ID   RRP46_SCHPO             Reviewed;         226 AA.
AC   O42894;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Exosome complex component rrp46;
DE   AltName: Full=Ribosomal RNA-processing protein 46;
GN   Name=rrp46; ORFNames=SPBC115.01c;
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: Non-catalytic component of the RNA exosome complex which has
CC       3'->5' exoribonuclease activity and participates in a multitude of
CC       cellular RNA processing and degradation events. In the nucleus, the RNA
CC       exosome complex is involved in proper maturation of stable RNA species
CC       such as rRNA, snRNA and snoRNA, in the elimination of RNA processing
CC       by-products and non-coding 'pervasive' transcripts, such as antisense
CC       RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with
CC       processing defects, thereby limiting or excluding their export to the
CC       cytoplasm. In the cytoplasm, the RNA exosome complex is involved in
CC       general mRNA turnover and in RNA surveillance pathways, preventing
CC       translation of aberrant mRNAs. The catalytic inactive RNA exosome core
CC       complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the
CC       binding and presentation of RNA for ribonucleolysis, and to serve as a
CC       scaffold for the association with catalytic subunits and accessory
CC       proteins or complexes. ski6 is part of the hexameric ring of RNase PH
CC       domain-containing subunits proposed to form a central channel which
CC       threads RNA substrates for degradation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA exosome complex. Specifically part of the
CC       catalytically inactive RNA exosome core (Exo-9) complex which
CC       associates with catalytic subunits dis3 and rrp6 in cytoplasmic- and
CC       nuclear-specific RNA exosome complex forms. Exo-9 is formed by a
CC       hexameric ring of RNase PH domain-containing subunits and peripheral S1
CC       domain-containing components csl4, rrp4 and rrp40 located on the top of
CC       the ring structure (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17913.1; -; Genomic_DNA.
DR   PIR; T39298; T39298.
DR   RefSeq; NP_595260.1; NM_001021167.2.
DR   AlphaFoldDB; O42894; -.
DR   SMR; O42894; -.
DR   BioGRID; 276215; 5.
DR   STRING; 4896.SPBC115.01c.1; -.
DR   iPTMnet; O42894; -.
DR   MaxQB; O42894; -.
DR   PaxDb; O42894; -.
DR   EnsemblFungi; SPBC115.01c.1; SPBC115.01c.1:pep; SPBC115.01c.
DR   GeneID; 2539660; -.
DR   KEGG; spo:SPBC115.01c; -.
DR   PomBase; SPBC115.01c; rrp46.
DR   VEuPathDB; FungiDB:SPBC115.01c; -.
DR   eggNOG; KOG1069; Eukaryota.
DR   HOGENOM; CLU_063514_2_1_1; -.
DR   InParanoid; O42894; -.
DR   OMA; GSSEWKQ; -.
DR   PhylomeDB; O42894; -.
DR   Reactome; R-SPO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:O42894; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000178; C:exosome (RNase complex); IDA:PomBase.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); EXP:PomBase.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:PomBase.
DR   GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:PomBase.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; ISO:PomBase.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
DR   GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; ISO:PomBase.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; ISO:PomBase.
DR   GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; ISO:PomBase.
DR   GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; ISO:PomBase.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; ISO:PomBase.
DR   GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
DR   Gene3D; 3.30.230.70; -; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF01138; RNase_PH; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exosome; Nucleus; Reference proteome; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..226
FT                   /note="Exosome complex component rrp46"
FT                   /id="PRO_0000139977"
FT   REGION          205..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  24926 MW;  D314DB825300C8FD CRC64;
     MNRIGILSRS DGSSEWKQGS ARVICGVNGP IDVKIRDERL NKATVEVLVQ PVSGVAETLE
     KMISSRIVGI LEDAIFLNTY PRTLIQVSIQ IIEEDGTDTL AAVINGAVLA LLDAGISLKY
     IPCAINCHWK NKITQDEPDV DGTINKLESI ITICYSISSE PAKLIFLETA GPIPEEDFFR
     VLETAPLHAE EVSKKMKELL FETYNESDGH ENEKNPKEDV EMDVVA