| Type: | Domain | Name: | Tail specific protease |
| Description: | 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 [], and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in Escherichia coli[].The tricorn protease is responsible for degrading oligopeptides, probably derived from the proteasome. Its crystal structure has been resolved to 2 A resolution []. | Short Name: | Tail-specific_protease |
