ID W3XM02_PESFW Unreviewed; 393 AA.
AC W3XM02;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 18-JUN-2025, entry version 41.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=PFICI_00852 {ECO:0000313|EMBL:ETS87024.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS87024.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KI912109; ETS87024.1; -; Genomic_DNA.
DR RefSeq; XP_007827624.1; XM_007829433.1.
DR AlphaFoldDB; W3XM02; -.
DR STRING; 1229662.W3XM02; -.
DR GeneID; 19265865; -.
DR KEGG; pfy:PFICI_00852; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_4_0_1; -.
DR InParanoid; W3XM02; -.
DR OMA; RSPQFMQ; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR Gene3D; 1.10.2020.20; -; 1.
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 InterPro; IPR038108; RPN13_DEUBAD_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:UP000030651}.
FT DOMAIN 1..137
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 143..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 41687 MW; 5B29EF9096E2F4D2 CRC64;
MSIQPIITFK AGICEVDPST KPYKVSAKPE KGYVYLYSED DLIHFCWRQR SSPIDEPDLD
LVMVPTDGHF VPHESHKQTN SASKTNGRVF VLKFMSSSQR HMFWMQSKPQ GRNGDPAWFS
PRDLKIGQIV DALLQGEEVD VQSELNSVVN NNNDDRPDDD EDDAMEDVQG HGDSNDPRGG
AGAGGAGSDA TGGDVREEGE GAREGGADGA RAAAGGNVDA ATAVRNLLNS LQGGLPGQGG
SGPSQGGEGK LYPMLSDLLT PPTTVPVAQD ATEEQLDELL DYLPPQVLIL SQQSDSGDAS
TEPTPAAVEA AKQAMSVGQK KALLVKVLRS PQFHQSLTSL TMALRDGGLP TIAEALSVKV
ENNGYMKGSS MPLGGGEAVE AFVEGVKKTV EKK
//
