{"metadata":{"accession":"IPR053648","entry_id":null,"type":"family","go_terms":null,"source_database":"interpro","member_databases":{"ncbifam":{"NF041077":"tRNA Cytidine-2'-O-Methyltransferase"}},"integrated":null,"hierarchy":{"accession":"IPR053648","name":"tRNA Cytidine-2'-O-Methyltransferase","type":"Family","children":[]},"name":{"name":"tRNA Cytidine-2'-O-Methyltransferase","short":"tRNA_Cytidine-2'-O-MTase"},"description":[{"text":"<p>This family of proteins includes enzymes that are responsible for the methylation of cytidine residues in tRNA molecules. Specifically, they catalyze the 2'O-methylation of cytidine at the 32nd position, resulting in the formation of 2'O-methylcytidine. This modification is crucial for the proper functioning of tRNA. The enzymes exhibit specificity for cytidine and are part of a larger superfamily of SAM-binding methyltransferases. They are related to the RNA methyltransferase TrmH family, which shares similar structural motifs and catalytic functions.</p>","llm":true,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00090189":{"PMID":24951554,"ISBN":null,"volume":"20","issue":"8","year":2014,"title":"Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates.","URL":null,"raw_pages":"1257-71","medline_journal":"RNA","ISO_journal":"RNA","authors":["Somme J","Van Laer B","Roovers M","Steyaert J","Versees W","Droogmans L."],"DOI_URL":"https://doi.org/10.1261/rna.044503.114"}},"set_info":null,"overlaps_with":[{"accession":"IPR029026","name":"tRNA (guanine-N1-)-methyltransferase, N-terminal","type":"homologous_superfamily"},{"accession":"IPR029028","name":"Alpha/beta knot methyltransferases","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":46,"pathways":0,"proteins":46,"proteomes":28,"sets":0,"structural_models":{"alphafold":45,"bfvd":0},"structures":2,"taxa":69},"entry_annotations":{},"cross_references":{},"is_llm":true,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4cng","name":"Crystal structure of Sulfolobus acidocaldarius TrmJ in complex with S-adenosyl-L-Homocysteine"}}}