Protein Domain : Large tegument protein deneddylase IPR034702

Type	Family
Description	All herpesviruses contain a Ubiquitin (Ub)-specific cysteine protease (USP) domain embedded within their large tegument protein. The herpesvirus tegument ubiquitin (Ub)-specific protease (htUSP) domain of ~200 amino acids adopts an α-β-alpha sandwich fold that features a central catalytic cleft, ideally suited to accommodate the C-terminal stretch of Ub. The catalytic triad Cys-His-Asp is strictly conserved, along with a putative oxyanion hole-forming Gln residue. The htUSP domain is a member of peptidase family C76 of clan CA [ , , , , ].BPLF1, the Epstein-Barr-virus-encoded member of this protease family, is a deneddylase that regulates virus production by modulating the activity of cullin-RING ligases. Homologues encoded by other herpesviruses share the deneddylase activity [ ].
Short Name	HSV_LTP