Protein Family Models

Pair of presumed choline-binding repeats often found adjacent to Pfam:PF01473. (from Pfam)

Date:

2024-08-14

This is an N-terminal immunoglobulin (Ig)-like domain found in esterases such as EstA. Analysis of the EstA structure confirms that it is a member of the alpha/beta hydrolase family, with a conserved Ser-Asp-His catalytic triad. The Ig-like domain presumably plays a role in the multimerization of EstA into an unusual hexameric structure. Additionally, it may also participate in the catalysis of EstA by guiding the substrate to the active site [1]. [1]. 19013466. Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain. Levisson M, Sun L, Hendriks S, Swinkels P, Akveld T, Bultema JB, Barendregt A, van den Heuvel RH, Dijkstra BW, van der Oost J, Kengen SW;. J Mol Biol. 2009;385:949-962. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

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

This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by Pfam model PF01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by PF01473.

Date:

2023-11-14