ID A0A815EZV0_ADIRI Unreviewed; 419 AA.
AC A0A815EZV0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 13.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=XAT740_LOCUS29810 {ECO:0000313|EMBL:CAF1319094.1};
OS Adineta ricciae (Rotifer).
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Adinetida; Adinetidae; Adineta.
OX NCBI_TaxID=249248 {ECO:0000313|EMBL:CAF1319094.1, ECO:0000313|Proteomes:UP000663828};
RN [1] {ECO:0000313|EMBL:CAF1319094.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
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:CAF1319094.1}.
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DR EMBL; CAJNOR010002619; CAF1319094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A815EZV0; -.
DR Proteomes; UP000663828; 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; 1.10.2020.20:FF:000001; Proteasomal ubiquitin receptor ADRM1; 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:UP000663828}.
FT DOMAIN 11..124
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 296..408
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 123..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..268
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 44169 MW; 79746FFF306AC220 CRC64;
MSLFGGMTSQ ARSRNLVEFK AGKMNLRGNM VHPDTRKGLV YLYQGNDMLM HFCWKERASN
TAEDDLVIFP DEIEFKKVTQ NTTGRVYILK WRSNARKLFF WMQEPKEDKD EEWCKKINEM
LNHPPTPGFG DDSNSSGGLG GGAHPLQSLM DRMTGGSGAG GIDPNDLSNV LRGMNPNDLA
SLLSSVGSGG GAPGLMQGSH RDTFGQQTPD SRPNTAPAAT RSSGAATATT GAAAASSTRP
SGSSSKPRNG GTSSSPSTAG GASSATSGGP KGGPIQMSAL SNILANLGGG AAGQSAAASK
PAIDLYDIMT TENLIPILSK KEVQETLRSH LPDGSTIPGT EKELRDSIQS PQFRQAVSTF
GVALQTGQLG PVLAQFGLPE EAITAANQGD IQAFAQAMEK HYKKDNDEKK PSDNTMDTS
//
