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{
"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
}
}
