PDR1_CANGA
ID PDR1_CANGA Reviewed; 1107 AA.
AC Q6FXU7;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Transcription factor PDR1 {ECO:0000303|PubMed:15388433};
DE AltName: Full=Pleiotropic drug resistance protein 1 {ECO:0000303|PubMed:15388433};
GN Name=PDR1 {ECO:0000303|PubMed:15388433}; OrderedLocusNames=CAGL0A00451g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION.
RX PubMed=15388433; DOI=10.1128/aac.48.10.3773-3781.2004;
RA Vermitsky J.P., Edlind T.D.;
RT "Azole resistance in Candida glabrata: coordinate upregulation of multidrug
RT transporters and evidence for a Pdr1-like transcription factor.";
RL Antimicrob. Agents Chemother. 48:3773-3781(2004).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16078083; DOI=10.1007/s00294-005-0008-3;
RA Edlind T.D., Henry K.W., Vermitsky J.P., Edlind M.P., Raj S., Katiyar S.K.;
RT "Promoter-dependent disruption of genes: simple, rapid, and specific PCR-
RT based method with application to three different yeast.";
RL Curr. Genet. 48:117-125(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-297 AND PHE-575.
RX PubMed=16569856; DOI=10.1128/aac.50.4.1384-1392.2006;
RA Tsai H.F., Krol A.A., Sarti K.E., Bennett J.E.;
RT "Candida glabrata PDR1, a transcriptional regulator of a pleiotropic drug
RT resistance network, mediates azole resistance in clinical isolates and
RT petite mutants.";
RL Antimicrob. Agents Chemother. 50:1384-1392(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16803598; DOI=10.1111/j.1365-2958.2006.05235.x;
RA Vermitsky J.P., Earhart K.D., Smith W.L., Homayouni R., Edlind T.D.,
RA Rogers P.D.;
RT "Pdr1 regulates multidrug resistance in Candida glabrata: gene disruption
RT and genome-wide expression studies.";
RL Mol. Microbiol. 61:704-722(2006).
RN [6]
RP INDUCTION.
RX PubMed=18627600; DOI=10.1186/1471-2164-9-333;
RA Salin H., Fardeau V., Piccini E., Lelandais G., Tanty V., Lemoine S.,
RA Jacq C., Devaux F.;
RT "Structure and properties of transcriptional networks driving selenite
RT stress response in yeasts.";
RL BMC Genomics 9:333-333(2008).
RN [7]
RP FUNCTION.
RX PubMed=18385733; DOI=10.1038/nature06836;
RA Thakur J.K., Arthanari H., Yang F., Pan S.J., Fan X., Breger J.,
RA Frueh D.P., Gulshan K., Li D.K., Mylonakis E., Struhl K., Moye-Rowley W.S.,
RA Cormack B.P., Wagner G., Naeaer A.M.;
RT "A nuclear receptor-like pathway regulating multidrug resistance in
RT fungi.";
RL Nature 452:604-609(2008).
RN [8]
RP FUNCTION.
RX PubMed=19380598; DOI=10.1128/aac.01384-08;
RA Vandeputte P., Tronchin G., Rocher F., Renier G., Berges T., Chabasse D.,
RA Bouchara J.P.;
RT "Hypersusceptibility to azole antifungals in a clinical isolate of Candida
RT glabrata with reduced aerobic growth.";
RL Antimicrob. Agents Chemother. 53:3034-3041(2009).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LEU-280; LEU-344; GLY-348; SER-391; ASN-764;
RP ARG-772 AND GLY-943.
RX PubMed=20547810; DOI=10.1128/aac.00535-10;
RA Tsai H.F., Sammons L.R., Zhang X., Suffis S.D., Su Q., Myers T.G.,
RA Marr K.A., Bennett J.E.;
RT "Microarray and molecular analyses of the azole resistance mechanism in
RT Candida glabrata oropharyngeal isolates.";
RL Antimicrob. Agents Chemother. 54:3308-3317(2010).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=21131438; DOI=10.1128/ec.00277-10;
RA Paul S., Schmidt J.A., Moye-Rowley W.S.;
RT "Regulation of the CgPdr1 transcription factor from the pathogen Candida
RT glabrata.";
RL Eukaryot. Cell 10:187-197(2011).
RN [11]
RP FUNCTION.
