Protein Family Models

This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with Pfam:PF00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. (from Pfam)

Date:

2024-08-14

This family contains alpha/beta hydrolase enzymes of diverse specificity. (from Pfam)

Date:

2024-08-14

This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans (Swiss:Q54410). A member of this family (Swiss:Q6E3K7) is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterised from Propionibacterium freudenreichii [1]. [1]. 15574930. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Brede DA, Faye T, Johnsborg O, Odegard I, Nes IF, Holo H;. Appl Environ Microbiol 2004;70:7303-7310. (from Pfam)

Date:

2024-10-16

This catalytic domain is found in a very wide range of enzymes. [1]. 1409539. The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A;. Protein Eng 1992;5:197-211. (from Pfam)

Date:

2024-10-16

Members of this family alpha/beta hydrolase-fold proteins. Known members include hydrolases such as S-formylglutathione hydrolase (called esterase D in human) and the three paralogous mycolyltransferases of the Ag85 complex in Mycobacterium tuberculosis.

Date:

2024-08-14

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Date:

2024-03-26