The domain within your query sequence starts at position 416 and ends at position 616; the E-value for the TSPc domain shown below is 1.98e-63.

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
PositionAmino acidPresent?
DomainProtein
130545SNo
EEDARRALVDSVFQVSVLPGNVGYLRFDRFADAAVLETLGPYVLKQVWEPLQDTEHLIMD
LRHNPGGPSSAMPLVLSYFQGPEAGPVRLFTTYDRRTNITQEHFSHRELLGQRYGNQRGV
YLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGSLLHTCTVPLLDSPQGGLALTVPVLT
FIDNHGEAWLGGGVVPDAIVL

TSPc

tail specific protease
TSPc
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:
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There are 36024 TSPc domains in 35205 proteins in SMART's nrdb database.

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