RX PubMed=21193550; DOI=10.1128/ec.00073-10;
RA Caudle K.E., Barker K.S., Wiederhold N.P., Xu L., Homayouni R.,
RA Rogers P.D.;
RT "Genomewide expression profile analysis of the Candida glabrata Pdr1
RT regulon.";
RL Eukaryot. Cell 10:373-383(2011).
RN [12]
RP FUNCTION, MUTAGENESIS OF 947-SER--LEU-1107, AND BIOTECHNOLOGY.
RX PubMed=21129149; DOI=10.1111/j.1567-1364.2010.00702.x;
RA Goffa E., Bialkova A., Batova M., Dzugasova V., Subik J.;
RT "A yeast cell-based system for screening Candida glabrata multidrug
RT resistance reversal agents and selection of loss-of-function pdr1
RT mutants.";
RL FEMS Yeast Res. 11:155-159(2011).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF LEU-280; ARG-376; TYR-584; THR-588; PRO-822;
RP ASP-1082 AND GLU-1083.
RX PubMed=21408004; DOI=10.1371/journal.pone.0017589;
RA Ferrari S., Sanguinetti M., Torelli R., Posteraro B., Sanglard D.;
RT "Contribution of CgPDR1-regulated genes in enhanced virulence of azole-
RT resistant Candida glabrata.";
RL PLoS ONE 6:E17589-E17589(2011).
RN [14]
RP FUNCTION.
RX PubMed=23979762; DOI=10.1128/aac.02394-12;
RA Steier Z., Vermitsky J.P., Toner G., Gygax S.E., Edlind T., Katiyar S.;
RT "Flucytosine antagonism of azole activity versus Candida glabrata: role of
RT transcription factor Pdr1 and multidrug transporter Cdr1.";
RL Antimicrob. Agents Chemother. 57:5543-5547(2013).
RN [15]
RP FUNCTION.
RX PubMed=23229483; DOI=10.1128/aac.01278-12;
RA Noble J.A., Tsai H.F., Suffis S.D., Su Q., Myers T.G., Bennett J.E.;
RT "STB5 is a negative regulator of azole resistance in Candida glabrata.";
RL Antimicrob. Agents Chemother. 57:959-967(2013).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF LEU-280; ARG-376 AND THR-588.
RX PubMed=23460523; DOI=10.1128/iai.00074-13;
RA Vale-Silva L., Ischer F., Leibundgut-Landmann S., Sanglard D.;
RT "Gain-of-function mutations in PDR1, a regulator of antifungal drug
RT resistance in Candida glabrata, control adherence to host cells.";
RL Infect. Immun. 81:1709-1720(2013).
RN [17]
RP FUNCTION.
RX PubMed=25199772; DOI=10.1128/aac.03921-14;
RA Paul S., Bair T.B., Moye-Rowley W.S.;
RT "Identification of genomic binding sites for Candida glabrata Pdr1
RT transcription factor in wild-type and rho0 cells.";
RL Antimicrob. Agents Chemother. 58:6904-6912(2014).
RN [18]
RP INDUCTION.
RX PubMed=24645630; DOI=10.1080/08927014.2014.886108;
RA Fonseca E., Silva S., Rodrigues C.F., Alves C.T., Azeredo J., Henriques M.;
RT "Effects of fluconazole on Candida glabrata biofilms and its relationship
RT with ABC transporter gene expression.";
RL Biofouling 30:447-457(2014).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF ASP-243.
RX PubMed=25132632; DOI=10.1111/1567-1364.12193;
RA Faria-Ramos I., Tavares P.R., Farinha S., Neves-Maia J., Miranda I.M.,
RA Silva R.M., Estevinho L.M., Pina-Vaz C., Rodrigues A.G.;
RT "Environmental azole fungicide, prochloraz, can induce cross-resistance to
RT medical triazoles in Candida glabrata.";
RL FEMS Yeast Res. 14:1119-1123(2014).
RN [20]
RP FUNCTION.
RX PubMed=27303714; DOI=10.1128/msphere.00065-15;
RA Vale-Silva L.A., Moeckli B., Torelli R., Posteraro B., Sanguinetti M.,
RA Sanglard D.;
RT "Upregulation of the adhesin gene EPA1 mediated by PDR1 in Candida glabrata
RT leads to enhanced host colonization.";
RL MSphere 1:0-0(2016).
