{"metadata":{"accession":"PF08694","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR014806","hierarchy":null,"name":{"name":"Ubiquitin-fold modifier-conjugating enzyme 1","short":"UFC1"},"description":[{"text":"<p>Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00034740":{"PMID":15071506,"ISBN":null,"volume":"23","issue":"9","year":2004,"title":"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier.","URL":null,"raw_pages":"1977-86","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Komatsu M","Chiba T","Tatsumi K","Iemura S","Tanida I","Okazaki N","Ueno T","Kominami E","Natsume T","Tanaka K."],"DOI_URL":"http://dx.doi.org/10.1038/sj.emboj.7600205"}},"set_info":{"accession":"CL0208","name":"UBC"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":35,"interactions":0,"matches":1996,"pathways":0,"proteins":1967,"proteomes":1503,"sets":1,"structural_models":{"alphafold":1687},"structures":28,"taxa":4915},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":24,"alignment:full":1383},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7nw1","name":"Crystal structure of UFC1 in complex with UBA5"}}}