ID A5DI96_PICGU Unreviewed; 354 AA.
AC A5DI96;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Ubiquitin fusion degradation protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGUG_02997 {ECO:0000313|EMBL:EDK38899.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38899.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK38899.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
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; CH408157; EDK38899.2; -; Genomic_DNA.
DR RefSeq; XP_001485268.1; XM_001485218.1.
DR AlphaFoldDB; A5DI96; -.
DR STRING; 294746.A5DI96; -.
DR GeneID; 5127419; -.
DR KEGG; pgu:PGUG_02997; -.
DR VEuPathDB; FungiDB:PGUG_02997; -.
DR eggNOG; KOG1816; Eukaryota.
DR HOGENOM; CLU_037790_1_0_1; -.
DR InParanoid; A5DI96; -.
DR OMA; VCMIETD; -.
DR OrthoDB; 1125766at2759; -.
DR Proteomes; UP000001997; 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:UP000001997};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT REGION 302..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 38857 MW; 0E7D19BC528983CB CRC64;
MFSGFGTGMF GTLGSFAPMN TKFEDYFRCY PVAMMPDNIR KDDANFGGKI FLPPSALNKL
TMLHIRYPML FELENEAESV KTHSGVLEFV AEEGRAYLPQ WMMATLNVSP GSLLKISNCD
LPLGSFVKIE PQSVDFLDIS DPKAVLENVL RKFSTLTVND IIEINYNDAT YGIKVLEAKP
ESSSQGICVV ETDLQTDFAP PVGYVEPEYK PAVKEPQSKP ITPSSVNRGV GAGTMANSIN
YAKIVAEQSN NTFKGSGQKL SGKPSQEATK TISMDDLDPN AAPVPLDLPS NQLFFGFPVQ
LPTPSYTPES TPEQQPTFGG VGQSLRQSKK RKDSNKNHPS LKNHERSPET IEID
//