RN [21]
RP FUNCTION, INTERACTION WITH GAL11A, AND DOMAIN.
RX PubMed=26886795; DOI=10.1038/nature16963;
RA Nishikawa J.L., Boeszoermenyi A., Vale-Silva L.A., Torelli R.,
RA Posteraro B., Sohn Y.J., Ji F., Gelev V., Sanglard D., Sanguinetti M.,
RA Sadreyev R.I., Mukherjee G., Bhyravabhotla J., Buhrlage S.J., Gray N.S.,
RA Wagner G., Naeaer A.M., Arthanari H.;
RT "Inhibiting fungal multidrug resistance by disrupting an activator-Mediator
RT interaction.";
RL Nature 530:485-489(2016).
RN [22]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28700656; DOI=10.1371/journal.pone.0180990;
RA Nagayoshi Y., Miyazaki T., Shimamura S., Nakayama H., Minematsu A.,
RA Yamauchi S., Takazono T., Nakamura S., Yanagihara K., Kohno S., Mukae H.,
RA Izumikawa K.;
RT "Unexpected effects of azole transporter inhibitors on antifungal
RT susceptibility in Candida glabrata and other pathogenic Candida species.";
RL PLoS ONE 12:E0180990-E0180990(2017).
RN [23]
RP FUNCTION, INDUCTION, AND INTERACTION WITH GAL11A.
RX PubMed=29648590; DOI=10.1093/femsyr/foy038;
RA Tian Y., Gao N., Ni Q., Mao Y., Dong D., Huang X., Jiang C., Li Z.,
RA Zhang L., Wang X., Peng Y., Chen C.;
RT "Sequence modification of the master regulator Pdr1 interferes with its
RT transcriptional autoregulation and confers altered azole resistance in
RT Candida glabrata.";
RL FEMS Yeast Res. 18:0-0(2018).
RN [24]
RP FUNCTION, INDUCTION, DOMAIN, AND MUTAGENESIS OF 255-ASN--SER-968; ARG-376;
RP TYR-584; PRO-822 AND ASP-1082.
RX PubMed=29363861; DOI=10.1111/mmi.13913;
RA Khakhina S., Simonicova L., Moye-Rowley W.S.;
RT "Positive autoregulation and repression of transactivation are key
RT regulatory features of the Candida glabrata Pdr1 transcription factor.";
RL Mol. Microbiol. 107:747-764(2018).
RN [25]
RP FUNCTION.
RX PubMed=29581110; DOI=10.1128/aac.00153-18;
RA Hou X., Xiao M., Wang H., Yu S.Y., Zhang G., Zhao Y., Xu Y.C.;
RT "Profiling of PDR1 and MSH2 in Candida glabrata bloodstream isolates from a
RT multicenter study in China.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
RN [26]
RP INDUCTION.
RX PubMed=29507891; DOI=10.1128/msphere.00466-17;
RA Whaley S.G., Caudle K.E., Simonicova L., Zhang Q., Moye-Rowley W.S.,
RA Rogers P.D.;
RT "Jjj1 is a negative regulator of Pdr1-mediated fluconazole resistance in
RT Candida glabrata.";
RL MSphere 3:0-0(2018).
RN [27]
RP FUNCTION, AND MUTAGENESIS OF LEU-344; GLY-346; PRO-927 AND GLY-1099.
RX PubMed=29464833; DOI=10.1111/myc.12756;
RA Ni Q., Wang C., Tian Y., Dong D., Jiang C., Mao E., Peng Y.;
RT "CgPDR1 gain-of-function mutations lead to azole-resistance and increased
RT adhesion in clinical Candida glabrata strains.";
RL Mycoses 61:430-440(2018).
CC -!- FUNCTION: Master transcriptional regulator of a pleiotropic drug
CC resistance network that contributes to the azole resistance of clinical
CC isolates and petite mutants (PubMed:15388433, PubMed:16569856,
CC PubMed:16803598, PubMed:19380598, PubMed:20547810, PubMed:21131438,
CC PubMed:21193550, PubMed:21129149, PubMed:23979762, PubMed:23229483,
CC PubMed:28700656, PubMed:29648590, PubMed:29363861, PubMed:29581110).
