PROSITE documentation PDOC51548
Birnavirus VP4 protease domain profile


Viruses of the Birnaviridae family [E1] infect animal species belonging to vertebrates, mollusks, insects and rotifers and are characterized by their bi-segmented double-stranded RNA genome (segments A and B). Segment A encodes two overlapping reading frames and the larger open reading frame encodes a polyprotein (NH2-pVP2-VP4-VP3-COOH). The polyprotein is processed through the proteolytic activity of VP4 to generate pVP2 and VP3. During virus assembly pVP2 is further processed by VP4 to generate the capsid protein VP2 and structural peptides. Evolutionarily, the VP4 protease of the Birnaviridae family belongs to clan SJ and family S50 [E2] [1,2,3].

The birnavirus VP4 protease domain displays a catalytic serine/lysine dyad in its active site. The birnavirus VP4 protease domain has an α/β fold (see <PDB:2PNL>) [2,3].

The profile we developed covers the entire birnavirus VP4 protease domain.

Last update:

September 2011 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

BIRNAVIRUS_VP4_PRO, PS51548; Birnavirus VP4 protease domain profile  (MATRIX)


1AuthorsPetit S. Lejal N. Huet J.-C. Delmas B.
TitleActive residues and viral substrate cleavage sites of the protease of the birnavirus infectious pancreatic necrosis virus.
SourceJ. Virol. 74:2057-2066(2000).
PubMed ID10666235

2AuthorsFeldman A.R. Lee J. Delmas B. Paetzel M.
TitleCrystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism.
SourceJ. Mol. Biol. 358:1378-1389(2006).
PubMed ID16584747

3AuthorsLee J. Feldman A.R. Delmas B. Paetzel M.
TitleCrystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction.
SourceJ. Biol. Chem. 282:24928-24937(2007).
PubMed ID17553791



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