GenomeNet

Database: UniProt
Entry: A0A836EVD0_9HYME
LinkDB: A0A836EVD0_9HYME
Original site: A0A836EVD0_9HYME 
ID   A0A836EVD0_9HYME        Unreviewed;       398 AA.
AC   A0A836EVD0;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   18-JUN-2025, entry version 14.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
DE   Flags: Fragment;
GN   Name=Rpn13 {ECO:0000313|EMBL:KAG5308678.1};
GN   ORFNames=G6Z75_0011418 {ECO:0000313|EMBL:KAG5308678.1};
OS   Acromyrmex insinuator.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=230686 {ECO:0000313|EMBL:KAG5308678.1, ECO:0000313|Proteomes:UP000667349};
RN   [1] {ECO:0000313|EMBL:KAG5308678.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BGI-DK2013a {ECO:0000313|EMBL:KAG5308678.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KAG5308678.1};
RA   Bi X.;
RT   "Relaxed selection underlies rapid genomic changes in the transitions from
RT   sociality to social parasitism in ants.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC       the deubiquitinating activity associated with the 26S proteasome.
CC       {ECO:0000256|ARBA:ARBA00054744}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ADRM1 family.
CC       {ECO:0000256|ARBA:ARBA00009216}.
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:KAG5308678.1}.
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DR   EMBL; JAANHZ010000648; KAG5308678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A836EVD0; -.
DR   Proteomes; UP000667349; 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   CDD; cd13314; PH_Rpn13; 1.
DR   FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000667349}.
FT   DOMAIN          14..127
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          240..366
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          120..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..198
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..243
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..371
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..398
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAG5308678.1"
FT   NON_TER         398
FT                   /evidence="ECO:0000313|EMBL:KAG5308678.1"
SQ   SEQUENCE   398 AA;  42710 MW;  93F191A5341F6791 CRC64;
     MSSGALFGNN ASRGASKNLV EFKAGKMTVK GKMVYPDTRK GQLYVYQSDD SLMHFCWKDR
     TTGVVEDDLI IFPDDCEFKH VPQCKTGRVY LLRFKSSNKK FFFWLQDLKT DKDEEHCRKI
     NDVLNNPPTP GSQRSGGTNA EGDLQNLLNN MSQQQLIQLF GGVGQIGGLG SLLGTMNRPH
     GVQSTRASTT TSSTPATTNV TRPPHSLTPG PNTDSKSSSN NKSSTRTTTP STPAATAAAP
     SNRIQLSDLQ NFLSEIPTPS RTEPAVQRGV ATELTNAIPT AISTTESLES AMNVHLPPGD
     NLSTTLSSPQ FSQALSMFWS ALQSGQAGPV IRQFGLGSDA VNAASSGNIE EFVSALESEA
     KNGQGQQAQQ GQDDKNKKQS SAASPDKKDD DDEGMALD
//
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