CC Regulates the efflux of rhodamine 6G (PubMed:16569856). Regulates both
CC constitutive and drug-induced expression of the pleiotropic ABC efflux
CC transporter CDR1 (PubMed:16569856, PubMed:23979762, PubMed:23229483).
CC Commonly regulated genes include also those encoding ABC transporters
CC PDH1, SNQ2, and YOR1, a phospholipid biosynthetic enzyme (PDR16),
CC seven-transmembrane (TM) domain-containing proteins (RTA1 and RSB1), an
CC oxidoreductase (YMR102c-like), a sphingolipid biosynthetic enzyme
CC (IPT1), and a transcription factor (RPN4). Second, along with this
CC common core of regulated genes, interesting unique genes including
CC genes encoding an ABC transporter likely localized to the vacuolar
CC membrane (YBT1), proteins involved in DNA repair (REV1 and MEC3), the
CC mitochondrially targeted proteins YIM1 and PUP1, 3 oxidoreductases
CC (OYE2, YIR036c-like, and YNL134c-like proteins), a major facilitator
CC superfamily member (QDR2), a carbonic anhydrase (NCE103), an alcohol
CC acetyltransferase (ATF2), and a transcription factor (HAPI)
CC (PubMed:25199772). Activates transcription of target genes in response
CC to direct binding to specific xenobiotics by a discrete transferable
CC ligand-binding domain (PubMed:18385733). Stimulates gene expression of
CC target genes via binding to 5'-TCCGYGGA-3' elements called pleiotropic
CC drug response elements (PDREs) (PubMed:21131438). PDR1 is recruited to
CC the target promoters by mediator subunit GAL11A via its interaction
CC with the KIX domain of GAL11A (PubMed:21131438, PubMed:26886795).
CC Modulates the interaction with host cells in ways that may contribute
CC to increased virulence (PubMed:21408004, PubMed:23460523,
CC PubMed:29464833). Regulates specific cell wall adhesins and in
CC particular EPA1, explaining the increase in adherence to epithelial
CC cells in gain-of-function mutants (PubMed:27303714, PubMed:29464833).
CC {ECO:0000269|PubMed:15388433, ECO:0000269|PubMed:16569856,
CC ECO:0000269|PubMed:16803598, ECO:0000269|PubMed:18385733,
CC ECO:0000269|PubMed:19380598, ECO:0000269|PubMed:20547810,
CC ECO:0000269|PubMed:21129149, ECO:0000269|PubMed:21131438,
CC ECO:0000269|PubMed:21193550, ECO:0000269|PubMed:21408004,
CC ECO:0000269|PubMed:23229483, ECO:0000269|PubMed:23460523,
CC ECO:0000269|PubMed:23979762, ECO:0000269|PubMed:25199772,
CC ECO:0000269|PubMed:26886795, ECO:0000269|PubMed:27303714,
CC ECO:0000269|PubMed:28700656, ECO:0000269|PubMed:29363861,
CC ECO:0000269|PubMed:29464833, ECO:0000269|PubMed:29581110,
CC ECO:0000269|PubMed:29648590}.
CC -!- SUBUNIT: Interacts (via the activation domain AD) with the mediator
CC subunit GAL11A (via the KIX domain). {ECO:0000269|PubMed:26886795,
CC ECO:0000269|PubMed:29648590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expression is up-regulated by fluconazole and during biofilm
CC formation (PubMed:24645630). Expression is also induced by oxidative
CC stress caused by the antifungal drug, benomyl (PubMed:18627600).
CC Expression is regulated by the regulator of proteasome expression RPN4
CC (PubMed:18627600, PubMed:29648590). Transcriptionally autoregulated
CC through a pleiotropic drug response elements (PDRE) within its own
CC promoter (PubMed:21131438, PubMed:29363861). Expression is also up-
CC regulated by clorgyline, an inhibitor of azole transporters
CC (PubMed:28700656). Expression is negatively regulated by the J protein
CC JJJ1 (PubMed:29507891). {ECO:0000269|PubMed:18627600,
CC ECO:0000269|PubMed:21131438, ECO:0000269|PubMed:24645630,
CC ECO:0000269|PubMed:28700656, ECO:0000269|PubMed:29363861,
CC ECO:0000269|PubMed:29507891, ECO:0000269|PubMed:29648590}.
