ID S8AV13_PENO1 Unreviewed; 390 AA.
AC S8AV13;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 05-FEB-2025, entry version 31.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=PDE_00631 {ECO:0000313|EMBL:EPS25697.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25697.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS25697.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB644408; EPS25697.1; -; Genomic_DNA.
DR AlphaFoldDB; S8AV13; -.
DR STRING; 933388.S8AV13; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_4_0_1; -.
DR OrthoDB; 340431at2759; -.
DR PhylomeDB; S8AV13; -.
DR Proteomes; UP000019376; 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 FunFam; 1.10.2020.20:FF:000004; WGS project CABT00000000 data, contig 2.6; 1.
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:UP000019376}.
FT DOMAIN 1..133
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 139..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 41805 MW; 90474E60B7819F96 CRC64;
MSSAPIITFK AGICDFDGSS NPAIVKPKPT PGYIYLYSED DLMHFCWRPR NSPLSEPELD
LVMIPSDGSF TPYRPPGRNS INGRVFVLKF SSSSQRYLFW LQSQTQHDNG DLSWFSPRDL
KLGEIVDVLL QGEDVDVEHE IANLPRPSPG GDDDETMEDV EGTHHDPNHN HGGSSGGAGP
DATGGDIREE GEESREGGAD GGRAASSGDP SLVVQDFLRS LGGGQQDQAQ SQGPERPSTT
LQDLLTPPST LPFIEAADES NVDHLLSFLP PALLLLAQGN AEAAEAAEAE TDSDLAQAAL
LSLDLSQKKD ILRRVLRSPQ FMQSLASLTV ALRDGGLPSI SEALQIPVTN GGFMRRGGVP
LGGGDAVEAF LDGVRQHVKQ EDQSGHMETD
//
