ID   RPN11_ASHGO             Reviewed;         311 AA.
AC   Q750E9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=26S proteasome regulatory subunit RPN11;
GN   Name=RPN11; OrderedLocusNames=AGR006W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; AE016820; AAS54495.1; -; Genomic_DNA.
DR   RefSeq; NP_986671.1; NM_211733.1.
DR   AlphaFoldDB; Q750E9; -.
DR   SMR; Q750E9; -.
DR   STRING; 33169.AAS54495; -.
DR   MEROPS; M67.001; -.
DR   EnsemblFungi; AAS54495; AAS54495; AGOS_AGR006W.
DR   GeneID; 4622970; -.
DR   KEGG; ago:AGOS_AGR006W; -.
DR   eggNOG; KOG1555; Eukaryota.
DR   HOGENOM; CLU_052991_0_1_1; -.
DR   InParanoid; Q750E9; -.
DR   OMA; VFQTRMM; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0031595; C:nuclear proteasome complex; IEA:EnsemblFungi.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0000266; P:mitochondrial fission; IEA:EnsemblFungi.
DR   GO; GO:0016559; P:peroxisome fission; IEA:EnsemblFungi.
DR   GO; GO:0043248; P:proteasome assembly; IEA:EnsemblFungi.
DR   GO; GO:1902906; P:proteasome storage granule assembly; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR035299; PSMD14.
DR   InterPro; IPR024969; Rpn11/EIF3F_C.
DR   PANTHER; PTHR10410:SF22; PTHR10410:SF22; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Proteasome;
KW   Reference proteome; Zinc.
FT   CHAIN           1..311
FT                   /note="26S proteasome regulatory subunit RPN11"
FT                   /id="PRO_0000213957"
FT   DOMAIN          32..167
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           114..127
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   311 AA;  35202 MW;  8E85814D0E1B34C6 CRC64;
     MDRLQRLMMS QRSNMIGAAA TEMPLDDTKE TVYISSLALL KMLKHSRAGV PMEVMGLMLG
     DFVDEYTVNV VDVFAMPQSG TGVSVEAVDD VFQAKMMDML KQTGRDQMVV GWYHSHPGFG
     CWLSSVDVDT QRSFEQLNSR AVAVVVDPIQ SVKGKVVIDA FRLISPATVV RNQEPRQTTS
     NVGLLNKPNI QSLIHGLNRH YYSLNIDYHK TSAELNMLMN LHKEQWQSGL KMHDYKEKER
     INLEATKKSV RIAEQYTKRI EEEKELTEDE LKTRYVGKQD PKKHLSETAE RVLEENIVSV
     LTAGVNSVAI K