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Database: UniProt
Entry: A0A5N6TSL1_9EURO
LinkDB: A0A5N6TSL1_9EURO
Original site: A0A5N6TSL1_9EURO 
ID   A0A5N6TSL1_ASPAV        Unreviewed;       387 AA.
AC   A0A5N6TSL1;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   SubName: Full=Putative adhesion regulating molecule {ECO:0000313|EMBL:KAE8149290.1};
GN   ORFNames=BDV25DRAFT_4250 {ECO:0000313|EMBL:KAE8149290.1};
OS   Aspergillus avenaceus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=36643 {ECO:0000313|EMBL:KAE8149290.1, ECO:0000313|Proteomes:UP000325780};
RN   [1] {ECO:0000313|EMBL:KAE8149290.1, ECO:0000313|Proteomes:UP000325780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 18842 {ECO:0000313|EMBL:KAE8149290.1,
RC   ECO:0000313|Proteomes:UP000325780};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
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; ML742128; KAE8149290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6TSL1; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000325780; 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; 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; 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:UP000325780}.
FT   DOMAIN          1..134
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   REGION          137..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  41650 MW;  7E40C7C4D1FE711C CRC64;
     MSITPIITFK AGICDLDTSG DTQLVKPKST PGYIYLYSED ELVHFCWRPR TASHTEPELD
     LVMVPSDGSF TPYRPAGKAN PTNGRIYVLK FSSSSQRYLF WLQSKSQHEE EDPSFFSPRD
     VRLGDIVNTL LQGEDVDVEH EIANLPRGPG GGDDDETMED VEGVDHNPNH NHGGNSGGAG
     PDATGGDIRE EGEESREGGA DGGRAAAADS NPSSVVQNFL QSLQGGSAGS RSQDPERPFT
     TLQELLSPAA TLPFLEIADE KTVDNLLSFL PPTLLLLAQD VDDISSIDDP EIIEAVMASL
     DISQKKNILR KVLHSPQFTQ SLASLTVAIR DGGLPSISEA LKIPVENGGF MRRGGVPLGG
     GDAVEAFLRG VRGHVQDSPQ DNQMETD
//
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