pfam09401: CoV_NSP10 (This model is not part of the current CDD release)
Coronavirus RNA synthesis protein NSP10
Non-structural protein 10 (NSP10) is involved in RNA synthesis. It is synthesised as a polyprotein whose cleavage generates many non-structural proteins. NSP10 contains two zinc binding motifs and forms two anti-parallel helices which are stacked against an irregular beta sheet. A cluster of basic residues on the protein surface suggests a nucleic acid-binding function. NSP10 interacts with NSP14 and NSP16 and regulates their respective ExoN and 2-O-MTase activities. When binding to the N-terminal of NSP14, NSP10 allows the ExoN active site to adopt a stably closed conformation and is an allosteric regulator that stabilizes NSP16. The structure of the SARS-CoV-2 NSP10/NSP16 heterodimer revealed that it is extremely similar to that of its SARS-CoV-1 homologue. One NSP10 residue, Tyr-96 is of particular interest as it plays a crucial role in the NSP10-NSP16/NSP14 interaction. This residue is specific for SARS-CoV NSP10 and is a phenylalanine in most other Coronavirus homologues.
Jiyao W et al.(2023). "The conserved domain database in 2023.",