{"metadata":{"accession":"PF01900","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002759","hierarchy":null,"name":{"name":"Rpp14/Pop5 family","short":"RNase_P_Rpp14"},"description":[{"text":"<p>tRNA processing enzyme ribonuclease P (RNase P) is a ubiquitous ribozyme that catalyzes a Mg2-dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA). Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins [[cite:PUB00007201]]. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14- (Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. This family includes Rnp2 (also known as Pop5) from archaea [[cite:PUB00097410]] and Pop5/Rpp14 from eukaryotes [[cite:PUB00100655],[cite:PUB00097413]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00097413":{"PMID":28715256,"ISBN":null,"volume":"81","issue":"9","year":2017,"title":"Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.","URL":null,"raw_pages":"1670-1680","medline_journal":"Biosci Biotechnol Biochem","ISO_journal":"Biosci Biotechnol Biochem","authors":["Kimura M."],"DOI_URL":null},"PUB00100655":{"PMID":30262633,"ISBN":null,"volume":"362","issue":"6415","year":2018,"title":"Structural insight into precursor tRNA processing by yeast ribonuclease P.","URL":null,"raw_pages":null,"medline_journal":"Science","ISO_journal":"Science","authors":["Lan P","Tan M","Zhang Y","Niu S","Chen J","Shi S","Qiu S","Wang X","Peng X","Cai G","Cheng H","Wu J","Li G","Lei M."],"DOI_URL":null},"PUB00007201":{"PMID":10024167,"ISBN":null,"volume":"5","issue":"2","year":1999,"title":"Rpp14 and Rpp29, two protein subunits of human ribonuclease P.","URL":null,"raw_pages":"153-7","medline_journal":"RNA","ISO_journal":"RNA","authors":["Jarrous N","Eder PS","Wesolowski D","Altman S."],"DOI_URL":"http://dx.doi.org/10.1017/S135583829800185X"},"PUB00097410":{"PMID":16829535,"ISBN":null,"volume":"140","issue":"2","year":2006,"title":"Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3.","URL":null,"raw_pages":"293-8","medline_journal":"J Biochem","ISO_journal":"J Biochem","authors":["Terada A","Honda T","Fukuhara H","Hada K","Kimura M."],"DOI_URL":null}},"set_info":{"accession":"CL0734","name":"Rpp14-Pop5-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":79,"interactions":0,"matches":5297,"pathways":0,"proteins":5287,"proteomes":3673,"sets":1,"structural_models":{"alphafold":4599},"structures":15,"taxa":9445},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":184,"alignment:full":3869},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2czv","name":"Crystal structure of archeal RNase P protein ph1481p in complex with ph1877p"}}}