All herpesviruses [E1] 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-α sandwich fold that features a central catalytic
cleft, ideally suited to accommodate the C-terminal stretch of Ub (see
<PDB:2J7Q>). 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 [1,2,3,4,5,E2].
The profile we developed covers the entire htUSP domain.
Gredmark S. Schlieker C. Quesada V. Spooner E. Ploegh H.L.
Title
A functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infection.
Cleavage specificity of the UL48 deubiquitinating protease activity of human cytomegalovirus and the growth of an active-site mutant virus in cultured cells.
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