Rubella virus (RUBV) is the etiological agent of a disease known as rubella or
German measles. RUBV, a positive sense, single-strand RNA virus, is the sole
member of the Rubivirus genus [E1] in the Togaviridae family [E2] of animal
viruses. The RUBV genome contains two open reading frames (ORFs) encoding five
proteins after postranslational proteolytic processing; two proteins (P150 and
P90) involved in viral replication are translated from the nonstructural
protein ORF (NSP-ORF) and the three structural proteins that form the virus
particle are translated from the structural protein ORF (ST-ORF). A cysteine
protease domain situated at the C-terminus of P150 and immediately upstream
from the cleavage site within the NS-ORF precursor (P200) is responsible for
self-cleavage of P200 into P150 and P90. This protease domain, termed the NS
protease domain, is a papain-like protease with catalytic dyad of Cys and His.
The NS protease domain contains an EF-hand Ca(2+) binding motif, which plays a
structural role in stabilizing the protease at physiological temperatures, as
well as a structural Zn(2+) binding site coordinated by four cysteines, which
is necessary for protease activity. The RUBV NS protease domain forms
peptidase family C27 [E3] of clan CA [1,2,3,4].
The profile we developed covers the entire RUBV NS protease domain.
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