{"metadata":{"accession":"PF03671","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR005375","hierarchy":null,"name":{"name":"Ubiquitin fold modifier 1 protein","short":"Ufm1"},"description":[{"text":"<p>This is a family of short ubiquitin-like proteins, that is like neither type-1 or type-2. It is a ubiquitin-fold modifier 1 (Ufm1) that is synthesised in a precursor form of 85 amino-acid residues. In humans the enzyme for Ufm1 is Uba5 and the conjugating enzyme is Ufc1. Prior to activation by Uba5 the extra two amino acids at the C-terminal region of the human pro-Ufm1 protein are removed to expose Gly whose residue is necessary for conjugation to target molecule(s). The mature Ufm1 is conjugated to yet unidentified endogenous proteins,[[cite:PUB00034740]]. While Ubiquitin and many Ubls possess the conserved C-terminal di-glycine that is adenylated by each specific E1 or E1-like enzyme, respectively, in an ATP-dependent manner, Ufm1(1-83) possesses a single glycine at its C-terminus, which is followed by a Ser-Cys dipeptide in the precursor form of Ufm1. The C-terminally processed Ufm1(1-83) is specifically activated by Uba5, an E1-like enzyme, and then transferred to its cognate Ufc1, an E2-like enzyme [[cite:PUB00034738]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00034738":{"PMID":16527251,"ISBN":null,"volume":"343","issue":"1","year":2006,"title":"Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1.","URL":null,"raw_pages":"21-6","medline_journal":"Biochem Biophys Res Commun","ISO_journal":"Biochem. Biophys. Res. Commun.","authors":["Sasakawa H","Sakata E","Yamaguchi Y","Komatsu M","Tatsumi K","Kominami E","Tanaka K","Kato K."],"DOI_URL":"http://dx.doi.org/10.1016/j.bbrc.2006.02.107"},"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":"CL0072","name":"Ubiquitin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":36,"interactions":0,"matches":1977,"pathways":0,"proteins":1961,"proteomes":1382,"sets":1,"structural_models":{"alphafold":1706},"structures":18,"taxa":4552},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":11,"alignment:full":1419},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5iaa","name":"Crystal structure of human UBA5 in complex with UFM1"}}}