 32.18 E-value: 7.75e-03
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