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Database: UniProt
Entry: A3V929_9RHOB
LinkDB: A3V929_9RHOB
Original site: A3V929_9RHOB 
ID   A3V929_9RHOB            Unreviewed;       130 AA.
AC   A3V929;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-NOV-2023, entry version 78.
DE   SubName: Full=Ribonuclease P protein component {ECO:0000313|EMBL:EAQ05392.1};
GN   ORFNames=SKA53_00410 {ECO:0000313|EMBL:EAQ05392.1};
OS   Yoonia vestfoldensis SKA53.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ05392.1, ECO:0000313|Proteomes:UP000004507};
RN   [1] {ECO:0000313|EMBL:EAQ05392.1, ECO:0000313|Proteomes:UP000004507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA53 {ECO:0000313|EMBL:EAQ05392.1,
RC   ECO:0000313|Proteomes:UP000004507};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (JAN-2006) 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:EAQ05392.1}.
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DR   EMBL; AAMS01000010; EAQ05392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3V929; -.
DR   STRING; 314232.SKA53_00410; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_6_3_5; -.
DR   Proteomes; UP000004507; 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:UP000004507};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ   SEQUENCE   130 AA;  14197 MW;  B363E83504F4446C CRC64;
     MSVLKPPAEP DTGAPAVCVC LTVLTKRADF VRASHALRQG TPGIHLQARE RARGEAAGIR
     VGFTCSKKVG NAVARNRAKR RLREVARQVL PEQGRDGWDY VLVGRHDVTA SLPFDALVAD
     LRRALRKVHA
//
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