PROSITE documentation PDOC51889

Rubella virus (RUBV) nonstructural (NS) protease domain profile

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.