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Database: UniProt
Entry: A0A150VDC7_9PEZI
LinkDB: A0A150VDC7_9PEZI
Original site: A0A150VDC7_9PEZI 
ID   A0A150VDC7_9PEZI        Unreviewed;       370 AA.
AC   A0A150VDC7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=Ubiquitin fusion degradation protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M433DRAFT_61085 {ECO:0000313|EMBL:KYG48480.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48480.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG48480.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG48480.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the UFD1 family.
CC       {ECO:0000256|ARBA:ARBA00006043}.
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:KYG48480.1}.
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DR   EMBL; JPDO01000047; KYG48480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VDC7; -.
DR   STRING; 766039.A0A150VDC7; -.
DR   Proteomes; UP000075602; 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:UP000075602};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   REGION          202..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  40381 MW;  F858B2979A5A5651 CRC64;
     MSYYFQDDDM GIYQRAMLAR GGGRPRRFDE YYRCYPIAMM PGPERETANH GGKIFLPASA
     LDKLTQLHIT YPMLFELING AKSKSTHAGV LEFTAEEGRC YLPYWLMQTL LLEPGDLLQI
     KSTDLSPGSF IKLQPQNTNF LEISDPKAVL ETSFRNFSCL TVGDIFTFSY NDTIYEIAVL
     EVKPDSESHA ISVQETDLEV DFAPPVGYQE PAKTSGTSTP RSIGSTMASR GGMVHTEGSM
     AQAINYSAIA PSSSTAAVGH SRSTSAFAGS GNRLVPKKGK SSTVASTPAS TPRTSTPVPG
     TSSTPADSAQ HKTAQRRNGP QPLRLPPGKL FFGYEIKPLK NKEAQAAAEA EQRNQFKGDG
     QTLRKKKDQK
//
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