ID RNPA_BLOFL Reviewed; 120 AA. AC Q7VQV1; 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=Bfl014; OS Blochmannia floridanus. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; ant endosymbionts; Blochmannia. OX NCBI_TaxID=203907; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12886019; DOI=10.1073/pnas.1533499100; RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., RA van Ham R.C.H.J., Gross R., Moya A.; RT "The genome sequence of Blochmannia floridanus: comparative analysis of RT reduced genomes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(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; BX248583; CAD83542.1; -; Genomic_DNA. DR AlphaFoldDB; Q7VQV1; -. DR SMR; Q7VQV1; -. DR STRING; 203907.Bfl014; -. DR KEGG; bfl:Bfl014; -. DR eggNOG; COG0594; Bacteria. DR HOGENOM; CLU_117179_11_0_6; -. DR OrthoDB; 9796422at2; -. DR Proteomes; UP000002192; 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; RNA-binding; tRNA processing. FT CHAIN 1..120 FT /note="Ribonuclease P protein component" FT /id="PRO_0000198442" SQ SEQUENCE 120 AA; 14710 MW; 39CF6C67D43594B8 CRC64; MNKNHLSKRV RLLKINEFFF VFQKPQRIKV HSMTLFSRSN KLNFPRIGLA ISKKYIKHSH ERNRIKRHVR ETFRTHKHNL LSLDFILTVH SKQILSLTNN NLIEELKKLW YHYQNYQQKS //