| Primary Identifier | IPR044348 | Type | Domain |
| Short Name | NSP10_1B_Av |
| description | Nidoviruses (Coronaviridae, Arteriviridae, and Roniviridae) feature the most complex genetic organization among plus-strand RNA viruses. Their replicase genes encode an exceptionally large replicase polyprotein 1a/ab which is then proteolytically processed to release different nonstructural proteins (NSPs) that mediate the key functions required for replication and transcription. One of these NSPs, called NSP10 in arteriviruses (Av) and NSP13 in coronaviruses (CoV) functions as a helicase [, ]. It is a multidomain protein consisting of a N-terminal Cys/His rich zinc-binding domain (ZBD) and a helicase core that belongs to the superfamily SF1 of helicases. The helicase core contains two RecA1 and RecA2 domains and a 1B domain [].This entry represents the 1B domain, which has a regulatory role modulating the nucleic acid substrate binding. Based on the structures from the Equine arteritis virus (EAV) NSP10, 1B domain undergoes large conformational change upon substrate binding, and forms a channel together with 1A and 2A domains that accommodates the single stranded nucleic acids [, ]. |
