Conserved Protein Domain Family
HTH_Cfa-like_unk

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cd04790: HTH_Cfa-like_unk 
Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators
Putative helix-turn-helix (HTH) MerR-like transcription regulator; conserved, Cfa-like, unknown proteins (~172 a.a.). The N-terminal domain of these proteins appears to be related to the HTH domain of Cfa, a cyclopropane fatty acid synthase. These Cfa-like proteins have a unique C-terminal domain with conserved histidines (motif HXXFX7HXXF). Based on sequence similarity of the N-terminal domains, 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 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: 133417
View PSSM: cd04790
Aligned: 7 rows
Threshold Bit Score: 257.359
Threshold Setting Gi: 84387134
Created: 1-Feb-2007
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         ###             #                ###                                          
YP_437552     1 MYTIGQMSRKFGVSRSTLLYYDSIGLLsPSARSEaNYRLYSeADLSRMEKIVFYREAGLPLENIAGVLAqphd-gvqAIL 79  Hahella chejuens...
YP_589343     1 MHTVSQLAKHCQLSRSTVLYYESIGLLqPAVRTEsNYRLYGeRELQRLEQIKLYRSVGVSVKDIRAVLNaprg-efsGVL 79  Acidobacteria ba...
NP_953823     1 MYRIGQLARQFGLSRSTLLYYDRIGLLsPSGRSEsNYRRYSpADRDRLETICSLRRAGVDIRGIQAILAsagd-gatDVL 79  Geobacter sulfur...
ZP_01165346   1 MYTISQLAKQMNLSRSSLIYYDKIDLLkPSCRSSsNYRLYSeQDKVKLEQINQFRAAGLSLEAIKQLLQqnns-sagLFL 79  Oceanospirillum ...
ZP_00990156   1 MLSIKQFCEQLEVSRTTVLYYERKGLItPAARTPnGYRQYGeRELERFRAILAYRSYGIPVSEIESLLQqsqdedrdVVL 80  Vibrio splendidu...
ZP_01221331   1 MLTVSQLAKMYQISRTTILYYERAGLLlPTSRSDnGYRWYGkNEMKRLEAIIAYRSYGVSITNIAPLLErqddmpqeHIL 80  Photobacterium p...
YP_822817     2 TLTVTRLARECKLSRSTVLYYESIGLLrRPRRSDgNYRVYGdRDVERLRQICVYRDAGLALADIRSVLDtpps-daaSVL 80  Solibacter usita...
Feature 1                                                                                       
YP_437552    80 EQRLQSINREIQRLRAQQQVIATILKservr-kksriIDKQGWVAMLAAVGLDEAAMRQWHVEFESMSPEAHQDFLESLG 158 Hahella chejuens...
YP_589343    80 KRRLSQLEKEIEALQAHQRVILKLLNmktlr--rkkdMTKDKWVAVMKDAGFTEDDMHRWHRQFEKSAPTDHQEFLQFLN 157 Acidobacteria ba...
NP_953823    80 HRRLLEINREIGALQMKQRMLAGMLRlkgeg-gprtaVDKEMFVAMLRAAGMDDAAMKRLHTEFEQHSPEAHHQFLLSLG 158 Geobacter sulfur...
ZP_01165346  80 EQRLEQINHEICQLRSQQQQIVNLLGqttll-pstrlVNKAQWVEMLEASGMDEADMRQWHIEFERKLPEAHTDFLQSLG 158 Oceanospirillum ...
ZP_00990156  81 RQQFAALDLEIQKLRQQQQSIMALLKepelr--nqglLTKERWTEILKESGMDEQGMINWHKRFEQMEPLGHLKFLQSLN 158 Vibrio splendidu...
ZP_01221331  81 CEQFNSLEQEIQRLRQQKKAIVTLLEqptll--eqnkLTKAAWVEIMKSAGLNEQDMKNWHIQFEKMEPEAHQEFLESLS 158 Photobacterium p...
YP_822817    81 RRRMAELSVGIERMREHQRAIARLLKgagklskekdmVTKQKWTAIMSAAGFSEDDMRRWHREFEKSAPAEHQEFLEFLH 160 Solibacter usita...
Feature 1                     
YP_437552   159 IPAEEIKTIRHWSR 172 Hahella chejuensis KCTC 2396
YP_589343   158 IPTDEISRIREWSK 171 Acidobacteria bacterium Ellin345
NP_953823   159 IPEHEALSIRAWSA 172 Geobacter sulfurreducens PCA
ZP_01165346 159 IPEQEIEIIKSWAK 172 Oceanospirillum sp. MED92
ZP_00990156 159 IDEDEIEQIRAWSR 172 Vibrio splendidus 12B01
ZP_01221331 159 IDTEEINRIRHWSK 172 Photobacterium profundum 3TCK
YP_822817   161 IPPDEIKTIRAWSA 174 Solibacter usitatus Ellin6076

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