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.
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