ID A0A9W7ABZ9_9STRA Unreviewed; 368 AA.
AC A0A9W7ABZ9;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=TL16_g04611 {ECO:0000313|EMBL:GMH67170.1};
OS Triparma laevis f. inornata.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bolidophyceae; Parmales;
OC Triparmaceae; Triparma.
OX NCBI_TaxID=1714386 {ECO:0000313|EMBL:GMH67170.1, ECO:0000313|Proteomes:UP001162640};
RN [1] {ECO:0000313|Proteomes:UP001162640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=37420035; DOI=10.1038/s42003-023-05002-x;
RA Ban H., Sato S., Yoshikawa S., Yamada K., Nakamura Y., Ichinomiya M.,
RA Sato N., Blanc-Mathieu R., Endo H., Kuwata A., Ogata H.;
RT "Genome analysis of Parmales, the sister group of diatoms, reveals the
RT evolutionary specialization of diatoms from phago-mixotrophs to
RT photoautotrophs.";
RL Commun. Biol. 6:0-0(2023).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GMH67170.1}.
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DR EMBL; BLQM01000128; GMH67170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W7ABZ9; -.
DR Proteomes; UP001162640; 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 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}.
FT DOMAIN 25..150
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 151..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 38703 MW; DC58B6CC18E8CB8B CRC64;
MNGLNLQQMM AMMQQGQAGG GDTSSSLASL CSFKAGRCTA SPQPDGSLKI TPMKGKGTLN
LTRTNASHSE GEGMIHLQWE DRKTKETPDK FIIFPSEAKF EEIQTGTETD TPVCMLSYMG
NSERRNFYWV QELEFDKENI NEINTLMNDP AKAKKKADPE GAESSAPPSS TSSPTSAPAS
STTDTSMDVV SNDVISSANL PADTSVADIS TTTPSATTPA PPAGGVDVQN LQSILSGLGL
PAASSSPSPT ASITTPAAPA APSKTTGGIT LSDLQSAMSL AQEGEAKLTD YVSYSEVERQ
GLLENSTTVD KLTALLPEGQ RTKEDLVKTL RSPQVLSALG SLSNALNGPE FASVLANFDL
QLGEEEQR
//
