{"metadata":{"accession":"PF10354","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR019446","hierarchy":null,"name":{"name":"rRNA (uridine-N3-)-methyltransferase BTM5-like","short":"BMT5-like"},"description":[{"text":"<p>This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterised Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteristic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains [[cite:PUB00075659]]. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00075659":{"PMID":24335083,"ISBN":null,"volume":"42","issue":"5","year":2014,"title":"Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae.","URL":null,"raw_pages":"3246-60","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res.","authors":["Sharma S","Yang J","Duttmann S","Watzinger P","Kotter P","Entian KD."],"DOI_URL":"http://dx.doi.org/10.1093/nar/gkt1281"}},"set_info":{"accession":"CL0063","name":"NADP_Rossmann"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":206,"interactions":0,"matches":6225,"pathways":0,"proteins":5700,"proteomes":3040,"sets":1,"structural_models":{"alphafold":4666},"structures":0,"taxa":7802},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":140,"alignment:full":4573},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}