ID   RPR2_SCHPO              Reviewed;         107 AA.
AC   Q9Y813;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Ribonuclease P protein subunit rpr2;
DE            EC=3.1.26.5;
DE   AltName: Full=RNA-processing protein rpr2;
GN   Name=rpr2; ORFNames=SPBC1105.16c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 4 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB50979.1; -; Genomic_DNA.
DR   PIR; T39293; T39293.
DR   RefSeq; NP_596472.1; NM_001022391.2.
DR   AlphaFoldDB; Q9Y813; -.
DR   SMR; Q9Y813; -.
DR   STRING; 284812.Q9Y813; -.
DR   PaxDb; 4896-SPBC1105-16c-1; -.
DR   EnsemblFungi; SPBC1105.16c.1; SPBC1105.16c.1:pep; SPBC1105.16c.
DR   GeneID; 2539745; -.
DR   KEGG; spo:SPBC1105.16c; -.
DR   PomBase; SPBC1105.16c; rpr2.
DR   VEuPathDB; FungiDB:SPBC1105.16c; -.
DR   eggNOG; KOG4394; Eukaryota.
DR   HOGENOM; CLU_079140_4_0_1; -.
DR   InParanoid; Q9Y813; -.
DR   OMA; HCRISYL; -.
DR   PhylomeDB; Q9Y813; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q9Y813; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004526; F:ribonuclease P activity; ISO:PomBase.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   Gene3D; 6.20.50.20; -; 1.
DR   InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR   PANTHER; PTHR14742:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P21; 1.
DR   PANTHER; PTHR14742; RIBONUCLEASE P SUBUNIT P21; 1.
DR   Pfam; PF04032; Rpr2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..107
FT                   /note="Ribonuclease P protein subunit rpr2"
FT                   /id="PRO_0000317087"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  12366 MW;  131B4C7FD257F4EB CRC64;
     MSTKSKDQHA RVSYLYQASQ LLFRNVQEPT LSRHYISTAK DVSQKSVMRI HPDIKRTICK
     GCNSLLVPGK SCSIRFEEPS RKNPSIDRVL WICKKCAFKK RFSDKSC
//