ID G8BPD2_TETPH Unreviewed; 159 AA.
AC G8BPD2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 05-FEB-2025, entry version 46.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN Name=TPHA0B01910 {ECO:0000313|EMBL:CCE61863.1};
GN OrderedLocusNames=TPHA_0B01910 {ECO:0000313|EMBL:CCE61863.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61863.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE61863.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
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; HE612857; CCE61863.1; -; Genomic_DNA.
DR RefSeq; XP_003684297.1; XM_003684249.1.
DR AlphaFoldDB; G8BPD2; -.
DR STRING; 1071381.G8BPD2; -.
DR GeneID; 11535094; -.
DR KEGG; tpf:TPHA_0B01910; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_115505_0_0_1; -.
DR OMA; IPGETMW; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
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:UP000005666}.
FT DOMAIN 5..136
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 159 AA; 18196 MW; 88CAB1BB6AEE71BA CRC64;
MSTVKSIPKK IKFRAGIAKF DEVTKECIPL AVQGEIHLDA SEEESELGFY DFEWKPTEDV
NNPNNTPINL ILIPGETVFV PIKSCTTGRV FAIIFSSNEK YFFWLQEKNP SNLRVNELSS
NDKEIYQRIT AILTAFEDDE DNEEGKALLN EKEKDVEME
//
