ID RNPA_RHOBA Reviewed; 146 AA. AC Q7UNR1; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 95. 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}; OrderedLocusNames=RB7431; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10527 / NCIMB 13988 / SH1; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., RA Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). 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; BX294146; CAD75357.1; -; Genomic_DNA. DR RefSeq; NP_867810.1; NC_005027.1. DR RefSeq; WP_011121387.1; NC_005027.1. DR AlphaFoldDB; Q7UNR1; -. DR SMR; Q7UNR1; -. DR STRING; 243090.RB7431; -. DR EnsemblBacteria; CAD75357; CAD75357; RB7431. DR KEGG; rba:RB7431; -. DR PATRIC; fig|243090.15.peg.3585; -. DR eggNOG; COG0594; Bacteria. DR HOGENOM; CLU_117179_9_2_0; -. DR InParanoid; Q7UNR1; -. DR OrthoDB; 9810867at2; -. DR Proteomes; UP000001025; Chromosome. DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central. DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central. DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central. 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..146 FT /note="Ribonuclease P protein component" FT /id="PRO_0000198516" SQ SEQUENCE 146 AA; 16299 MW; 452AC34BA15A9B76 CRC64; MSRTGGKRPL EFPKSSRVVR SSEFTKALRR GGVAANDCLV VFALPHDVPD ADGEPSPDES KTVKCRLGVT IPKKTGNAVV RNRWKRLIRE AFRLNQTQLP SGFDYVVRPK KDVTADWKMI EKGFVKLVGR AVRRSQSSAD RSSTRS //