Ontology Term : Pfam:PF14901 Cleavage inducing molecular chaperone EMBL-EBI

Description  Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity [1]. In eukaryotes, it usually lies 40 residues downstream of DnaJ family Pfam:PF00226. However, the function in eukaryotes is still unknown.
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