{"rfam": {"acc": "RF00010", "id": "RNaseP_bact_a", "description": "Bacterial RNase P class A", "comment": "Ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised activity is the generation of mature 5'-ends of tRNAs by cleaving the 5'-leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins. RNA from bacterial RNase Ps retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. Isolated eukaryotic and archaeal RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryotic holoenzyme s have a much greater protein content than the bacterial ones, the RNA cores from all the three lineages are homologous -- helices corresponding to P1, P2, P3, P4, and P10/11 are common to all cellular RNase P RNAs. Yet, there is considerable sequence variation, particularly among the eukaryotic RNAs. Identified in Yersinia as Ysr151/RnpB. ", "curation": {"author": "Griffiths-Jones SR, Mifsud W", "seed_source": "Brown JW, The Ribonuclease P Database, PMID:9847214", "num_seed": 458, "num_full": 8471, "num_species": 8783, "type": "Gene; ribozyme;", "structure_source": "Published; PMID:9847214"}, "cm": {"build_command": "cmbuild -F CM SEED", "calibrate_command": "cmcalibrate --mpi CM", "search_command": "cmsearch --cpu 4 --verbose --nohmmonly -T 17.69 -Z 2958934 CM SEQDB", "cutoffs": {"gathering": 100.0, "trusted": 101.0, "noise": 99.9}}, "release": {"date": "2026-01-16", "number": "15.1"}, "clan": {"acc": "CL00002", "id": "RNaseP"}}}