| Primary Identifier | IPR044382 | Type | Domain |
| Short Name | NSP3_SUD_C_MERS-CoV |
| description | This entry represents the SUD-C of Middle East respiratory syndrome-related (MERS) coronavirus (CoV) NSP3 and other NSP3s from betacoronaviruses in the merbecovirus subgenera (C lineage), including several bat-CoVs such as Tylonycteris bat CoV HKU4, Pipistrellus bat CoV HKU5, and Hypsugo bat CoV HKU25.NSP3 of SARS coronavirus includes a SARS-unique domain (SUD) consisting of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C. SUD-N and SUD-M are macro domains which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides) []. SUD is not as specific to SARS CoV as originally thought and is also found in MERS and related bat coronaviruses. Similar to SARS SUD-C, Tylonycteris bat-CoV HKU4 SUD-C (HKU4 C), a member of the MERS SUD-C group, also adopts a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. However, there is little sequence similarity between the two domains. SARS SUD-C has been shown to bind to single-stranded RNA and recognise purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behaviour of the SARS SUD-M macrodomain. It is not known whether MERS SUD-C or HKU4 C functions in the same way [, ]. |
