(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJC9_CANGA

ID   Q6FJC9_CANGA            Unreviewed;      1515 AA.
AC   Q6FJC9;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 106.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62641.1};
GN   OrderedLocusNames=CAGL0M07293g {ECO:0000313|CGD:CAL0137191,
GN   ECO:0000313|EMBL:CAG62641.1};
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:CAG62641.1, 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 ABC transporter superfamily. ABCG
CC       family. PDR (TC 3.A.1.205) subfamily.
CC       {ECO:0000256|SAAS:SAAS00709344}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00434}.
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DR   EMBL; CR380959; CAG62641.1; -; Genomic_DNA.
DR   RefSeq; XP_449665.1; XM_449665.1.
DR   ProteinModelPortal; Q6FJC9; -.
DR   STRING; 284593.XP_449665.1; -.
DR   EnsemblFungi; CAG62641; CAG62641; CAGL0M07293g.
DR   KEGG; cgr:CAGL0M07293g; -.
DR   CGD; CAL0137191; CAGL0M07293g.
DR   EuPathDB; FungiDB:CAGL0M07293g; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   eggNOG; COG0842; LUCA.
DR   HOGENOM; HOG000162078; -.
DR   InParanoid; Q6FJC9; -.
DR   OMA; WMYWLTP; -.
DR   OrthoDB; EOG092C1HKF; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0005342; F:organic acid transmembrane transporter activity; IEA:EnsemblFungi.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010929; PDR_CDR_ABC.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14510; ABC_trans_N; 1.
DR   Pfam; PF06422; PDR_CDR; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJC9.
DR   SWISS-2DPAGE; Q6FJC9.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00555301};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Membrane {ECO:0000256|SAAS:SAAS00709359, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00555311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Repeat {ECO:0000256|SAAS:SAAS00709352};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00709342,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00709353,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00709346}.
FT   TRANSMEM    552    572       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    601    619       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    662    681       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    765    785       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1180   1201       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1213   1235       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1256   1283       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1295   1316       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1328   1344       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1450   1469       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      148    400       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      839   1088       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND     881    888       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   1515 AA;  171802 MW;  609DEB955E28E15B CRC64;
     MPASISSSII SKERKDDADT TSNSYADSVH SYENINRDDN EQQPVSTQLS RHLTQILSEE
     GGKERLESMA RVISTKTKAE MDKFEVNDMD FDLRMLLNYL RNRQLEQGIE PGDSGVAFKN
     LTAVGIDASA AYGPSVEEML RDTGKLPLTL INKLRRKKDS VPLRNIIQNC TGVVESGEML
     FVVGRPGAGC STLLKCISGE TSELVSVDGE FSYDGLDQEE MMKNYKGYVI YCPELDFHFP
     KITVKETIDF ALKCKTPRVR IDRMTRKQYV DNIRDMWCTV FGLRHTYATK VGNDFVRGVS
     GGERKRVSLV EAQAMNASIY SWDNATRGLD ASTALEFAQA IRTATNMMNN SAIVAIYQAG
     ENIYELFDKT TVLYNGKQIY FGPAKKAVQY FENMGWIKPP RMTSAEFLTS VTVDFENRTL
     DIKPGYEDTI PKSGFEFEEY WLNSPEYQEL LRHYDDYHAR HPAEETRERF DTAKKQMLQS
     GQRESSRYVV NYWSQVWYCM IRGFQRVKGD STYTKVYLSS FLIKGLIVGS MFHKIDNKSQ
     STTAGAYSRG GLLFYVLLFA SVTSLAEIAN SFSTRPIIVK HKSYSMYHIS AESLQEIITE
     LPTKFVAIIV LSLVTYWIPY LKFEAGAFFQ YILYLFTVQQ CTSFIFKFVA TITKDGVTAH
     AIGGLWVLML CVYAGFVLPL GEMHHWIKWL HFLNPLTYAF ESLVSTEFHH REMLCSQLIP
     SGPGYENVSV ANQICNAAGA IKGHMFVNGD TYIDRQYHFA YRHAWRSWGV NIVWTFGYIV
     FNVILSEFIK PVSGGGDLLL YKRGHMPEFG TENADARVAS REEMMETLNG PDVDLPKVIA
     AKDVFTWNHL NYTIPYDGAT RQLLSDVFGY VKPGKMTALM GESGAGKTTL LNVLAQRINM
     GVITGDMLVN SQSLPASFNR SCGYVAQADN HMAELSVRES LRFAAELRQP RSVPLEEKYE
     YVEKIIALLG MQNYAEALVG KTGRGLNVEQ RKKLSIGVEL VAKPSLLLFL DEPTSGLDSQ
     SAWSIVQFMR ALADSGQSIL CTIHQPSATL FEQFDRLLLL KKGGKMVYFG DIGENSSTLL
     NYFERQSGVK CGISENPAEY ILNCIGAGAT ASASADWHDL WQQSPECAAA RAELDELHKN
     LLSRPVTEDP ELVTKFAASY TTQMKCVLRR TMIQFWRSPV YIRAKFLECV SCALFVGLSY
     IAVNHSVGGA TEAFSSIFML LLIALAMINQ LHVFAYDSRE LYEVREAASN TFHWSVLLLC
     HYVVETGWST LCQFMCFICY YWPAGYSGRA SHAGFFFFFY VLIFPMYFVS YGLWILYMSP
     DVPSASMINS NLFAAMLLFC GILQPKEKMP GFWRGLMYNV SPFTYVVQAL VGPLVHDKKV
     VCNKNEFAIM DPPAGQTCGE YLRTYIGNNS GYLVNPQATS NCNYCPYSVQ DEVVARFNVK
     WSYRWRNFGF MWVYICFNIF AMLSCYYIMR VKVWSLKSVL DFKKWFNGPR KDRHEKDKSI
     FEKKPGDEEK VKQKF
//

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