CC -!- DOMAIN: PDR1 contains several specific functional domains including an
CC N-terminal DNA-binding domain (DBD) containing the Zn(2)-C6 fungal-type
CC zinc finger; an inhibitory domain (ID) that may be involved in the
CC negative regulation of the activity of the protein; a middle homology
CC region (MHR) that probably assists the C6 zinc cluster in DNA target
CC discrimination; and a C-terminal activation domain (AD) that binds to
CC the KIX domain of GAL11A for recruitment to target promoters.
CC {ECO:0000305|PubMed:26886795, ECO:0000305|PubMed:29363861}.
CC -!- DOMAIN: The 9aaTAD motif (residues 1091 to 1099) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000250|UniProtKB:P12383}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to cycloheximide
CC (PubMed:16078083). Leads to an 8- to 16-fold increase in fluconazole
CC susceptibility (PubMed:16569856, PubMed:16803598, PubMed:28700656).
CC Leads also to increased rhodamine accumulation (PubMed:16569856).
CC {ECO:0000269|PubMed:16078083, ECO:0000269|PubMed:16569856,
CC ECO:0000269|PubMed:16803598, ECO:0000269|PubMed:28700656}.
CC -!- BIOTECHNOLOGY: The identification of PDR1 inhibitors or loss-of-
CC function mutations enhancing activities of antimycotics may be useful
CC for the development of novel strategies to combat fungal infections
CC caused by the multidrug-resistant C.glabrata strains.
CC {ECO:0000269|PubMed:21129149}.
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DR EMBL; CR380947; CAG57683.1; -; Genomic_DNA.
DR RefSeq; XP_444792.1; XM_444792.1.
DR AlphaFoldDB; Q6FXU7; -.
DR SMR; Q6FXU7; -.
DR STRING; 5478.XP_444792.1; -.
DR EnsemblFungi; CAG57683; CAG57683; CAGL0A00451g.
DR GeneID; 2886430; -.
DR KEGG; cgr:CAGL0A00451g; -.
DR CGD; CAL0126583; PDR1.
DR VEuPathDB; FungiDB:CAGL0A00451g; -.
DR eggNOG; ENOG502QV4Q; Eukaryota.
DR HOGENOM; CLU_304446_0_0_1; -.
DR InParanoid; Q6FXU7; -.
DR OMA; HRWEFYV; -.
DR PHI-base; PHI:7980; -.
DR Proteomes; UP000002428; Chromosome A.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:CGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:CGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071409; P:cellular response to cycloheximide; IEA:EnsemblFungi.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:CGD.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; IMP:CGD.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:EnsemblFungi.
DR GO; GO:2001040; P:positive regulation of cellular response to drug; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
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 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Virulence; Zinc.
FT CHAIN 1..1107
FT /note="Transcription factor PDR1"
FT /id="PRO_0000445081"
FT DNA_BIND 31..57
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..296
FT /note="DNA-binding domain (DBD)"
FT /evidence="ECO:0000305|PubMed:26886795,
FT ECO:0000305|PubMed:29363861"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..476
FT /note="Inhibitory domain (ID)"
FT /evidence="ECO:0000305|PubMed:29363861"
FT REGION 542..616
FT /note="Middle homology region (MHR)"
FT /evidence="ECO:0000305|PubMed:29363861"
FT REGION 968..1107
FT /note="Activation domain (AD)"
FT /evidence="ECO:0000305|PubMed:26886795,
FT ECO:0000305|PubMed:29363861"
FT REGION 999..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1091..1099
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P12383"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 243
FT /note="D->N: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:25132632"
FT MUTAGEN 255..968
FT /note="Missing: Behaves as a hyperactive transcription
FT factor that is lethal unless conditionally expressed."
