Conserved Protein Domain Family
ACT_TyrR

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cd04877: ACT_TyrR 
N-terminal ACT domain of the TyrR protein
ACT_TyrR: N-terminal ACT domain of the TyrR protein. The TyrR protein of Escherichia coli controls the expression of a group of transcription units (TyrR regulon) whose gene products are involved in the biosynthesis or transport of the aromatic amino acids. Binding to specific DNA sequences known as TyrR boxes, the TyrR protein can either activate or repress transcription at different sigma70 promoters. Its regulatory activity occurs in response to intracellular levels of tyrosine, phenylalanine and tryptophan. The TyrR protein consists of an N-terminal region important for transcription activation with an ATP-independent aromatic amino acid binding site (contained within the ACT domain) and is involved in dimerization; a central region with an ATP binding site, an ATP-dependent aromatic amino acid binding site and is involved in hexamerization; and a helix turn helix DNA binding C-terminal region. In solution, in the absence of cofactors or in the presence of phenylalanine alone, the TyrR protein exists as a dimer. However, in the presence of ATP and tyrosine the TyrR protein self-aggregates to form a hexamer. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153149
View PSSM: cd04877
Aligned: 11 rows
Threshold Bit Score: 99.6574
Threshold Setting Gi: 28212110
Created: 24-Aug-2005
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
putative
Feature 1:putative aromatic amino acid binding site
Evidence:
  • Comment:E. coli tyrR mutants with small deletions in the N-terminal region or with substitutions affecting residues 2-19 retain full function in repression, but can no longer activate gene expression.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                         ##                                                                 
AAG56479                1 MRLEVFCEDRLGLTRELLDLLVLRGIDLRGIEIDPi-GRIYLNFAELEFESFSSLMAEIRRIAGVTDVRTVPWMP 74  Escherichia...
YP_155113               1 MRLEITCDDRLGICQDVLQILRDHEIDLRGIEVDPk-GKIFLNFPELAFDDFRHLMPQIRRIPNIIDVKTIPYMP 74  Idiomarina ...
YP_270431               1 MRLEITCHDRVGMGQKVLGIFVEHGINVRGIELMQp-GRIFINIPSLDFSDLQTFMPQLRLLEGVGDVKTAPYMP 74  Colwellia p...
REF_goetting:CTC02531   5 IRLEITAVDRMGMTLKILDKIYELNINLTSVEVFP--NKVYVKVENIHKNKISKLIKNIYSIDGIYNIKKVELLE 77  Clostridium...
ZP_00417699             1 MRIHVTFIDRVGITQEVLALLGGRNLNLDAVEMVP--PNVYIDAPTLGPEVLEELRDALFKVRGVRAVEVVDILP 73  Azotobacter...
ZP_01113717             1 MRLYIRCEERLGICAEILDILVNHEIDLRGIEIDPs-GEIFLNFPTVEFDEFQHLMPEIRLIPGVHDVSLVPYMP 74  Reinekea sp...
ZP_01132661             1 MRLEIHCADRIGIAQEILNILVSYHVDLKGIEVDSkhCRMYVSFPPIEFEQFQKIMPSIRLIDGVEDVRTTAFMP 75  Pseudoalter...
ZP_01077171             1 MILEIHCHDRIGMASQVLDLFIPYDIDLKGIEIDRkhDRMYCAFADIAFEHLQTLMAEIRRIDGVFDVKTAMFTP 75  Marinomonas...
ZP_01450872             1 MRLEISCQDRLGIAQDVLELLKAHEIDLRGIEINEa-GKIYLSFPTIEFTDFQQFMPKIRRIEGIDDVKTTLFMP 74  alpha prote...
ZP_01598484             1 MRLEIQCEDRIGMVREALDLFIPHGIDMRLVEVDTkrRCIYCGFSDIPFSKLQQLLADIRRLDSVEDVKTVMFTP 75  Marinomonas...
ZP_01074444             1 MQLAIACTDRTGIAQDVLDILAHQDIDLTGIEINHeqGGFFLSTEQVALASMQTVMAEIRKVEGVKDVKTTSYLP 75  Marinomonas...

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