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{
"metadata": {
"accession": "PF18553",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR040725",
"hierarchy": null,
"name": {
"name": "PheRS DNA binding domain 3",
"short": "PheRS_DBD3"
},
"description": [
{
"text": "<p>This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNAPhe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains [[cite:PUB00091172]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00091172": {
"PMID": 20223217,
"ISBN": null,
"volume": "18",
"issue": "3",
"year": 2010,
"title": "Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns.",
"URL": null,
"raw_pages": "343-53",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Finarov I",
"Moor N",
"Kessler N",
"Klipcan L",
"Safro MG."
],
"DOI_URL": "https://doi.org/10.1016/j.str.2010.01.002"
}
},
"set_info": {
"accession": "CL0123",
"name": "HTH"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 98,
"interactions": 0,
"matches": 4271,
"pathways": 0,
"proteins": 4267,
"proteomes": 2797,
"sets": 1,
"structural_models": {
"alphafold": 3810,
"bfvd": 0
},
"structures": 2,
"taxa": 8006
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 75,
"alignment:full": 2778
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}