ID C5M665_CANTT Unreviewed; 362 AA.
AC C5M665;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Ubiquitin fusion degradation protein 1 {ECO:0000313|EMBL:EER34485.1};
GN ORFNames=CTRG_01346 {ECO:0000313|EMBL:EER34485.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34485.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34485.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the UFD1 family.
CC {ECO:0000256|ARBA:ARBA00006043}.
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DR EMBL; GG692396; EER34485.1; -; Genomic_DNA.
DR RefSeq; XP_002547040.1; XM_002546994.1.
DR AlphaFoldDB; C5M665; -.
DR STRING; 294747.C5M665; -.
DR EnsemblFungi; CTRG_01346-t43_1; CTRG_01346-t43_1-p1; CTRG_01346.
DR GeneID; 8296648; -.
DR KEGG; ctp:CTRG_01346; -.
DR VEuPathDB; FungiDB:CTRG_01346; -.
DR eggNOG; KOG1816; Eukaryota.
DR HOGENOM; CLU_037790_1_0_1; -.
DR OrthoDB; 1125766at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0030894; C:replisome; IEA:EnsemblFungi.
DR GO; GO:1990112; C:RQC complex; IEA:EnsemblFungi.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IEA:EnsemblFungi.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0006274; P:DNA replication termination; IEA:EnsemblFungi.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IEA:EnsemblFungi.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:EnsemblFungi.
DR GO; GO:0072665; P:protein localization to vacuole; IEA:EnsemblFungi.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:EnsemblFungi.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
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:UP000002037};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT REGION 253..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 40347 MW; 904FA28629EFA3BC CRC64;
MFSSFGSSFG FGSPPPMNNK FEEYFRCYPV SMMPELIRKD DANYGGKIFL PPSALNKLTM
LHIRYPMLFE LKNEQNDKLT HSGVLEFIAE EGRTYLPQWM MSTLQLSPGS LIKITNCDLS
LGKFVKIEPQ SVDFLDISDP KAVLENVLRK FSTLTVNDII EVNYNDTIYG IKVLEVKPDN
TSQGICVVET DLETDFAPPV GYVEPEYKPK AIKPETTPID PSKVSRGAGA ATMAKSINYA
KLVADSGKVE KFTGSGQKLS GKTVETKKDE ETNKSYNIDD LDPNAPPVPL NLPENQLFFG
FPVVLPTPEE SEEGANDEFK KKQEAFSGSG QSLRQSKKRK DKSTNYPSLK NHSRSPDVIE
ID
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