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{
    "metadata": {
        "accession": "IPR003313",
        "entry_id": null,
        "type": "domain",
        "go_terms": [
            {
                "identifier": "GO:0006355",
                "name": "regulation of DNA-templated transcription",
                "category": {
                    "code": "P",
                    "name": "biological_process"
                }
            }
        ],
        "source_database": "interpro",
        "member_databases": {
            "pfam": {
                "PF02311": "AraC-like ligand binding domain"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR003313",
            "name": "AraC-type arabinose-binding/dimerisation domain",
            "type": "Domain",
            "children": [
                {
                    "accession": "IPR047220",
                    "name": "HTH-type transcriptional activator RhaR/RhaS, N-terminal domain",
                    "type": "Domain",
                    "children": []
                }
            ]
        },
        "name": {
            "name": "AraC-type arabinose-binding/dimerisation domain",
            "short": "AraC-bd"
        },
        "description": [
            {
                "text": "<p>This entry defines the ligand-binding and dimerisation domain of the bacterial regulatory protein AraC and other HTH-type transcriptional regulators. The crystal structure of the arabinose-binding and dimerisation domain of the Escherichia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a β-barrel and completely burying the arabinose with the N-terminal arm of the protein. Dimer contacts in the presence of arabinose are mediated by an antiparallel coiled-coil. In the uncomplexed protein, the N-terminal arm is disordered, uncovering the sugar-binding pocket and allowing it to serve as an oligomerisation interface [[cite:PUB00008093]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00008093": {
                "PMID": 9103202,
                "ISBN": null,
                "volume": "276",
                "issue": "5311",
                "year": 1997,
                "title": "Structural basis for ligand-regulated oligomerization of AraC.",
                "URL": null,
                "raw_pages": "421-5",
                "medline_journal": "Science",
                "ISO_journal": "Science",
                "authors": [
                    "Soisson SM",
                    "MacDougall-Shackleton B",
                    "Schleif R",
                    "Wolberger C."
                ],
                "DOI_URL": "http://dx.doi.org/10.1126/science.276.5311.421"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 74,
            "interactions": 0,
            "matches": 86727,
            "pathways": 0,
            "proteins": 86723,
            "proteomes": 11560,
            "sets": 0,
            "structural_models": {
                "alphafold": 63216,
                "bfvd": 0
            },
            "structures": 11,
            "taxa": 18546
        },
        "entry_annotations": {
            "alignment:seed": 58,
            "alignment:full": 27025
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "2arc",
            "name": "ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE"
        }
    }
}