v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | 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 in the Togaviridae family 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 stabilising 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 the MEROPS peptidase family C27 of clan CA [ , , , ]. |
| Short Name | RUBV_NS_PRO |