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Database: UniProt
Entry: G0WH74_NAUDC
LinkDB: G0WH74_NAUDC
Original site: G0WH74_NAUDC 
ID   G0WH74_NAUDC            Unreviewed;       166 AA.
AC   G0WH74;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-FEB-2025, entry version 49.
DE   RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN   Name=NDAI0J02600 {ECO:0000313|EMBL:CCD27152.1};
GN   OrderedLocusNames=NDAI_0J02600 {ECO:0000313|EMBL:CCD27152.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD27152.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD27152.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., Oheigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; HE580276; CCD27152.1; -; Genomic_DNA.
DR   RefSeq; XP_003672395.1; XM_003672347.1.
DR   AlphaFoldDB; G0WH74; -.
DR   STRING; 1071378.G0WH74; -.
DR   GeneID; 11494489; -.
DR   KEGG; ndi:NDAI_0J02600; -.
DR   eggNOG; KOG3037; Eukaryota.
DR   HOGENOM; CLU_115505_0_0_1; -.
DR   OMA; IPGETMW; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000000689; Chromosome 10.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:EnsemblFungi.
DR   GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR   GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR006773; Rpn13/ADRM1.
DR   InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR   InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR   PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR   Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR   PROSITE; PS51917; PRU; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          3..145
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   REGION          145..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   166 AA;  18817 MW;  055D85E5065C2E6F CRC64;
     MPATKVTNLT FRAGVAKYDE DTKICTPLPV QGQISIKKAG GDGEDEEDEE DEMSLYELIW
     KPMEKVVGDN VEYCQELNLM LIPDDTQWVS VKSCKNGRVF ALVYSSNQKY FFWLQEKNAT
     NLSLNELSEK DKCIFKNLAS ILSTEGGDEQ EEVKDEKKED IAMIDA
//
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