Protein Family Models

This domain is found as tandem repeats in bacterial cell surface proteins, associated with TED adhesive domains. This domain contains a conserved lysine, glutamic acid and asparagine diagnostic of an intradomain isopeptide bond. (from Pfam)

Date:

2024-08-14

This HMM described a domain that is often repeated in pilins such as SpaA, and that often forms isopeptide bonds cross-linking amino acid side chains, giving the pilins added strength.

Date:

2024-08-14

This HMM describes a domain commonly found in surface-anchored bacterial proteins such as adhesins, in which a thioester bond forms between a conserved Cys and a conserved Gln.

Date:

2024-08-14

This HMM describes a domain of about 40 residues with an invariant TQ dipeptide in an almost invariant TQxA[VI]W motif. This domain occurs in surface-expressed proteins of Gram-positive bacteria, many of which are involved in adhesion and anchored by LPXTG-containing sortase target domains. Numerous members of this family have domains PF05738 (Cna protein B-type domain) and PF08341 (fibronectin-binding protein signal sequence). The Q in the motif becomes part of an unusual Cys-Gln thioester crosslink.

Date:

2019-11-20

Date:

2020-10-26

This model describes a conserved region, fairly rich in insertions and deletions, located just past the signal peptide region in long, variable, and typically highly repetitive and sortase-dependent surface proteins. Members are found in a broad range of taxa, including many strains of Streptococcus pneumoniae. A conserved Cys forms a thioester bond, often to a host protein for covalent attachment.

Date:

2022-03-28