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Database: UniProt
Entry: A0A4S2MZL7_9PEZI
LinkDB: A0A4S2MZL7_9PEZI
Original site: A0A4S2MZL7_9PEZI 
ID   A0A4S2MZL7_9PEZI        Unreviewed;       303 AA.
AC   A0A4S2MZL7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   05-FEB-2025, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:TGZ82181.1};
GN   ORFNames=EX30DRAFT_340068 {ECO:0000313|EMBL:TGZ82181.1};
OS   Ascodesmis nigricans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascodesmidaceae; Ascodesmis.
OX   NCBI_TaxID=341454 {ECO:0000313|EMBL:TGZ82181.1, ECO:0000313|Proteomes:UP000298138};
RN   [1] {ECO:0000313|EMBL:TGZ82181.1, ECO:0000313|Proteomes:UP000298138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 389.68 {ECO:0000313|EMBL:TGZ82181.1,
RC   ECO:0000313|Proteomes:UP000298138};
RG   DOE Joint Genome Institute;
RA   Lutkenhaus R., Traeger S., Breuer J., Kuo A., Lipzen A., Pangilinan J.,
RA   Dilworth D., Sandor L., Poggeler S., Barry K., Grigoriev I.V.,
RA   Nowrousian M.;
RT   "Comparative genomics and transcriptomics to analyze fruiting body
RT   development in filamentous ascomycetes.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; ML220116; TGZ82181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2MZL7; -.
DR   STRING; 341454.A0A4S2MZL7; -.
DR   InParanoid; A0A4S2MZL7; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000298138; 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; IPR044867; DEUBAD_dom.
DR   InterPro; IPR006773; Rpn13/ADRM1.
DR   InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR   InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR   InterPro; IPR032368; RPN13_DEUBAD.
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   Pfam; PF16550; RPN13_C; 1.
DR   PROSITE; PS51916; DEUBAD; 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:UP000298138}.
FT   DOMAIN          2..125
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          182..302
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          123..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  33348 MW;  F1FC0DEF2BE6953B CRC64;
     MPPIRPIISI KAGKCNVDGT TVMPVEEPGI LYIYLNPDEE LHHLCWKPRS ATEPEIDLLI
     IPSDARFLPY EGNTTGRIFV LKFSSSSARH FFWLQSKAQH ESDAGFWSER DLEWGRRIDT
     ILQGDGDEEM GDAPVQSAEI EQEGEESRRG GEDGGRAQTQ PQGDMDLAAL IRSIQVPGGQ
     QQQQTLPPIS LHDLLSTSST LPTVDDLDEP AIIELAKNLP EGLFPDGSDI TAKRRIMKRV
     IQSPQFAQSL VSLTTAIREG GIAGVAESLR VPIDLNEARS GADLVEVFVK GVKKQAEKED
     TDQ
//
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