FT /evidence="ECO:0000269|PubMed:29363861"
FT MUTAGEN 280
FT /note="L->F: Gain-of-function mutation leading to increased
FT PDR1 activity, fluconazole resistance, as well as to
FT decreased adherence to and uptake by host macrophages."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:23460523"
FT MUTAGEN 280
FT /note="L->P: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 297
FT /note="W->S: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:16569856"
FT MUTAGEN 344
FT /note="L->S: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810,
FT ECO:0000269|PubMed:29464833"
FT MUTAGEN 346
FT /note="G->D: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:29464833"
FT MUTAGEN 348
FT /note="G->A: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 376
FT /note="R->W: Gain-of-function mutation leading to increased
FT PDR1 activity, fluconazole resistance, as well as to
FT decreased adherence to and uptake by host macrophages."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:23460523, ECO:0000269|PubMed:29363861"
FT MUTAGEN 391
FT /note="S->L: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 575
FT /note="F->L: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:16569856"
FT MUTAGEN 584
FT /note="Y->C: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:29363861"
FT MUTAGEN 588
FT /note="T->A: Gain-of-function mutation leading to increased
FT PDR1 activity, fluconazole resistance, as well as to
FT decreased adherence to and uptake by host macrophages."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:23460523"
FT MUTAGEN 764
FT /note="N->I: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 772
FT /note="R->I: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 822
FT /note="P->L: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:29363861"
FT MUTAGEN 927
FT /note="P->S: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:29464833"
FT MUTAGEN 943
FT /note="G->S: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:20547810"
FT MUTAGEN 947..1107
FT /note="Missing: Loss-of-function mutation enhancing the
FT sensitivity to cycloheximide."
FT /evidence="ECO:0000269|PubMed:21129149"
FT MUTAGEN 1082
FT /note="D->G: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:21408004,
FT ECO:0000269|PubMed:29363861"
FT MUTAGEN 1083
FT /note="E->Q: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:21408004"
FT MUTAGEN 1099
FT /note="G->D: Gain-of-function mutation leading to increased
FT PDR1 activity and fluconazole resistance."
FT /evidence="ECO:0000269|PubMed:29464833"
SQ SEQUENCE 1107 AA; 126195 MW; 60A7D9A2BDAF1401 CRC64;
MQTLETTSKS NPGEVKAQKP STRRTKVGKA CDSCRRRKIK CNGLKPCPSC TIYGCECTYT
DAKSTKNLKS NDAGKSKPTG RVSKNKETTR VDKDIRKLEQ QYVPINANIH VGPRFPSENI
LNGYPQCGAP QNNVVGNPLA VNTQCHRGLS ETPMSSTFKE SNLRDDRLLQ SSDTDDMRNG
DSEERDLKGS DSENVKSKDN KSDPLIIYKD DTHIESTVNK LTQAVNELKS LQNAPSSIKS
SIDAIELQLR NILDNWKPEV DFEKAKINES ATTKSLETNL LRNKYTNHVH LTRFRIWIDY
KNANKNNHFM GECGFSLAES FFASNQPLVD ELFGLYSQVE AFSLQGLGYC VHLYEPYMKT
EEAIKLMKET LYIILRFIDI CVHHINEESI SIANPLETYL RKKHLMPMTP TPRSSYGSPQ
SASTKSLVSK IIERIPQPFI ESVTNVSSLQ LLDLRDDESK MFGTLLNMCK SIRRKFDSVM
SDYDSIVTEK SEGEQNDGKV TVAEFTSLCE AEEMLLALCY NYYNLTLYSF FEFGTNIEYM
EHLLLLLEEQ LALDEYYGFE KVLNVAVANA KKMGFHRWEF YVGYEESTAE KRRLLWWKLY
NYEKASTMKK GFFSVIDDAT VNCLLPKIFR NFGYLDRVEF LENIQKPMDL SVFSDVPISV
LCKYGELALT IVTSEFHEKF LYADRYTSIR NSAKPPTLKN QLIKEIVDGI AYTETSYEAI
RKQTAKLWDI ALGKVTKDKI NKEDTAAASK FTLSYEYHRF RLINMADNLI ARLMVKPKSD
WLISVMKGHL NRLYEHWKVM NEIILSMDND YSIATTFEYY APSCLCLATQ TFLIVRNMEM
DDVKMMVAVY KRFLNLGMFL QSAKVCSLAD SHTFRDFSRS FSFITIISRL MIIEFMQIKE
LTKVEFIEKF SEVCPDLADL PPMLLDPNSC LYFSLLQQIK KSGFTLSFKK ILEDARMMDF
NYDRNLDSEA IKKCNGEFSK SMPSCTNVSD TTTAVSDNSA KKKASMGSAR VNSTDTLTAS
PLSGLRNQTQ LDSKDSVPSL EAYTPIDSVS DVPTGEINVP FPPVYNQNGL DQQTTYNLGT
LDEFVNKGDL NELYNSLWGD LFSDVYL
