Conserved Protein Domain Family
HTH_MerR2

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cd04769: HTH_MerR2 
Helix-Turn-Helix DNA binding domain of MerR2-like transcription regulators
Helix-turn-helix (HTH) transcription regulator MerR2 and related proteins. MerR2 in Bacillus cereus RC607 regulates resistance to organomercurials. 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 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.
Statistics
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PSSM-Id: 133397
View PSSM: cd04769
Aligned: 10 rows
Threshold Bit Score: 150.979
Threshold Setting Gi: 113968430
Created: 8-Dec-2006
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
DNA bindingputative dimer
Feature 1:DNA binding residues [nucleic acid binding site]
Evidence:
  • Comment:Based on sequence similarity to BmrR and the structure of Bacillus subtilis BmrR bound to DNA (1EXI).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        ###             #                 ###                                          
AAD25959      4 LTIGQLAQQTGVSRKAIRLYEEKELILpSIKRSEgNYRVYNqEHVFCINGIKQLRSLGVSLEEMKDLIVIFeknt-veie 82  Bacillus sp. RC607
BAA86118      4 LTIGQLAQQTGVSRKAIRLYEEKELILpSIKRTGgNYRVYNqEHVFCINGIKQLRSLGVSLEEMKDLIVIFeknt-veie 82  Clostridium buty...
AAF64139      9 MTIGELSHRTGVPIKTLREYTDTGLIY-TVGRSPaNYRLYDaDALWCVHWIGELRGLGLTVAEIRASTREClgradrsvg 87  Streptomyces sp....
ZP_00655684  11 MTVGELSRRTGVPAKNLRAYTDAGLVY-SVGRTGaNYRLYDaEALWCVAAITELRQLGLTLAEIREFGAGYlaregepig 89  Nocardioides sp....
YP_732223     1 MYIGAVAKQTGLSIKAIRLYEEWGLIS-APIRKG-RYRTYSaTDIKQLMLIKEAKTLGIKLSQLKDLFTEGeqa---aql 75  Shewanella sp. MR-4
NP_744932     1 MYIGKAAQLSGTTVKSIRHYEEIGLLP-PPQREG-KYRIYSqQSVELLTFIKCAQQLGFKLKEMQAILQDHrgqe--lpw 76  Pseudomonas puti...
ZP_00585076   7 MYIGEAARVTGLTIKAIRFYEQKGLLP-SPQRDG-RYRVYSpQHLELLRLIRDAKALGVPLTKLMAVVPAKgdt---ldw 81  Shewanella amazo...
YP_257901     1 MYIGQAAQLSGTTVKSIRHYEAIGLLP-EAPRQG-RYRLYDaQSVEQLIFIKCAQQLGFKLKELQQVFATHqgqa--fpw 76  Pseudomonas fluo...
YP_346446     1 MYIGQAAQRSGTTIKTIRHYESIGLLP-EAPRQG-KYRVYDpQTVELLSFIKCAQALGFRLRELQAIFAGQpel---tpy 75  Pseudomonas fluo...
ZP_01113919   1 MYIGEFCKQTQTTPKTIRYYESLGLLP-PAKRLG-SYRVYDdTYVETVRRIKQAQSYGFTLTELKKIFTGVdirr-glpa 77  Reinekea sp. MED297
Feature 1                                              
AAD25959     83 PHLQHLLKDKLTKIDEQINELQKLRKHIESYLDSPKEAF 121 Bacillus sp. RC607
BAA86118     83 PHLQHLLKDKLTKIDEQINELQKLRKHIESYLDSPKEAF 121 Clostridium butyricum
AAF64139     88 PHLAELLHRSRERARWRITEQQQILARIDAFEADHRADL 126 Streptomyces sp. CHR28
ZP_00655684  90 PRLAQMLERSRARVEQQIAELEEVRRRIDDFVAANRDRL 128 Nocardioides sp. JS614
YP_732223    76 ESVQQFLLNIKADFQRQISELEDKLVRLDACIDGLDTCE 114 Shewanella sp. MR-4
NP_744932    77 DLAMQAIDNKKQELMGQIQALQQVHDGLVEFELSLKDAQ 115 Pseudomonas putida KT2440
ZP_00585076  82 QQIRRFLEGIKQDIRAQQLRLEQQLATVDECLSAIDDCP 120 Shewanella amazonensis SB2B
YP_257901    77 DRAQAALAQKKRELQQQIEDLQQLQGRLELFETSLQQAR 115 Pseudomonas fluorescens Pf-5
YP_346446    76 EKARRAIADKQQEIAAQLLKLTRQQEELSALEASLEHAQ 114 Pseudomonas fluorescens PfO-1
ZP_01113919  78 DVMRRAIQEKRRAIAAQITELQQTDAALVDLEGFLKQSG 116 Reinekea sp. MED297

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