Tail specific protease (IPR005151)

Short name: Tail-specific_protease

Overlapping homologous superfamilies


Domain relationships



This entry represents a domain found in the tail-specific proteases, such as retinol-binding protein 3 (also known as IRBP) from animals, C-terminal processing peptidases from algae and tricorn proteases from archaea. This domain share structural similarity with the crotonase fold that is formed from repeated beta/beta/alpha units, which comprises two perpendicular beta-sheet surrounded by alpha-helices.

The C-terminal processing peptidases have different substrates in different species, including processing of D1 protein of the photosystem II reaction centre in higher plants [PMID: 8702985], and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in Escherichia coli [PMID: 1856173].

The tricorn protease is responsible for degrading oligopeptides, probably derived from the proteasome. Its crystal structure has been resolved to 2 A resolution [PMID: 11719810].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0008236 serine-type peptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.