"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF12124"	"{'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}"	"{}"	"[{'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}]"	""	""	""	"IPR022733"	False	False	False	"{'PUB00050012': {'PMID': 19436709, 'ISBN': None, 'volume': '5', 'issue': '5', 'year': 2009, 'title': 'The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes.', 'URL': None, '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': None, 'volume': '149', 'issue': None, 'year': 2018, 'title': 'Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.', 'URL': None, 'raw_pages': '58-74', 'medline_journal': 'Antiviral Res', 'ISO_journal': 'Antiviral Res.', 'authors': ['Lei J', 'Kusov Y', 'Hilgenfeld R.'], 'DOI_URL': None}, 'PUB00062522': {'PMID': 20493876, 'ISBN': None, 'volume': '400', 'issue': '4', 'year': 2010, 'title': 'SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.', 'URL': None, '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'}}"	""	"{'name': 'Betacoronavirus SUD-C domain', 'short': 'bCoV_SUD_C'}"	""	""	"{'accession': 'CL0789', 'name': 'SUD_C-like'}"	"pfam"	"domain"	""