{"metadata":{"accession":"PF05127","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007807","hierarchy":null,"name":{"name":"RNA cytidine acetyltransferase NAT10/TcmA, helicase domain","short":"NAT10_TcmA_helicase"},"description":[{"text":"<p>This domain contains a P-loop (Walker A) motif, suggesting that it has ATPase activity, and a Walker B motif. It si found in RNA cytidine acetyltransferase NAT10 from eukaryotes and tRNA(Met) cytidine acetyltransferase TcmA from prokaryotes. NAT10 catalyses the formation of N4-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs [[cite:PUB00050413],[cite:PUB00076725],[cite:PUB00158943],[cite:PUB00158942]]. In tRNA(Met) cytidine acetyltransferase (TmcA) it may function as an RNA helicase motor (driven by ATP hydrolysis) which delivers the wobble base to the active centre of the GCN5-related N-acetyltransferase (GNAT) domain [[cite:PUB00050413]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00050413":{"PMID":19322199,"ISBN":null,"volume":"28","issue":"9","year":2009,"title":"RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon.","URL":null,"raw_pages":"1362-73","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Chimnaronk S","Suzuki T","Manita T","Ikeuchi Y","Yao M","Suzuki T","Tanaka I."],"DOI_URL":"http://dx.doi.org/10.1038/emboj.2009.69"},"PUB00158943":{"PMID":35679869,"ISBN":null,"volume":"82","issue":"15","year":2022,"title":"Direct epitranscriptomic regulation of mammalian translation initiation through N4-acetylcytidine.","URL":null,"raw_pages":"2797-2814.e11","medline_journal":"Mol Cell","ISO_journal":"Mol Cell","authors":["Arango D","Sturgill D","Yang R","Kanai T","Bauer P","Roy J","Wang Z","Hosogane M","Schiffers S","Oberdoerffer S."],"DOI_URL":"https://doi.org/10.1016/j.molcel.2022.05.016"},"PUB00158942":{"PMID":30449621,"ISBN":null,"volume":"175","issue":"7","year":2018,"title":"Acetylation of Cytidine in mRNA Promotes Translation Efficiency.","URL":null,"raw_pages":"1872-1886.e24","medline_journal":"Cell","ISO_journal":"Cell","authors":["Arango D","Sturgill D","Alhusaini N","Dillman AA","Sweet TJ","Hanson G","Hosogane M","Sinclair WR","Nanan KK","Mandler MD","Fox SD","Zengeya TT","Andresson T","Meier JL","Coller J","Oberdoerffer S."],"DOI_URL":"https://doi.org/10.1016/j.cell.2018.10.030"},"PUB00076725":{"PMID":25653167,"ISBN":null,"volume":"43","issue":"4","year":2015,"title":"Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1.","URL":null,"raw_pages":"2242-58","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res.","authors":["Sharma S","Langhendries JL","Watzinger P","Kotter P","Entian KD","Lafontaine DL."],"DOI_URL":"http://dx.doi.org/10.1093/nar/gkv075"}},"set_info":{"accession":"CL0023","name":"P-loop_NTPase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":137,"interactions":0,"matches":6486,"pathways":0,"proteins":6449,"proteomes":5368,"sets":1,"structural_models":{"alphafold":5050},"structures":35,"taxa":11846},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":93,"alignment:full":4148},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}