TSPctail specific protease
|SMART accession number:||SM00245|
|Description:||tail specific protease|
|Interpro abstract (IPR005151):|
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 [(PUBMED:8702985)], and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in Escherichia coli [(PUBMED:1856173)].
The tricorn protease is responsible for degrading oligopeptides, probably derived from the proteasome. Its crystal structure has been resolved to 2 A resolution [(PUBMED:11719810)].
|GO process:||proteolysis (GO:0006508)|
|GO function:||serine-type peptidase activity (GO:0008236)|
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- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)