(data stored in SCRATCH zone)

SWISSPROT: Q6FJU9_CANGA

ID   Q6FJU9_CANGA            Unreviewed;       214 AA.
AC   Q6FJU9;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 91.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62471.1};
GN   OrderedLocusNames=CAGL0M03399g {ECO:0000313|CGD:CAL0136287,
GN   ECO:0000313|EMBL:CAG62471.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62471.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   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 ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00388,
CC       ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS00805669}.
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DR   EMBL; CR380959; CAG62471.1; -; Genomic_DNA.
DR   RefSeq; XP_449495.1; XM_449495.1.
DR   ProteinModelPortal; Q6FJU9; -.
DR   STRING; 284593.XP_449495.1; -.
DR   EnsemblFungi; CAG62471; CAG62471; CAGL0M03399g.
DR   KEGG; cgr:CAGL0M03399g; -.
DR   CGD; CAL0136287; CAGL0M03399g.
DR   EuPathDB; FungiDB:CAGL0M03399g; -.
DR   eggNOG; KOG0416; Eukaryota.
DR   eggNOG; ENOG410XRC5; LUCA.
DR   HOGENOM; HOG000233452; -.
DR   InParanoid; Q6FJU9; -.
DR   KO; K10576; -.
DR   OMA; MRHPKEY; -.
DR   OrthoDB; EOG092C50OL; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJU9.
DR   SWISS-2DPAGE; Q6FJU9.
KW   ATP-binding {ECO:0000256|RuleBase:RU362109};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU362109,
KW   ECO:0000256|SAAS:SAAS00805691}.
FT   DOMAIN       27    138       UBIQUITIN_CONJUGAT_2.
FT                                {ECO:0000259|PROSITE:PS50127}.
FT   ACT_SITE     86     86       Glycyl thioester intermediate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00388}.
SQ   SEQUENCE   214 AA;  24433 MW;  A7DB82A1199ACC77 CRC64;
     MSGNSKRRIE TDVMKLLMSD HEVELVEDSM QEFHVKFYGP KDTPYEGGVW RLHVELPDNY
     PYKSPSIGFV NKIFHPNIDI ASGSICLDVI NSTWSPLYDL LNIVEWMLPG LLKEPNGSDP
     LNNEAANLQL KDKKVYEEKV REYIDKYATK ERYESQFGTP EDDEDDGDDA EMKDEDGDDD
     IDEPVSDLED ISDDNADPSE ELSDISDIEL SDED
//

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