Protein Family Models

Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins. (from Pfam)

Date:

2024-08-14

This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses. (from Pfam)

Date:

2024-08-14

This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins. (from Pfam)

Date:

2024-08-14

This model represents a C-terminal domain associated with secretion by type 1 secretion systems (T1SS). Members of this subclass do not include the RtxA toxin of Vibrio cholerae and its homologs, although the two classes of proteins share large size, occurrence in genomes with T1SS, regions with long tandem repeats, and regions with the glycine-rich repeat modeled by PF00353.

Date:

2021-10-27

This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.

Date:

2020-10-26

This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.

Date:

2020-10-26