{"metadata":{"accession":"PF12124","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR022733","hierarchy":null,"name":{"name":"Betacoronavirus SUD-C domain","short":"bCoV_SUD_C"},"description":[{"text":"<p>This domain is found in betacoronavirus non-structural protein NSP3,  and is about 65 amino acids in length. It was originally thought to  exist only in SARS-coronaviruses, and so was termed the SARS-unique  domain (SUD), however this has since been shown to be incorrect. The NSP3 is the product of ORF1a, proteolytically released from the pp1a/1ab polyprotein [[cite:PUB00094069],[cite:PUB00050012]]. The SUD domain has three globular domains, SUD-N (N-terminal), SUD-M (middle region of SUD), and SUD-C (C-terminal). SUD-C adopts a fold consisting of seven beta-strands arranged in an anti-parallel beta-sheet, and two alpha-helices which are packed against the same side of the beta-sheet. It adopts a frataxin-like fold with structural similarities to DNA-binding domains. It has been shown that SUD-C binds to single-stranded RNA and recognises purine bases more strongly than pyrimidine bases, but these interactions are stabilised in the presence of SUD-M. The function of this domain is not clear but studies of structural homologues of SUD-C suggest that it could be related to metal, adenylate and nucleic acid binding [[cite:PUB00062522]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00050012":{"PMID":19436709,"ISBN":null,"volume":"5","issue":"5","year":2009,"title":"The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes.","URL":null,"raw_pages":"e1000428","medline_journal":"PLoS Pathog","ISO_journal":"PLoS Pathog.","authors":["Tan J","Vonrhein C","Smart OS","Bricogne G","Bollati M","Kusov Y","Hansen G","Mesters JR","Schmidt CL","Hilgenfeld R."],"DOI_URL":"http://dx.doi.org/10.1371/journal.ppat.1000428"},"PUB00094069":{"PMID":29128390,"ISBN":null,"volume":"149","issue":null,"year":2018,"title":"Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.","URL":null,"raw_pages":"58-74","medline_journal":"Antiviral Res","ISO_journal":"Antiviral Res.","authors":["Lei J","Kusov Y","Hilgenfeld R."],"DOI_URL":null},"PUB00062522":{"PMID":20493876,"ISBN":null,"volume":"400","issue":"4","year":2010,"title":"SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.","URL":null,"raw_pages":"724-42","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Johnson MA","Chatterjee A","Neuman BW","Wuthrich K."],"DOI_URL":"http://dx.doi.org/10.1016/j.jmb.2010.05.027"}},"set_info":{"accession":"CL0789","name":"SUD_C-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":233,"interactions":0,"matches":3960,"pathways":0,"proteins":3960,"proteomes":2,"sets":1,"structural_models":{"alphafold":0,"bfvd":2},"structures":8,"taxa":109},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":1,"alignment:full":10},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}