ID   RNP2_THESM              Reviewed;         120 AA.
AC   C6A460;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=TSIB_1353;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS90405.1; -; Genomic_DNA.
DR   RefSeq; WP_015849623.1; NC_012883.1.
DR   AlphaFoldDB; C6A460; -.
DR   SMR; C6A460; -.
DR   STRING; 604354.TSIB_1353; -.
DR   EnsemblBacteria; ACS90405; ACS90405; TSIB_1353.
DR   GeneID; 8096354; -.
DR   KEGG; tsi:TSIB_1353; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OMA; NPWLIDY; -.
DR   OrthoDB; 89278at2157; -.
DR   Proteomes; UP000009079; 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; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..120
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_1000212860"
SQ   SEQUENCE   120 AA;  14061 MW;  A1CEDD4EF0716D9D CRC64;
     MRRKPKTLPP TLRDKNRYIA FQVTGERPFK KEMIKKAIWD VSLKTLGELG TARAKPWFIK
     FDEKTQTGIV RCDRKYVEEI RFVLTLITEI NGSKAIVRTL GVSGTIKRLK MKFLKEFGWK