ID   RNP2_METJA              Reviewed;         134 AA.
AC   Q57917;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=MJ0494;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=18558617; DOI=10.1093/nar/gkn360;
RA   Pulukkunat D.K., Gopalan V.;
RT   "Studies on Methanocaldococcus jannaschii RNase P reveal insights into the
RT   roles of RNA and protein cofactors in RNase P catalysis.";
RL   Nucleic Acids Res. 36:4172-4180(2008).
RN   [3]
RP   FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012;
RA   Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.;
RT   "Cooperative RNP assembly: complementary rescue of structural defects by
RT   protein and RNA subunits of archaeal RNase P.";
RL   J. Mol. Biol. 411:368-383(2011).
RN   [4]
RP   FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT.
RX   PubMed=22298511; DOI=10.1093/nar/gks013;
RA   Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P.,
RA   Gopalan V.;
RT   "Fidelity of tRNA 5'-maturation: a possible basis for the functional
RT   dependence of archaeal and eukaryal RNase P on multiple protein
RT   cofactors.";
RL   Nucleic Acids Res. 40:4666-4680(2012).
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, ECO:0000269|PubMed:18558617,
CC       ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}.
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. Forms a subcomplex with Rnp3 which stimulates the catalytic
CC       RNA. {ECO:0000255|HAMAP-Rule:MF_00755, ECO:0000269|PubMed:18558617,
CC       ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}.
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; L77117; AAB98484.1; -; Genomic_DNA.
DR   PIR; F64361; F64361.
DR   PDB; 6K0A; EM; 4.60 A; A/B=1-134.
DR   PDB; 6K0B; EM; 4.30 A; A/B=1-134.
DR   PDBsum; 6K0A; -.
DR   PDBsum; 6K0B; -.
DR   AlphaFoldDB; Q57917; -.
DR   SMR; Q57917; -.
DR   STRING; 243232.MJ_0494; -.
DR   EnsemblBacteria; AAB98484; AAB98484; MJ_0494.
DR   KEGG; mja:MJ_0494; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   InParanoid; Q57917; -.
DR   OMA; NPWLIDY; -.
DR   PhylomeDB; Q57917; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
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:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endonuclease; Hydrolase; Nuclease;
KW   Reference proteome; tRNA processing.
FT   CHAIN           1..134
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_0000140020"
SQ   SEQUENCE   134 AA;  15941 MW;  5BD64AB14CF0D9B7 CRC64;
     MIEMLKTLPP TLREKKRYIA FKILYDEELK EGEVVNLIRK AVLEYYGSWG TSKANPWLVY
     YDFPYGILRC QRDNVDYVKA SLILIREFKE KPVNIICLGV SGTIRKAKIK FLGIKKPKRW
     FVIRRERLKA KKQK