The domain within your query sequence starts at position 109 and ends at position 308; the E-value for the TSPc domain shown below is 5.72e-69.
WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 21576514 ) for details.
Catalytic residues | |||
---|---|---|---|
Position | Amino acid | Present? | |
Domain | Protein | ||
129 | 237 | S | No |
TREELLAQIQRNIRHEVLEGNVGYLRVDDLPGQEVLSELGEFLVSHVWRQLMSTSSLVLD
LRHCSGGHFSGIPYVISYLHPGNTVMHVDTVYDRPSNTTTEIWTLPEVLGERYSADKDVV
VLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLRIGQSNFFLTVPVSRSLGP
LGGGGQTWEGSGVLPCVGTP
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) |
Family alignment: |
There are 36024 TSPc domains in 35205 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)