ID A0A395RGB6_FUSSP Unreviewed; 389 AA.
AC A0A395RGB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 05-FEB-2025, entry version 18.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=FSPOR_11550 {ECO:0000313|EMBL:RGP59137.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP59137.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP59137.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP59137.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP59137.1}.
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DR EMBL; PXOF01000234; RGP59137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RGB6; -.
DR STRING; 5514.A0A395RGB6; -.
DR Proteomes; UP000266152; 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 FunFam; 2.30.29.70:FF:000009; WGS project CABT00000000 data, contig 2.6; 1.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 1..137
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 138..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 41675 MW; 50C859C19B2D0DEB CRC64;
MPISPIITFK AGQCEVDTSS KPYKVKPQSE PGYIYLYSED DLVHFCWRKR SEPLDNPELD
LIMVPTDGSF TPYESTTSSE PTSKTDGRIF VLKFSSSSQR YIFWLQSKPQ SENGDPAYYS
PRDRKIGDIV HRLLQGEEVE VAEEMSTVRN DDQDDDEDET MEDAENQRPR EQRGSGGAGP
DATGGDVREE GEGSREGGAD GARAVSSSAP GTDASAAVRS FLDSLRGQSG LSGGQQQQQG
ADKAYPYLNH LLPTSITVPM IDSAPEDFAD TLISFLPPAV VVLASGSAGA VDGKSDPPAT
TVEAAKASLS LDDKRTLLKK VLRSPQFNQA LASLTMAIRD GGLPSIADAL GVKVQDGGYL
RGSGMPLGGG QAVEAFVNGV KKTVEEEKK
//
