(data stored in ACNUC8465 zone)

SWISSPROT: Q6FK23_CANGA

ID   Q6FK23_CANGA            Unreviewed;      1499 AA.
AC   Q6FK23;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 116.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62397.1};
GN   Name=CDR1 {ECO:0000313|CGD:CAL0136775};
GN   OrderedLocusNames=CAGL0M01760g {ECO:0000313|CGD:CAL0136775,
GN   ECO:0000313|EMBL:CAG62397.1};
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:CAG62397.1, 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.
CC       {ECO:0000256|SAAS:SAAS00709360}.
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; CAG62397.1; -; Genomic_DNA.
DR   RefSeq; XP_449421.1; XM_449421.1.
DR   ProteinModelPortal; Q6FK23; -.
DR   SMR; Q6FK23; -.
DR   STRING; 284593.XP_449421.1; -.
DR   EnsemblFungi; CAG62397; CAG62397; CAGL0M01760g.
DR   KEGG; cgr:CAGL0M01760g; -.
DR   CGD; CAL0136775; CDR1.
DR   EuPathDB; FungiDB:CAGL0M01760g; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   eggNOG; COG0842; LUCA.
DR   HOGENOM; HOG000162078; -.
DR   InParanoid; Q6FK23; -.
DR   KO; K08711; -.
DR   OMA; LMALIVM; -.
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; ISA:CGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015238; F:drug transmembrane transporter activity; ISA:CGD.
DR   GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IDA:CGD.
DR   GO; GO:0045117; P:azole transport; IMP:CGD.
DR   GO; GO:0035690; P:cellular response to drug; IMP:CGD.
DR   GO; GO:0046618; P:drug export; IEA:InterPro.
DR   GO; GO:0006855; P:drug transmembrane transport; ISA:CGD.
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; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR005285; Drug-R_PDR/CDR.
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   TIGRFAMs; TIGR00956; 3a01205; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK23.
DR   SWISS-2DPAGE; Q6FK23.
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    510    531       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    543    568       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    589    612       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    624    642       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    654    673       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    763    781       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1193   1213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1225   1244       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1264   1294       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1314   1337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1343   1362       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1466   1487       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      146    399       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      857   1099       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND     893    900       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   1499 AA;  169312 MW;  5F395297D29AAE84 CRC64;
     MSLASDKKDA DVASTTTTAQ DDDNLSTYHG FDHHVQDQVR QLARTLTQQS SLHQKKEHTL
     PEEGINPIFT NTEADDYNPR LDPTSDEFSS AEWVQNMSNI SNSDPDYYKP YSLGCYWKDL
     VATGESADIE YQANFLNGPY KGLKTVYNTV VPSTASSKDK NFKILKSMEG AVNPGELLVV
     LGRPGSGCTT LLKSISSNTH GFNIAKESTI SYSGMTPNDI RKHFRGEVVY NAEADIHLPH
     LTVYQTLLTV ARLKTPQNRL KGIDRETYAR HLTEVAMATF GLSHTRNTKV GNDLVRGVSG
     GERKRVSIAE VSICGSKFQC WDNATRGLDS ATALEFIRAL KVQASISNAA ATVAIYQCSQ
     DAYDLFDKVC VLYDGYQIYF GPAGKAKEYF QKMGYVSPER QTTADFLTAV TSPSERIINQ
     DYINRGIFVP QTPKEMWEYW RASEDHADLI KEIDSKLSDN YDANLAEIKD AHVARQSKRA
     RPSSPYTVSY GMQIKYLLIR NFWRIKQSSG VTLFMVIGNS SMAFILGSMF YKVMKHNTTS
     TFYFRGAAMF FAVLFNAFSS LLEIFSLFEA RPITEKHRTY SLYHPSADAF ASILSEVPAK
     LITAVCFNII YYFLVNFRRN GGVFFFYFLI NIVAVFAMSH LFRCVGSVSK TLSAAMVPAS
     MLLLGLSMYS GFAIPRTKIL GWSKWIWYIN PLAYLFESLM INEFHDRKFP CSQYIPSGSV
     YNNVPADSRI CSSVGAIRGN DYVLGDDFLR ESYSYLHKHK WRGFGIGLAY VIFFLVLYLI
     LCEYNEGAKQ KGEILVFPQN IVRRMKKERK LKNVSSDNDV EIGDVSDISD KKILADSSDE
     SEESGANIGL SQSEAIFHWR NLCYDVQIKK ETRRILNNVD GWVKPGTLTA LMGASGAGKT
     TLLDCLAERV TMGVITGEVS VDGKQRDDSF ARSIGYCQQQ DLHLKTSTVR ESLRFSAYLR
     QPADVSIEEK NQYVEDVIKI LEMEQYADAV VGVPGEGLNV EQRKRLTIGV ELAAKPKLLV
     FLDEPTSGLD SQTAWSICQL MKKLANHGQA ILCTIHQPSA ILMQEFDRLL FLQRGGKTVY
     FGDLGDGCKT MIDYFESHGS HKCPPDANPA EWMLEVVGAA PGSHANQDYH EVWRNSDEYQ
     KVQEELEWMS NELPKKNTNN SETVHKEFAT GVLYQCKLVS LRLFQQYWRS PDYLWSKFFL
     TIFNNIFIGF TFFKADRSLQ GLQNQMLAVF MFTVIFNPLL QQYLPSFVQQ RDLYEARERP
     SRTFSWKAFI VSQILVEIPW NILAGTVAFV IYYYAIGFYS NASVAHQLHE RGALFWLFSC
     AFYVYIGSLA LFCISFNQVA EAAANMASLM FTLSLSFCGV LVTPNGMPRF WIFMYRVSPL
     TYLIDGMLST GVANVAIKCS NYELLRFSPA ANLTCGEYLG PYLQTVKTGY IVDPSATDTC
     ELCPYSHTND FLSSVSSKYS RRWRNWGIFI CYIAFNYIAG IFLYWLARVP KKSGKLAKK
//

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