ID A0A4Z1JPE6_9HELO Unreviewed; 386 AA.
AC A0A4Z1JPE6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 15.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=BELL_0389g00080 {ECO:0000313|EMBL:TGO73112.1};
OS Botrytis elliptica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=278938 {ECO:0000313|EMBL:TGO73112.1, ECO:0000313|Proteomes:UP000297229};
RN [1] {ECO:0000313|EMBL:TGO73112.1, ECO:0000313|Proteomes:UP000297229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Be9601 {ECO:0000313|EMBL:TGO73112.1,
RC ECO:0000313|Proteomes:UP000297229};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TGO73112.1}.
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DR EMBL; PQXM01000387; TGO73112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z1JPE6; -.
DR STRING; 278938.A0A4Z1JPE6; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000297229; 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:UP000297229}.
FT DOMAIN 1..138
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 149..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..188
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 41012 MW; FF9D2B87AC82EE13 CRC64;
MSISPIITFK AGKCEIDTSS LPHKVKPEAT PGYIYLWSED DLIHFQWRER SKRMDDDENM
DLLLPPTDAI FQPYDSNQTT EPTAKTNGRI FVLKFSSSSQ RYLFWMQSKP QARNGDASWF
SPRDLKIGQI VNSLLQGDEV DVEQEIAQVR GDEGGNDDQD ETMEDVEGHG DSSEHQGGSG
GAGAGATGGD VREEGASSRE AGADGGRAAG SGPSDAASVV QNFLNSLKGP GGAGMQQQSQ
TQMYTTLPDL LPNKVTIPSI DAATPAQVDN LLSYLPPTIL QLAQESASSL EGMADATSAT
ANAAMEALSL DQKKSVLKRV VRSPQFHQSL GSLTMAIRDG GLPSIADALG VELKNNGLVK
GGSVPLGGGE AVEAFVEGVK RSVEKK
//
