{"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}}