(data stored in ACNUC8465 zone)

SWISSPROT: Q6FK30_CANGA

ID   Q6FK30_CANGA            Unreviewed;       632 AA.
AC   Q6FK30;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 87.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62390.1};
GN   OrderedLocusNames=CAGL0M01606g {ECO:0000313|CGD:CAL0136711,
GN   ECO:0000313|EMBL:CAG62390.1};
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:CAG62390.1, 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).
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DR   EMBL; CR380959; CAG62390.1; -; Genomic_DNA.
DR   RefSeq; XP_449414.1; XM_449414.1.
DR   ProteinModelPortal; Q6FK30; -.
DR   STRING; 284593.XP_449414.1; -.
DR   EnsemblFungi; CAG62390; CAG62390; CAGL0M01606g.
DR   KEGG; cgr:CAGL0M01606g; -.
DR   CGD; CAL0136711; CAGL0M01606g.
DR   EuPathDB; FungiDB:CAGL0M01606g; -.
DR   eggNOG; KOG2013; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   HOGENOM; HOG000216514; -.
DR   InParanoid; Q6FK30; -.
DR   KO; K10685; -.
DR   OMA; RRYVNKM; -.
DR   OrthoDB; EOG092C3FGE; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IEA:EnsemblFungi.
DR   GO; GO:0016925; P:protein sumoylation; IEA:EnsemblFungi.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR030661; Uba2.
DR   InterPro; IPR019572; UBA_E1_Cys.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF10585; UBA_e1_thiolCys; 1.
DR   PIRSF; PIRSF039133; SUMO_E1B; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   4: Predicted;
DR   PRODOM; Q6FK30.
DR   SWISS-2DPAGE; Q6FK30.
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR039133-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039133-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR039133-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Zinc {ECO:0000256|PIRSR:PIRSR039133-3}.
FT   DOMAIN        9    441       ThiF. {ECO:0000259|Pfam:PF00899}.
FT   DOMAIN      300    368       UBA_e1_thiolCys. {ECO:0000259|Pfam:
FT                                PF10585}.
FT   NP_BIND      29     34       ATP. {ECO:0000256|PIRSR:PIRSR039133-2}.
FT   NP_BIND      61     64       ATP. {ECO:0000256|PIRSR:PIRSR039133-2}.
FT   NP_BIND     122    127       ATP. {ECO:0000256|PIRSR:PIRSR039133-2}.
FT   ACT_SITE    178    178       Glycyl thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR039133-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10132}.
FT   METAL       163    163       Zinc. {ECO:0000256|PIRSR:PIRSR039133-3}.
FT   METAL       166    166       Zinc. {ECO:0000256|PIRSR:PIRSR039133-3}.
FT   METAL       440    440       Zinc. {ECO:0000256|PIRSR:PIRSR039133-3}.
FT   METAL       443    443       Zinc. {ECO:0000256|PIRSR:PIRSR039133-3}.
FT   BINDING      53     53       ATP. {ECO:0000256|PIRSR:PIRSR039133-2}.
FT   BINDING      77     77       ATP. {ECO:0000256|PIRSR:PIRSR039133-2}.
SQ   SEQUENCE   632 AA;  71152 MW;  D44E20EA34DD07E7 CRC64;
     MAVRESNLVK ILGDEGYQKL RSTKCLLVGA GGIGSELLKD LVLMEVGEIH VVDLDTIDLS
     NLNRQFLFRQ KDIKKPKSAI AVNAVQSFSN SKLVPYQDNI MDTNVFPLHW FQQFDIIFNA
     LDNLAARRYV NKMTQFLSIP LLESGTSGFD GYIQPIIPGK TECFDCTKKE TPKTFPVCTI
     RSTPSLPVHC IVWAKNFLFG QLFSSSANDI ANEQMNEQDW GTDDVEEINR IKNETNELKE
     LQNIIISGDK SRIRDIISKL FIQDIEKLLL IENLWKTRAK PVALTPKQLQ ESEQLGDVNH
     LNLNEIWDLE TQIAKFTQIT SKLMDRYNTE SAIDFDKDDQ DTLEFVATAA NIRAHIFHIP
     VKSVFDIKQI AGNIIPAIAT TNAIIAGLSS LMSLRVLNLL KYAKVDKPTD INMAFTAKAS
     NLAQNRYLSN PKLVSPNKKC AVCSKVIRGV FKVTKNQMEK HSFMDFINAL TSTSKLSDDI
     SILDATTQRL LYDYDFEDLA EKKLVDLSLK NGSVLLITDE EEEAGLTKQI MEYYIEISDE
     SEDKIEQLSL PQIIPQFSIP SETADENGGG DMLQNDSLMT SNDQTTPIVV SESDAVENGN
     NKRPLTEELE YQSIKSRKLN PIEDDDELVI LD
//

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