ID   A0A165RZ24_9APHY        Unreviewed;       482 AA.
AC   A0A165RZ24;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   SubName: Full=UFD1-domain-containing protein {ECO:0000313|EMBL:KZT71328.1};
GN   ORFNames=DAEQUDRAFT_125376 {ECO:0000313|EMBL:KZT71328.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT71328.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT71328.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT71328.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the UFD1 family.
CC       {ECO:0000256|ARBA:ARBA00006043}.
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DR   EMBL; KV429046; KZT71328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165RZ24; -.
DR   STRING; 1314783.A0A165RZ24; -.
DR   OrthoDB; 1125766at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 2.40.40.50; Ubiquitin fusion degradation protein UFD1, N-terminal domain; 1.
DR   InterPro; IPR004854; Ufd1-like.
DR   InterPro; IPR042299; Ufd1-like_Nn.
DR   PANTHER; PTHR12555; UBIQUITIN FUSION DEGRADATON PROTEIN 1; 1.
DR   PANTHER; PTHR12555:SF13; UBIQUITIN RECOGNITION FACTOR IN ER-ASSOCIATED DEGRADATION PROTEIN 1; 1.
DR   Pfam; PF03152; UFD1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   REGION          216..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..482
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  51786 MW;  D9B521CFDF4273EC CRC64;
     MDMNPFGVGP AGLFAQLAGG FGPVGHGLRP PPARSYDEYF RAYSVAMLPG RERENVSYGG
     KIIMPPSALA SITQMDLEPP WMFKLRNPEN PAASTHAGVL EFIAEEGCVH LPQWMMKTLR
     LNEGDPIRVT GAELPKGTFV KLQAQSTMFL EISDPKAVLE QALRNFSVLT QGDIIDISYN
     SIVFSLLVME TKPGGEGISV LNTDLEVDFA APVGYVEPER PKPPPPSTMA SKLNIDVNSQ
     TPGSSRPSSS LGGSFGPTGS RNVAVSKGGD QWESFKGKGE TLGGRKTKGK GISQRPIEET
     VTESKITRTE SVLIHCHCSL TDLTFRFSKH KIVTSDLLDA EASAPAPLNL PFGKLFFGYR
     IVPYQPPDKS DDKQKSQPFT GTGNALNGRP TGQTLSEATS SKDKGKGKEE PSSNTSWGSG
     GRTLGTRSTP VNVPGSGGRP AAPANVPAIR RRSPSPEPER AYDTDEMESD DESVIYISSD
     EE
//