ID   POP5_SCHPO              Reviewed;         139 AA.
AC   Q9UU90;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Ribonuclease P/MRP protein subunit POP5;
DE            EC=3.1.26.5;
GN   ORFNames=SPCC830.09c;
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).
CC   -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. Also a component of
CC       RNase MRP, which cleaves pre-rRNA sequences (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB52882.1; -; Genomic_DNA.
DR   PIR; T41635; T41635.
DR   RefSeq; NP_588479.1; NM_001023470.2.
DR   AlphaFoldDB; Q9UU90; -.
DR   SMR; Q9UU90; -.
DR   BioGRID; 275473; 4.
DR   STRING; 4896.SPCC830.09c.1; -.
DR   MaxQB; Q9UU90; -.
DR   PaxDb; Q9UU90; -.
DR   EnsemblFungi; SPCC830.09c.1; SPCC830.09c.1:pep; SPCC830.09c.
DR   PomBase; SPCC830.09c; -.
DR   VEuPathDB; FungiDB:SPCC830.09c; -.
DR   eggNOG; KOG4639; Eukaryota.
DR   HOGENOM; CLU_086710_1_2_1; -.
DR   InParanoid; Q9UU90; -.
DR   OMA; FLDRAMG; -.
DR   PhylomeDB; Q9UU90; -.
DR   PRO; PR:Q9UU90; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:PomBase.
DR   GO; GO:0000172; C:ribonuclease MRP complex; EXP:PomBase.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; IEA:InterPro.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:PomBase.
DR   GO; GO:1905267; P:endonucleolytic cleavage involved in tRNA processing; IDA:PomBase.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
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; IPR016819; RNase_P/MRP_POP5.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR   SUPFAM; SSF160350; SSF160350; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..139
FT                   /note="Ribonuclease P/MRP protein subunit POP5"
FT                   /id="PRO_0000140014"
SQ   SEQUENCE   139 AA;  15680 MW;  3E581179B769E589 CRC64;
     MVRFKSRYLL FEVLYPEAKE FFDYPTIPSD SSITTSSLSK IIRTMVAENF GDVGIGKVAS
     SLTVKYFSPN TSTGILRVSR QHFRLAWAAL VLIRELYGKP VIIRVVRVSG TIKKAELAAI
     ERNKSEIHNI SLMDEPIEV