{"metadata":{"accession":"PF18082","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR041273","hierarchy":null,"name":{"name":"N-acyltransferase N-terminal domain","short":"NAT_N"},"description":[{"text":"<p>This is the N-terminal all helix domain found in N-acyltransferases (NATs), the gene products orf11 and dbv8. The all-helix domain is composed of eight helices with two helix-turn-helix motifs in tandem. It is structurally akin to the AAA+ protein family (ATPases associated with diverse cellular activities) [[cite:PUB00091662]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00091662":{"PMID":25095906,"ISBN":null,"volume":"136","issue":"31","year":2014,"title":"Multiple complexes of long aliphatic N-acyltransferases lead to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics, effectively killing vancomycin-resistant enterococcus.","URL":null,"raw_pages":"10989-95","medline_journal":"J Am Chem Soc","ISO_journal":"J. Am. Chem. Soc.","authors":["Lyu SY","Liu YC","Chang CY","Huang CJ","Chiu YH","Huang CM","Hsu NS","Lin KH","Wu CJ","Tsai MD","Li TL."],"DOI_URL":"https://doi.org/10.1021/ja504125v"}},"set_info":{"accession":"CL0023","name":"P-loop_NTPase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":9,"interactions":0,"matches":1090,"pathways":0,"proteins":1090,"proteomes":979,"sets":1,"structural_models":{"alphafold":638},"structures":9,"taxa":1365},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":114,"alignment:full":557},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}