1Q05


Conserved Protein Domain Family
HTH_HMRTR

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cd04770: HTH_HMRTR 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 133398
View PSSM: cd04770
Aligned: 43 rows
Threshold Bit Score: 131.916
Threshold Setting Gi: 15893752
Created: 18-Jan-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
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        ###             #                 ###                                          
1Q05_B        1 MNISDVAKITGLTSKAIRFYEEKGLVt-pPMRSEnGYRTYTqQHLNELTLLRQARQVGFNLEESGELVNLfndpqrhSAD 79  Escherichia coli
AAB47524      2 LKIGEIAKQVGVAVGTIRYYETLQLIq-pSTRGEnGYRYYKpQTIQQLQFIRQAQTLGFSLEEIRQILTVyaegtppCSL 80  Synechococcus sp...
NP_485669     8 KQIGVVAKESGVPIKTIRYYEELGLLt-sSGRTEgGFRLFNsDVLARLHFIKRAQSLGLSLSEIKEFLNVhdggelpCEH 86  Nostoc sp. PCC 7120
ZP_01084340   1 MKIGALAIRSGLPIKTLRYYEDLGLLp-aVGRSEgGYRLFGeESLRRLDFIRRLKSLGLTLDEIQECLAVhdagelpCGD 79  Synechococcus sp...
YP_477329     5 LKIGQVALAAGLSVRTVRYYESIGLLkptVERAEsSYRLFDpSVLVRLAFIRRCQSLGLSLEEIRQILDVhdrgeqpCPE 84  Synechococcus sp...
ZP_01426163   1 MQIGQVARRCGVSVQTVRLYERMGLIe-tAQRREsGYRDYSnTVVARILAIKQGQALGFSLREMGMFLQLspq-nteQAL 78  Herpetosiphon au...
ZP_01223498   1 MKIGELANLSDVPVKSIRYYEAEGILa-sPQRLEnGYRDYSkTAVAELIFLRQSRQFGFTLHECRQLLQLwrdpnrrSAE 79  marine gamma pro...
ZP_01166749   4 LKIGQVAKQSDISVETVRYYEKRGLIp-aPQRLDsGYRVYPqSILQRLHFIQRCKDLGFSLQEIGELLNLqtdpatsSAL 82  Oceanospirillum ...
ZP_01300857   4 YTIGNLAKLVQQTPVTIRYYEKIGLIp-kSKRSEgGFRLYPeSLLRRFYFIQNAKLIGFDLNEIKNLLDLemn-qssSQP 81  Rickettsiella gr...
ZP_01348778  26 QPSSQAAQETGLSVKSIRYYEQIGLTn-pPPRGEnDYRYYPsALIKRLHFIKKTKDVGFSLKESKNLLALsensgrrSAD 104 Psychromonas ing...
Feature 1                                                                 
1Q05_B       80 VKRRTLEKVAEIERHIEELQSMRDQLLALAn----ACPGDds----------aDCPII 123 Escherichia coli
AAB47524     81 VQTLLNQKIASLEEKLQQIQTFKAQLESYRd----RWQQThpsngnevrnlsvNCNHS 134 Synechococcus sp. PCC 7942
NP_485669    87 IKIKLEDKVKAIDEQIQQLLILRQELSGLLsgweiKPDNShk----------tICPII 134 Nostoc sp. PCC 7120
ZP_01084340  80 IQRQLQRQIDLVDERLRELRLFRRELQSLLk----NWQSDpapn------tsvICPNL 127 Synechococcus sp. WH 5701
YP_477329    85 IRQHLQGKLQEIEQRIADLQALKSQIQGLLs----DWQITpaaad----ekevICPIL 134 Synechococcus sp. JA-2-3B'a(2-13)
ZP_01426163  79 IQQFVEQKVQQIDQTVQQFQRLRQALHEFA-----ARSADdl----------rECPVI 121 Herpetosiphon aurantiacus ATCC 23779
ZP_01223498  80 VHQLVIQRQRQVEEQIKDLTSMHGLLSNLLs----HCAADes----------pDCAII 123 marine gamma proteobacterium HTCC2207
ZP_01166749  83 VKEQVENKIQLVKQKIGELQKIEHSLEQLSd----LCCGDgp---------vsDCPII 127 Oceanospirillum sp. MED92
ZP_01300857  82 VKLEIQQKISQIENKIKSLQRIKHALMGWEq----ACDGNis---------iaECPIL 126 Rickettsiella grylli
ZP_01348778 105 VKALLSQKIEELQTKIKREQALLESLKNITl----KCCGDek----------pNCPII 148 Psychromonas ingrahamii 37

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