Protein Family Models

This entry describes the C-terminal domain of the uncharacterized HTH-type transcriptional regulator PF0864, identified in the Pyrococcus furiosus archaea. The protein is 162 amino acids long and contains an HTH asnC-type domain (amino acids 6-78) responsible for DNA binding. The crystal structure of PF0864 (PDB: 2IA0) reveals a helix-turn-helix motif within the DNA-binding domain. The function and specific role of PF0864 in transcriptional regulation remain unknown. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Date:

2024-08-14

The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to the usually C-terminal regulatory ligand binding domain. Structurally this domain has a dimeric alpha/beta barrel fold [2]. This domain binds almost exclusively amino acids but also 4-hydroxyphenylpyruvate and kynurenine (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 7770911. The eubacterial transcriptional activator Lrp is present in the archaeon Pyrococcus furiosus. Kyrpides NC, Ouzounis CA;. Trends Biochem Sci 1995;20:140-141. [2]. 17374605. The structure and transcriptional analysis of a global regulator from Neisseria meningitidis. Ren J, Sainsbury S, Combs SE, Capper RG, Jordan PW, Berrow NS, Stammers DK, Saunders NJ, Owens RJ;. J Biol Chem. 2007;282:14655-14664. (from Pfam)

Date:

2024-10-16

Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family transcriptional regulator regulates many cellular processes such as amino acid metabolism, pili synthesis, and DNA repair and recombination

Date:

2024-04-11