ID RNPA_GEOSW Reviewed; 116 AA. AC C5D9Z1; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 72. 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=GWCH70_3433; OS Geobacillus sp. (strain WCH70). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) 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; CP001638; ACS26069.1; -; Genomic_DNA. DR AlphaFoldDB; C5D9Z1; -. DR SMR; C5D9Z1; -. DR STRING; 471223.GWCH70_3433; -. DR KEGG; gwc:GWCH70_3433; -. DR eggNOG; COG0594; Bacteria. DR HOGENOM; CLU_117179_9_1_9; -. DR OrthoDB; 9810867at2; -. 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..116 FT /note="Ribonuclease P protein component" FT /id="PRO_1000204348" SQ SEQUENCE 116 AA; 13941 MW; CFEBB8EFF33063A7 CRC64; MKKKYRIKKN KEFQEVFQRG TSMANRQFVI YMLDRPEQPY FRIGLSVSKK LGKAVVRNRI KRYIRQVFLE MKDDIMPQKD YVIIARLPVA EMTYFEVKKS LLHVLRKAGA LKRDIK //