Protein Family Models

The N-terminal domain of tail specific proteases has a novel fold composed of 10 alpha helices [1]. [1]. 25349155. Structural basis of the proteolytic and chaperone activity of Chlamydia trachomatis CT441. Kohlmann F, Shima K, Hilgenfeld R, Solbach W, Rupp J, Hansen G;. J Bacteriol. 2015;197:211-218. (from Pfam)

Date:

2024-10-16

This presumed domain is found at the C-terminus of tail specific proteases. Its function is unknown. This family is found in bacteria and eukaryotes. This presumed domain is typically between 88 to 187 amino acids in length. (from Pfam)

Date:

2024-08-14

The serine endopeptidases in this family include C-terminal processing proteases such as the periplasmic protease Prc from Escherichia coli, involved in processing penicillin-binding protein (PBP) 3, and carboxyl-terminal processing protease CtpA from Pseudomonas aeruginosa.

Date:

2024-08-14

PDZ domains are found in diverse signaling proteins. Review article. [1]. 9204764. PDZ domains: targeting signalling molecules to sub-membranous sites. Ponting CP, Phillips C, Davies KE, Blake DJ. Bioessays 1997;19:469-479. [2]. 8674113. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R;. Cell. 1996;85:1067-1076. Extension of PDZ family. [3]. 9041651. Evidence for PDZ domains in bacteria, yeast, and plants. Ponting CP;. Protein Sci 1997;6:464-468. [4]. 19738200. Rapid evolution of functional complexity in a domain family. Ernst A, Sazinsky SL, Hui S, Currell B, Dharsee M, Seshagiri S, Bader GD, Sidhu SS;. Sci Signal. 2009;2:ra50. (from Pfam)

Date:

2024-10-16

Carboxy-terminal processing proteases (EC 3.4.21.102) have paralogs in some species, and different gene symbols in different lineages, such as prc in Escherichia coli K-12, ctpA, ctpB, and ctpC in Synechocystis sp. PCC 6803, and cptA and ctpB in Bacillus subtilis.

Date:

2023-10-20