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{
    "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"
        }
    }
}