ID   STS1_MAGO7              Reviewed;         313 AA.
AC   A4QYI9; G4N669;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Tethering factor for nuclear proteasome STS1;
GN   Name=STS1; ORFNames=MGG_08586;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Involved in ubiquitin-mediated protein degradation.
CC       Regulatory factor in the ubiquitin/proteasome pathway that controls the
CC       turnover of proteasome substrates. Targets proteasomes to the nucleus
CC       and facilitates the degradation of nuclear proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds the proteasome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cut8/STS1 family. {ECO:0000305}.
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DR   EMBL; CM001234; EHA49793.1; -; Genomic_DNA.
DR   RefSeq; XP_003716112.1; XM_003716064.1.
DR   AlphaFoldDB; A4QYI9; -.
DR   SMR; A4QYI9; -.
DR   STRING; 318829.MGG_08586T0; -.
DR   EnsemblFungi; MGG_08586T0; MGG_08586T0; MGG_08586.
DR   GeneID; 2678698; -.
DR   KEGG; mgr:MGG_08586; -.
DR   VEuPathDB; FungiDB:MGG_08586; -.
DR   eggNOG; ENOG502RNK4; Eukaryota.
DR   HOGENOM; CLU_033658_0_0_1; -.
DR   InParanoid; A4QYI9; -.
DR   OMA; SSLGWMH; -.
DR   OrthoDB; 1349270at2759; -.
DR   Proteomes; UP000009058; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; ISS:PAMGO_MGG.
DR   GO; GO:0031965; C:nuclear membrane; ISS:PAMGO_MGG.
DR   GO; GO:0005634; C:nucleus; ISS:PAMGO_MGG.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:PAMGO_MGG.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; ISS:PAMGO_MGG.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:PAMGO_MGG.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:PAMGO_MGG.
DR   GO; GO:0007059; P:chromosome segregation; ISS:PAMGO_MGG.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISS:PAMGO_MGG.
DR   GO; GO:0007052; P:mitotic spindle organization; ISS:PAMGO_MGG.
DR   GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:InterPro.
DR   GO; GO:0031144; P:proteasome localization; ISS:PAMGO_MGG.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:PAMGO_MGG.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1590; -; 1.
DR   InterPro; IPR013868; Cut8/Sts1_fam.
DR   InterPro; IPR038422; Cut8/Sts1_sf.
DR   PANTHER; PTHR28032; PTHR28032; 1.
DR   Pfam; PF08559; Cut8; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..313
FT                   /note="Tethering factor for nuclear proteasome STS1"
FT                   /id="PRO_0000409415"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34174 MW;  A5550FCD6ADE5ADD CRC64;
     MNVLLTPQPT PFPHQYETSR LSPQRSLSPY TNMTSRKRKA DDNEGDEMSV SPLSSPAIPS
     RHLSRPSKKI RAAEASGRPL PLPRLLETLD TTQLRTVLQK ICERHPDIGQ EVVNGAPRPS
     VGSALGILRD YQQRLRGAIP YGQTSSDYTY YRVKQPLMAL VDAISDFTPQ FLPPIETQVT
     ASLQYLDGAT KVVHELPDWD SQAYRQHKDN AYDEISRAWA LVITEASKRG GGFVLHTGGW
     DQMLAKHNQQ SGGRLGSAMQ AMASNGWIGN NSPNNQNASA SSSSGSGAGG DPNSILNQLV
     NGTYGNPVRV GPW