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cl02600: HTH_MerR-SF Superfamily 
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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.
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Statistics
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Accession: cl02600
PSSM Id: 261364
Name: HTH_MerR-SF
Created: 8-Feb-2008
Updated: 16-Jan-2014
Superfamily
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Curated CD Hierarchy
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cd00592:HTH_MerR-likecd01104:HTH_MlrA-CarAcd01105:HTH_GlnR-likecd01106:HTH_TipAL-Mtacd01107:HTH_BmrRcd01108:HTH_CueRcd01109:HTH_YyaNcd01110:HTH_SoxRcd01111:HTH_MerDcd01279:HTH_HspR-likecd01282:HTH_MerR-like_sg3cd04761:HTH_MerR-SFcd04762:HTH_MerR-trunccd04763:HTH_MlrA-likecd04764:HTH_MlrA-like_sg1cd04765:HTH_MlrA-like_sg2cd04766:HTH_HspRcd04767:HTH_HspR-like_MBCcd04768:HTH_BmrR-likecd04769:HTH_MerR2cd04770:HTH_HMRTRcd04772:HTH_TioE_rpt1cd04773:HTH_TioE_rpt2cd04774:HTH_YfmPcd04775:HTH_Cfa-likecd04776:HTH_GnyRcd04777:HTH_MerR-like_sg1cd04778:HTH_MerR-like_sg2cd04779:HTH_MerR-like_sg4cd04780:HTH_MerR-like_sg5cd04781:HTH_MerR-like_sg6cd04782:HTH_BltRcd04783:HTH_MerR1cd04784:HTH_CadR-PbrRcd04785:HTH_CadR-PbrR-likecd04786:HTH_MerR-like_sg7cd04787:HTH_HMRTR_unkcd04788:HTH_NolA-AlbRcd04789:HTH_Cfacd04790:HTH_Cfa-like_unk
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Imported CD
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Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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