RNP1_SCHPO
ID RNP1_SCHPO Reviewed; 217 AA.
AC Q9P7W9; Q7Z988;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Probable ribonuclease P protein subunit 1;
DE EC=3.1.26.5;
GN ORFNames=SPBC1703.01c, SPBP4H10.22c;
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: Part 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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAD99134.2; -; Genomic_DNA.
DR PIR; T50314; T50314.
DR RefSeq; XP_001713139.1; XM_001713087.2.
DR AlphaFoldDB; Q9P7W9; -.
DR SMR; Q9P7W9; -.
DR BioGRID; 276491; 3.
DR STRING; 4896.SPBC1703.01c.1; -.
DR MaxQB; Q9P7W9; -.
DR PaxDb; Q9P7W9; -.
DR EnsemblFungi; SPBC1703.01c.1; SPBC1703.01c.1:pep; SPBC1703.01c.
DR PomBase; SPBC1703.01c; -.
DR VEuPathDB; FungiDB:SPBC1703.01c; -.
DR eggNOG; KOG4046; Eukaryota.
DR HOGENOM; CLU_078577_0_0_1; -.
DR InParanoid; Q9P7W9; -.
DR OMA; IPKSECV; -.
DR PhylomeDB; Q9P7W9; -.
DR PRO; PR:Q9P7W9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0000172; C:ribonuclease MRP complex; EXP:PomBase.
DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
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: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 Gene3D; 2.30.30.210; -; 1.
DR InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR PANTHER; PTHR13348; PTHR13348; 1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..217
FT /note="Probable ribonuclease P protein subunit 1"
FT /id="PRO_0000128423"
SQ SEQUENCE 217 AA; 24629 MW; 441B0EADE8E8A7CD CRC64;
MADPLYSSLK TVNSTSKVTP ESLVFQTKIL TPEEAKNVIN EKIAFKPLLL VPSLNLEKQG
DRKESVASKK RKKLSSKEKK KLQLNVVPKI ADYSQFKHLH SMWCSYILEV IAGCTGESLM
AKLAKAEYQG AYMQVLRSKS TTRVGLEGIC IHESKHMLSL ITKENRVVRV PKQDSVMKVI
VDVPQRKLVF ELYTQHLLLR AGDRSNKRFK SKNTIDL
