ID Q6CUT2_KLULA Unreviewed; 345 AA.
AC Q6CUT2;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=KLLA0C02475p {ECO:0000313|EMBL:CAH01158.1};
GN ORFNames=KLLA0_C02475g {ECO:0000313|EMBL:CAH01158.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH01158.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAH01158.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the UFD1 family.
CC {ECO:0000256|ARBA:ARBA00006043}.
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DR EMBL; CR382123; CAH01158.1; -; Genomic_DNA.
DR RefSeq; XP_452307.1; XM_452307.1.
DR AlphaFoldDB; Q6CUT2; -.
DR STRING; 284590.Q6CUT2; -.
DR PaxDb; 284590-Q6CUT2; -.
DR GeneID; 2892535; -.
DR KEGG; kla:KLLA0_C02475g; -.
DR eggNOG; KOG1816; Eukaryota.
DR HOGENOM; CLU_037790_1_0_1; -.
DR InParanoid; Q6CUT2; -.
DR OMA; VCMIETD; -.
DR Proteomes; UP000000598; Chromosome C.
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:UP000000598};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38487 MW; D093393DA411EC22 CRC64;
MFSGFSGYGN AYANIPQRLE EFFRCYPIAM MNDNIRKDDA NYGGKIFLPP SALNKLTLLN
VRYPMLFELK SQESGKVTHG GVLEFIAEEG RVYLPQWMME TLEIQPGSVL QICSTDVPLG
QFVKLEPQSV DFLDISDPKA VLERVLRNFS TLTIDDIIEI SYNNKVYRIR ILEVKPESSS
KSICVIETDL VTDFAPPVGY VEPDYKSQKK QTPSFDPSIK GLGSMSKRIN YAEILDPTDK
DKSFHGEGQK LSGKAIKPKE DDIKEISVSL DGNPAPLNLP EGQLFFGFPY VPPKSDDGED
NEIASSKVFQ GEGKSLRQSA KRKDKGSHQG SKTKAPKSPE VIEID
//
