ID RNPA_FRASN Reviewed; 121 AA. AC A8L8W2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227}; DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227}; GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; GN OrderedLocusNames=Franean1_7340; OS Frankia sp. (strain EAN1pec). OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=298653; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EAN1pec; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C., RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., RA Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other CC RNA substrates such as 4.5S RNA. The protein component plays an CC auxiliary but essential role in vivo by binding to the 5'-leader CC sequence and broadening the substrate specificity of the ribozyme. CC {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00227}; CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP- CC Rule:MF_00227}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000820; ABW16659.1; -; Genomic_DNA. DR AlphaFoldDB; A8L8W2; -. DR SMR; A8L8W2; -. DR STRING; 298653.Franean1_7340; -. DR KEGG; fre:Franean1_7340; -. DR eggNOG; COG0594; Bacteria. DR HOGENOM; CLU_117179_4_1_11; -. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00227; RNase_P; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR000100; RNase_P. DR InterPro; IPR020539; RNase_P_CS. DR NCBIfam; TIGR00188; rnpA; 1. DR PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1. DR PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1. DR Pfam; PF00825; Ribonuclease_P; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00648; RIBONUCLEASE_P; 1. PE 3: Inferred from homology; KW Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing. FT CHAIN 1..121 FT /note="Ribonuclease P protein component" FT /id="PRO_1000100362" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 91..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 121 AA; 13140 MW; 54653FE082380002 CRC64; MLPRGSRVRT RQEHALVGRS GRRVRAGSIV VHSVQTDVDG PPRAGFVVGR RVGNAVVRNR VRRRLREQTR SRLSSLPPGT AVLIRALPDA AGSSSADLGR SLDSAFRTVR SPRPQRSARS G //