ID   A0A257CHZ0_9BURK        Unreviewed;       167 AA.
AC   A0A257CHZ0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Ribonuclease P protein component {ECO:0000313|EMBL:OYT88996.1};
GN   Name=rnpA {ECO:0000313|EMBL:OYT88996.1};
GN   ORFNames=CFE46_00750 {ECO:0000313|EMBL:OYT88996.1};
OS   Burkholderiales bacterium PBB6.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015568 {ECO:0000313|EMBL:OYT88996.1, ECO:0000313|Proteomes:UP000216978};
RN   [1] {ECO:0000313|EMBL:OYT88996.1, ECO:0000313|Proteomes:UP000216978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB6 {ECO:0000313|EMBL:OYT88996.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:0000256|ARBA:ARBA00002663}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYT88996.1}.
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DR   EMBL; NKIH01000001; OYT88996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257CHZ0; -.
DR   Proteomes; UP000216978; Unassembled WGS sequence.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 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   4: Predicted;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216978};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ   SEQUENCE   167 AA;  18176 MW;  CA9D4A5853B3D818 CRC64;
     MIGRIVRPAD FERVLAAPQR SRSAHFAVHY VAGVPSRPNA ALAKAAPEAV VPGLSPELST
     GQAGAACTIV DESGHWLGLV VPKRHAKRAV TRNLIKRQVR AAMARHAAEL PAGLWVVRLR
     APFDRQQFLS PGSDHLRATA HDEVDVLFDR AARSPLPPVP YRPRSRT
//