| Description | Nidoviruses (Coronaviridae, Arteriviridae, and Roniviridae) feature the most complex genetic organization among plus-strand RNA viruses. Their replicase genes encode an exceptionally large number of nonstructural protein domains which mediate the key functions required for genomic RNA synthesis (replication) and subgenomic RNA (sgRNA) synthesis (transcription). They encode a nonstructural protein, called NSP10 in arteriviruses (Av) and NSP13 in coronaviruses (CoV) [], that is comprised of a C-terminal nucleoside triphosphate-binding/helicase (Hel) motif and a N-terminal cysteine-rich zinc-binding domain (ZBD). The ZBD is critically involved in nidovirus replication and transcription, modulating the ATPase/helicase activity in cis [, , , ]. In SARS-CoV, it has been shown that NSP12 directly interacts with NSP13 and enhances its helicase activity [, , , ].The ZBD is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. It consists of a RING-like module and treble-cleft zinc finger, together coordinating three Zn atoms. The N-terminal RING-like module has a notable binuclear structure with a cross-brace topology involving 6 Cys and 2 His residues that coordinate two zinc ions. The C-terminal zinc finger of ZBD adopts a treble-cleft fold distinct from that of the RING module. It coordinates one Zn ion with a C[H/C]C[C/H] pattern [].This entry represents the ZBD domain from NSP10 of arteriviruses. | Name | Nonstructural protein 10, zinc-binding domain, arterivirus |
| Short Name | NSP10_Av_ZBD | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
