ID   RNP2_THEON              Reviewed;         120 AA.
AC   B6YV61;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Ribonuclease P protein component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE            Short=RNase P component 2 {ECO:0000255|HAMAP-Rule:MF_00755};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00755};
DE   AltName: Full=Pop5 {ECO:0000255|HAMAP-Rule:MF_00755};
GN   Name=rnp2 {ECO:0000255|HAMAP-Rule:MF_00755}; OrderedLocusNames=TON_1799;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
CC   -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC       Rule:MF_00755}.
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_00755};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00755}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000255|HAMAP-Rule:MF_00755}.
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DR   EMBL; CP000855; ACJ17289.1; -; Genomic_DNA.
DR   RefSeq; WP_012572761.1; NC_011529.1.
DR   AlphaFoldDB; B6YV61; -.
DR   SMR; B6YV61; -.
DR   STRING; 523850.TON_1799; -.
DR   EnsemblBacteria; ACJ17289; ACJ17289; TON_1799.
DR   GeneID; 7017468; -.
DR   KEGG; ton:TON_1799; -.
DR   PATRIC; fig|523850.10.peg.1813; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OMA; NPWLIDY; -.
DR   OrthoDB; 89278at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3250; -; 1.
DR   HAMAP; MF_00755; RNase_P_2; 1.
DR   InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   InterPro; IPR016434; Rnp2_archaea.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF004952; RNase_P_2; 1.
DR   SUPFAM; SSF160350; SSF160350; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; tRNA processing.
FT   CHAIN           1..120
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_1000194589"
SQ   SEQUENCE   120 AA;  13883 MW;  2091FB5CC3E1D96B CRC64;
     MKERPKTLPP TLRDKHRYIA FQVIGERTFT KDEIKRAIWE ASLSTLGTLG SARAKPWFIK
     FNEKSQTGIV RVDRKHVEEL RFALALVTHI NGSKAIFRTL GVSGTIKRLK RKFLSEFGWK