ID   STS1_DEBHA              Reviewed;         350 AA.
AC   Q6BWL0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Tethering factor for nuclear proteasome STS1;
GN   Name=STS1; OrderedLocusNames=DEHA2B10494g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382134; CAG85413.2; -; Genomic_DNA.
DR   RefSeq; XP_457409.2; XM_457409.1.
DR   AlphaFoldDB; Q6BWL0; -.
DR   SMR; Q6BWL0; -.
DR   STRING; 4959.XP_457409.2; -.
DR   EnsemblFungi; CAG85413; CAG85413; DEHA2B10494g.
DR   GeneID; 2913336; -.
DR   KEGG; dha:DEHA2B10494g; -.
DR   VEuPathDB; FungiDB:DEHA2B10494g; -.
DR   eggNOG; ENOG502RNK4; Eukaryota.
DR   HOGENOM; CLU_054606_2_0_1; -.
DR   InParanoid; Q6BWL0; -.
DR   OMA; NICYEQV; -.
DR   OrthoDB; 1349270at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:InterPro.
DR   GO; GO:0031144; P:proteasome localization; IEA:InterPro.
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..350
FT                   /note="Tethering factor for nuclear proteasome STS1"
FT                   /id="PRO_0000409410"
FT   REGION          17..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  39814 MW;  B30625696240B382 CRC64;
     MMSTGFSWGT QALSESTEVN SGLGDLPTSI PRYTPNLKPV NNNHHSNGKK RRYSEDQESK
     VVKPTGNRKH YTTPSTYYKS KKSRTPKIMG QKLPINRLVE ALDHTSLQRL LESLIHEHPE
     ISNTIDKISP KPTLTDSIEL IKQKFNSIMH HLPYKCDTES DYSYLRIKTH LNEFLNCLSD
     FILNFLPPIE TNVFNSLKFL DEVTDLIHTL PNFSNSEFQY TKSMAYEQIS NTWLIVLNHK
     MRPDDGTNNN NTSNTNEALS SSSSPSPVAQ CNMENSAQLI KIIDELNLQQ KLAKHDNMSI
     GKFKLVVEFV NSEIENYENF NHTVTNNGGI LNDLITVDYS NFSIAARTSH