ID   FCR1_CANAX              Reviewed;         517 AA.
AC   O93870;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Fluconazole resistance protein 1;
GN   Name=FCR1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476 {ECO:0000312|EMBL:AAC98670.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   PubMed=9864335; DOI=10.1128/jb.181.1.231-240.1999;
RA   Talibi D., Raymond M.;
RT   "Isolation of a putative Candida albicans transcriptional regulator
RT   involved in pleiotropic drug resistance by functional complementation of a
RT   pdr1 pdr3 mutation in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 181:231-240(1999).
CC   -!- FUNCTION: Transcription factor that acts as a negative regulator of
CC       fluconazole resistance in C.albicans. Also confers fluconazole
CC       resistance in S.cerevisiae by activation of the PDR5 gene.
CC       {ECO:0000269|PubMed:9864335}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AF057038; AAC98670.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93870; -.
DR   PRIDE; O93870; -.
DR   VEuPathDB; FungiDB:C3_06850W_A; -.
DR   VEuPathDB; FungiDB:CAWG_02995; -.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   4: Predicted;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..517
FT                   /note="Fluconazole resistance protein 1"
FT                   /id="PRO_0000114949"
FT   DNA_BIND        26..52
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          106..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  56875 MW;  FF71BCE1AED5F21B CRC64;
     MSDDHSIHSH TQGLHHIKKK RVGKACDSCR IKKTKCDGKK PCNRCTLDNK ICVFTEKKKT
     KEKKHPSGYV ELLEARLDIL TRSLEKLIEL SRPHLQFIDD IITEEKSVDQ EKSSPASSTP
     NSSSSDHHDD VEEQNSTGVV APINKVVSYL IKEQGLLKNI PLEWEQGTEI AANFDPNRNL
     KSSSRLFAEH KGEAFIGSPV TSPQQMPTSN PFRRTSMFKE ELESPSSDHY NESIFSQSVD
     EPYIKKEPNS AQFSKGTFSP QQQQLQQQQQ MLNQFSLNTS RDISDIESDS SNKEDGLNSG
     SVSPPTSNYR SFSLFSDSNG EPILGKTSSL TSLTNKYENH SLSSPQTAIN PVFNNSTTGP
     ILTTLRRNSS SHSQKTLGSI QLQQKPRGSV HKPVRNHSRV SSFDKRMEST ATAAATVAAV
     SGSVQLSQNT TPQNLPHLDN SQNNNYLRDN GMNNIGAGSV GGGLTFGAPS FTQPLSPSDD
     AIVYPTNQFT NRPATVSTFG GGLDVLVDNS LDPFFNI