POPI_SCHPO
ID POPI_SCHPO Reviewed; 698 AA.
AC Q9UTA4; Q9UU39;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Ribonucleases P/MRP protein subunit pop1;
DE EC=3.1.26.5;
GN Name=pop1; ORFNames=SPAC25B8.16;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-61, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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: Required for processing of 5.8S rRNA (short form) at site A3
CC and for 5' and 3' processing of pre-tRNA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the POP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA87135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB61782.1; -; Genomic_DNA.
DR EMBL; AB027831; BAA87135.1; ALT_INIT; Genomic_DNA.
DR PIR; T50203; T50203.
DR RefSeq; NP_594476.1; NM_001019905.2.
DR AlphaFoldDB; Q9UTA4; -.
DR SMR; Q9UTA4; -.
DR BioGRID; 278048; 4.
DR STRING; 4896.SPAC25B8.16.1; -.
DR MaxQB; Q9UTA4; -.
DR PaxDb; Q9UTA4; -.
DR EnsemblFungi; SPAC25B8.16.1; SPAC25B8.16.1:pep; SPAC25B8.16.
DR GeneID; 2541548; -.
DR KEGG; spo:SPAC25B8.16; -.
DR PomBase; SPAC25B8.16; -.
DR VEuPathDB; FungiDB:SPAC25B8.16; -.
DR eggNOG; KOG3322; Eukaryota.
DR HOGENOM; CLU_007205_0_0_1; -.
DR OMA; WNAKRSH; -.
DR PhylomeDB; Q9UTA4; -.
DR PRO; PR:Q9UTA4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000172; C:ribonuclease MRP complex; EXP:PomBase.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:PomBase.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IDA:PomBase.
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:0006379; P:mRNA cleavage; ISO:PomBase.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISS:PomBase.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR039182; Pop1.
DR InterPro; IPR009723; Pop1_N.
DR InterPro; IPR012590; POPLD_dom.
DR PANTHER; PTHR22731; PTHR22731; 2.
DR Pfam; PF06978; POP1; 1.
DR Pfam; PF08170; POPLD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleus; Reference proteome; rRNA processing; tRNA processing.
FT CHAIN 1..698
FT /note="Ribonucleases P/MRP protein subunit pop1"
FT /id="PRO_0000337990"
SQ SEQUENCE 698 AA; 79931 MW; 987A6BD0BA2C2427 CRC64;
MKRSTGGTQP KGLNVKRSKL ADARFIEVES PALSNGAVDL KKFIESRSFE ITALQDAMKR
SKESSAQRAF QALPRCLRRR AASHNIKRIP KGLRDRALYE MQLSSSSTLP IAPSRQRLKR
FIKRLRRKLA KSGETKAIDS TGSLVTDNST DDSRIPSLAA VKLIRGKFAG RQLRKVWLPT
HLWVCKRAHM INAWGYAIPE KPTEKSYRPT HRAAFRKDAI AFDMSYEPLF CISGPYEALK
EKFGNSFANG LPPVFLNSSR SFTSYLVKSD IHELICPCFL QWNNPTEDDK KQIPVKNPTE
CVQLVIRLHP SAFLQAWNYL SGIAVLDDRI AMHDWRLDLA SFDIHGPDSN IMLHKVFDDV
ELDEAGKVWQ SISNYSSACL PMGASISVKA LVNTRCDKNL SEKGEKSLLD SAENSLPASA
NQYSTHFRYW ERQEIPSFAV FENKNRHTHE KKSSEKEVIP VYITYRKEWN GLTVILPWDY
AKFVWRKMMY QKGIRFGGLE NLHQIAFEKR MPFFPIDYPD TISGQLCEEE RKKRNEDSWK
RRPPAKRVNY QKFGDNFSEI GNPFCCDWVY LNEMVKASRD EDKTLQLVRV QVQLVQRGSL
QDRARIYCLS DDELSKWKTI IYKENLTAEN LLYPKCPNET AIIGFVTTGN FNLNAGKPSG
IANVLAKTIK NEKSGYCIIR NVGCSVPRLA QWKFNQSH