ID RNPA_LACP7 Reviewed; 116 AA. AC A9KLY3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Cphy_3945; OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OS (Clostridium phytofermentans). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae. OX NCBI_TaxID=357809; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000885; ABX44292.1; -; Genomic_DNA. DR RefSeq; WP_012201939.1; NC_010001.1. DR AlphaFoldDB; A9KLY3; -. DR SMR; A9KLY3; -. DR STRING; 357809.Cphy_3945; -. DR KEGG; cpy:Cphy_3945; -. DR eggNOG; COG0594; Bacteria. DR HOGENOM; CLU_117179_9_3_9; -. DR OrthoDB; 9810867at2; -. DR Proteomes; UP000000370; Chromosome. 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 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. PE 3: Inferred from homology; KW Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding; KW tRNA processing. FT CHAIN 1..116 FT /note="Ribonuclease P protein component" FT /id="PRO_1000078194" SQ SEQUENCE 116 AA; 12947 MW; 7D99120631450931 CRC64; MSESLKNSQQ FGNVYKNGKS FANKYLVMYV CKNELSINRL GISVSKKVGN SVVRHRISRL IRESYRLNDS ISNSGLDIVI VARAGSKGKN YSEISSALMH LAKLHKIISS SEPDRN //