{"metadata":{"accession":"PF12379","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR024358","hierarchy":null,"name":{"name":"Betacoronavirus replicase NSP3, N-terminal","short":"bCoV_NSP3_N"},"description":[{"text":"<p>This domain family corresponds to the N-terminal domain of NSP3 (non-structural protein 3, also known as nsp3) found in Betacoronavirus, which is encoded on the replicase polyprotein. This family includes the NSP3a domain which has the ubiquitin-like 1 (UB1) and glutamic acid-rich acidic (AC) hypervariable domains [[cite:PUB00094113]]. NSP3a interacts with numerous other proteins involved in replication and transcription and may serve as a scaffolding protein for these processes. The N-terminal NSP3a domain interacts with N (nucleocapsid) protein to colocalise genomic RNA with the nascent replicase-transcriptase complex at the earliest stages of infection, essential for the virus [[cite:PUB00094112]]. The C-terminal Glu-rich subdomain is best described as a flexible tail attached to the globular UB1 subdomain [[cite:PUB00047544]]. The family is found in association with [pfam:PF08716], [pfam:PF01661], [pfam:PF05409], [pfam:PF06471], [pfam:PF08717], [pfam:PF06478], [pfam:PF09401], [pfam:PF06460], [pfam:PF08715], [pfam:PF08710].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00047544":{"PMID":17728234,"ISBN":null,"volume":"81","issue":"21","year":2007,"title":"Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.","URL":null,"raw_pages":"12049-60","medline_journal":"J Virol","ISO_journal":"J. Virol.","authors":["Serrano P","Johnson MA","Almeida MS","Horst R","Herrmann T","Joseph JS","Neuman BW","Subramanian V","Saikatendu KS","Buchmeier MJ","Stevens RC","Kuhn P","Wuthrich K."],"DOI_URL":"http://dx.doi.org/10.1128/JVI.00969-07"},"PUB00094113":{"PMID":18367524,"ISBN":null,"volume":"82","issue":"11","year":2008,"title":"Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.","URL":null,"raw_pages":"5279-94","medline_journal":"J Virol","ISO_journal":"J. Virol.","authors":["Neuman BW","Joseph JS","Saikatendu KS","Serrano P","Chatterjee A","Johnson MA","Liao L","Klaus JP","Yates JR 3rd","Wuthrich K","Stevens RC","Buchmeier MJ","Kuhn P."],"DOI_URL":null},"PUB00094112":{"PMID":23943763,"ISBN":null,"volume":"4","issue":"4","year":2013,"title":"Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles.","URL":null,"raw_pages":null,"medline_journal":"mBio","ISO_journal":"mBio","authors":["Angelini MM","Akhlaghpour M","Neuman BW","Buchmeier MJ."],"DOI_URL":null},"PUB00094055":{"PMID":31776274,"ISBN":null,"volume":"94","issue":"4","year":2020,"title":"Nucleocapsid Protein Recruitment to Replication-Transcription Complexes Plays a Crucial Role in Coronaviral Life Cycle.","URL":null,"raw_pages":null,"medline_journal":"J Virol","ISO_journal":"J. Virol.","authors":["Cong Y","Ulasli M","Schepers H","Mauthe M","V'kovski P","Kriegenburg F","Thiel V","de Haan CAM","Reggiori F."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":21,"interactions":0,"matches":308,"pathways":0,"proteins":308,"proteomes":3,"sets":0,"structural_models":{"alphafold":7},"structures":17,"taxa":63},"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":{"accession":"8hda","name":"Crystal structure of Ubl1 (residues 18-111) of SARS-CoV-2"}}}