ID A0A430QMT2_SCHBO Unreviewed; 419 AA.
AC A0A430QMT2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
DE SubName: Full=26S proteasome regulatory subunit N13 {ECO:0000313|EMBL:RTG88956.1};
GN ORFNames=DC041_0001916 {ECO:0000313|EMBL:RTG88956.1};
OS Schistosoma bovis (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6184 {ECO:0000313|EMBL:RTG88956.1, ECO:0000313|Proteomes:UP000290809};
RN [1] {ECO:0000313|EMBL:RTG88956.1, ECO:0000313|Proteomes:UP000290809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAN1997 {ECO:0000313|EMBL:RTG88956.1,
RC ECO:0000313|Proteomes:UP000290809};
RA Oey H., Zakrzewski M., Gobert G., Gravermann K., Stoye J., Jones M.,
RA Mcmanus D., Krause L.;
RT "Genome sequence of the bovine parasite Schistosoma bovis Tanzania.";
RL PLoS Pathog. 0:0-0(2019).
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:RTG88956.1}.
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DR EMBL; QMKO01001537; RTG88956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430QMT2; -.
DR STRING; 6184.A0A430QMT2; -.
DR Proteomes; UP000290809; 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, ECO:0000313|EMBL:RTG88956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290809}.
FT DOMAIN 14..127
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 252..367
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 190..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 45798 MW; DA8F44CAD71ECA26 CRC64;
MSGRTALFGR PQQSQTRHLL QFKAGKMTIG DDNWVHADPR KGWVYVYQSG DGKLHFCWID
RKTFLVEDNF VINAKQAEFQ KIPQCTTGRV YLLKFKGPKH FFIWMQEPNG KNDSDICSRI
NDYIRSPPAQ TTTLSSDWLS RFESLNQLSH SDILALLSMG VGLGGGLTSE SDISSAQANA
VTIGRHLNTG HLDESNVSTP VIGTTATPSS GTSSTGGNSL RPSTTDKRLE AGKIQLQDLR
NILSSISTGM RSSSNDAKVE LNDVLNVDNL HSLLNKPDIQ ERLLPHLPPL DPESASTNDL
ENITANIQSS QFKTTLKSFS AAFRTGELAP VLAQFNLGIK ADEAARRGDL VAFSNALQGK
TTDTTSQPSN DSGSNVTQST TSQESSKDKS DHKKEGKTIA DTKADKKDES FDDNKMDTD
//