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{
    "metadata": {
        "accession": "IPR029402",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "pfam": {
                "PF14810": "Patch-forming domain C2 of tRNA-guanine transglycosylase"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR029402",
            "name": "tRNA-guanine transglycosylase, patch-forming domain C2",
            "type": "Domain",
            "children": []
        },
        "name": {
            "name": "tRNA-guanine transglycosylase, patch-forming domain C2",
            "short": "TGT_C2"
        },
        "description": [
            {
                "text": "<p>Domain C2 of tRNA-guanine transglycosylase is formed by a four-stranded anti-parallel β-sheet lined with two α helices. It has conserved basic residues on the surface of the β-sheets as does the C-terminal domain PUA ([interpro:IPR002478]). The catalytic domain of TGT has conserved basic residues on the outer surface of the N-terminal three-stranded β sheet, which closes the barrel. It is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds [[cite:PUB00018357]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00018357": {
                "PMID": 12054814,
                "ISBN": null,
                "volume": "318",
                "issue": "3",
                "year": 2002,
                "title": "Crystal structure of archaeosine tRNA-guanine transglycosylase.",
                "URL": null,
                "raw_pages": "665-77",
                "medline_journal": "J Mol Biol",
                "ISO_journal": "J. Mol. Biol.",
                "authors": [
                    "Ishitani R",
                    "Nureki O",
                    "Fukai S",
                    "Kijimoto T",
                    "Nameki N",
                    "Watanabe M",
                    "Kondo H",
                    "Sekine M",
                    "Okada N",
                    "Nishimura S",
                    "Yokoyama S."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/S0022-2836(02)00090-6"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR038250",
                "name": "TGT, patch-forming C2 domain superfamily",
                "type": "homologous_superfamily"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 10,
            "interactions": 0,
            "matches": 1403,
            "pathways": 2,
            "proteins": 1403,
            "proteomes": 583,
            "sets": 0,
            "structural_models": {
                "alphafold": 1346,
                "bfvd": 0
            },
            "structures": 4,
            "taxa": 1304
        },
        "entry_annotations": {
            "alignment:seed": 66,
            "alignment:full": 439
        },
        "cross_references": {
            "ec": {
                "displayName": "ENZYME",
                "description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
                "rank": 19,
                "accessions": [
                    {
                        "accession": "2.4.2.48",
                        "url": "https://enzyme.expasy.org/EC/2.4.2.48"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}