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 27-MAR-2024, entry version 120. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 284812.Q9UU90; -. DR MaxQB; Q9UU90; -. DR PaxDb; 4896-SPCC830-09c-1; -. 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; MQNYLDK; -. DR PhylomeDB; Q9UU90; -. DR PRO; PR:Q9UU90; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0030681; C:multimeric ribonuclease P complex; IBA:GO_Central. DR GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:PomBase. DR GO; GO:0005730; C:nucleolus; IBA:GO_Central. DR GO; GO:0000172; C:ribonuclease MRP complex; EXP:PomBase. DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central. DR GO; GO:0033204; F:ribonuclease P RNA binding; IBA:GO_Central. 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:0001682; P:tRNA 5'-leader removal; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IDA:PomBase. DR Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 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 PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1. DR PANTHER; PTHR15441:SF2; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1. DR Pfam; PF01900; RNase_P_Rpp14; 1. DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 1. DR SUPFAM; SSF160350; Rnp2-like; 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 //