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.
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