Conserved Protein Domain Family
HTH_MerR-like_sg6

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cd04781: HTH_MerR-like_sg6 
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.
Statistics
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PSSM-Id: 133408
Aligned: 15 rows
Threshold Bit Score: 151.667
Created: 13-Nov-2006
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
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        ###             #               ###                                            
NP_106052     1 MDIAEVSRRTGVPASTLRYYEEKGLVASIGRRGQRRLFDpAVLDRLALIALGRAGGFTLDDISSMLTPdg----lPKMDR 76  Mesorhizobium lo...
NP_883610     1 MDIAEVARRTGVPASTLRYYDKVGLIAPVSPPGARRRYApAVLEQLALVALGQAGGLSLDDIRAMLSPqg----aPRVDR 76  Bordetella parap...
NP_746389     1 MDIADVAKRTGVPASTLRYYEKKGLLKSLAGRGQRRQFAaDVADRLALIALGQAAGFSLDEVGAMLVD-------LQVDR 73  Pseudomonas puti...
ZP_01055237   4 LDIAEVASQSGLAPSTLRYYEKRGLITSDGRRGLRREYDdSVLMRLALISLGRRAGYSLEEIRALFRPqg---gkYDLNR 80  Roseobacter sp. ...
YP_047457     4 ITMSELARQTGLKSSAIRYYEKEKLIHPIGRKGLQRVFSiQIIDQLALIHLAKQAGFSIQEIRSMLEKp-----qSPIDK 78  Acinetobacter sp...
YP_432420     7 LDIAEVAKLSGLPASTLRYYEEKGLIKSIGREGLKRIFRsTVIDQLGLISLGQYAGFSLEEIGAMFSHdg----kPKIDR 82  Hahella chejuens...
YP_168928     4 LDIGEIAAQSGVPPSTLRYYEEQGLIAPIGRKGLRRQYGpQTLLRLTLISMGKAAGFSLPEIAQMLGAdg----rPDLPR 79  Silicibacter pom...
NP_800295     5 MDIAEVVIKSGLPTSTLRYYEQLGLIRSIGRNGLRRQYSpEVLNKLNLISLGRIAGISLNEMAEMLNHseg--skPYIDR 82  Vibrio parahaemo...
ZP_00959919   4 LDIGEVAEATGLRVSALRYYEEKGLIEALGRKGLRRQYGpEVLQQLALVALGRQAGFSLDEIGGMFGAgg----aPALPR 79  Roseovarius nubi...
ZP_01425669   4 LSISMVAKQAGIKASTIRYYEEINLLPPAARQNGRRYYDqQIFERLAFIRTTQRLGFSLNEIQLLFQHeqqqaplAGLWR 83  Herpetosiphon au...
Feature 1                                                   
NP_106052    77 GRLDAKANELDQIIQRLRAIRKALRHAAKCPAArpMECPTFCRA 120 Mesorhizobium loti MAFF303099
NP_883610    77 QVLLAKAEEIDATVKQLQAMSRGLRHAAACPAPshAQCPTFRRL 120 Bordetella parapertussis 12822
NP_746389    74 QMLMAKADELDARIKRLQAMSKGLRHAAQCPEKdhLACPKFQQL 117 Pseudomonas putida KT2440
ZP_01055237  81 QELRSQANTLRRQAQELCATAELLDHIAACTAPsyLECPRFQDI 124 Roseobacter sp. MED193
YP_047457    79 NQLKQKALQIEEKIVEMKVLSKTLRHVAQCSFDnpLNCPKFQKI 122 Acinetobacter sp. ADP1
YP_432420    83 AQLIEKASELDQLIQRMETMRDSIIHVANCPEPnqLECPRFQTL 126 Hahella chejuensis KCTC 2396
YP_168928    80 DELHARADDLGRQIRRLQLLQETLRHVADCPAPshLDCPSFQKL 123 Silicibacter pomeroyi DSS-3
NP_800295    83 DLLAKKALEIDEQITRLKAVRDSLNHVASCPHEshMDCSSFQRL 126 Vibrio parahaemolyticus RIMD 2210633
ZP_00959919  80 AELKTRAAAMRDQARQLEALAQMLGHVADCPEPnhLDCPKFQQL 123 Roseovarius nubinhibens ISM
ZP_01425669  84 QLAKQKLADLSQLLEQASHVQQLLQRGLRCRCAtlEMCVHCVLQ 127 Herpetosiphon aurantiacus ATCC 23779

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