InterPro domain: IPR032843

This entry represents Jiv (J-domain protein interacting with viral protein), a domain found in the DnaJ protein from eukaryotes [ 1 ]. It can also be found 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 [ 2 ]. In eukaryotes, it usually lies 40 residues downstream of DnaJ domain ( IPR001623 ). However, the function of this domain in eukaryotes is still unknown.

1. A cellular J-domain protein modulates polyprotein processing and cytopathogenicity of a pestivirus. J. Virol. 75, 9470-82
2. Cell-derived sequences in the N-terminal region of the polyprotein of a cytopathogenic pestivirus. J. Virol. 77, 10663-9