The domain within your query sequence starts at position 469 and ends at position 498; the E-value for the Antistasin domain shown below is 4.5e-10.



PFAM accession number:PF02822
Interpro abstract (IPR004094):

Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. It is a potent anticoagulant by virtue of its ability to inhibit factor Xa in the coagulation cascade. Antistatin also exhibits a strong antimetastatic activity. It contains internal repeats of a 25-26 amino acid sequence with a highly conserved pattern of 6 cysteine (Cys) and 2 glycine residues [ (PUBMED:1516699) ]. Many metazoan proteins share sequence homology with this antistasin-like domain. The unique physical properties of these related Cys-rich proteins (protease resistance; heat, chemical resilience) appear to stem from the common six Cys loop that is cross-linked by three disulfide bonds [ (PUBMED:15013771) ]. Disulfide linkages are between Cys1-Cys4, Cys2-Cys5, and Cys3-Cys6 [ (PUBMED:16523290) (PUBMED:10512718) ].

The antistasin-like domain consists of very short antiparallel beta-sheets and interacts with proteinases [ (PUBMED:10512718) ].

GO function:serine-type endopeptidase inhibitor activity (GO:0004867)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Antistasin