ID   CURE_ASPTE              Reviewed;         571 AA.
AC   L7X3H5;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Dehydrocurvularin exporter {ECO:0000303|PubMed:23335766};
GN   Name=curE {ECO:0000303|PubMed:23335766};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AH-02-30-F7;
RX   PubMed=23335766; DOI=10.1128/aem.03334-12;
RA   Xu Y., Espinosa-Artiles P., Schubert V., Xu Y.M., Zhang W., Lin M.,
RA   Gunatilaka A.A., Sussmuth R., Molnar I.;
RT   "Characterization of the biosynthetic genes for 10,11-dehydrocurvularin, a
RT   heat shock response-modulating anticancer fungal polyketide from
RT   Aspergillus terreus.";
RL   Appl. Environ. Microbiol. 79:2038-2047(2013).
CC   -!- FUNCTION: Efflux pump that is probably involved in the export of
CC       dehydrocurvularin (PubMed:23335766). {ECO:0000269|PubMed:23335766}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23335766};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; JX971534; AGC95323.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7X3H5; -.
DR   SMR; L7X3H5; -.
DR   VEuPathDB; FungiDB:ATEG_04563; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..571
FT                   /note="Dehydrocurvularin exporter"
FT                   /id="PRO_0000438394"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   571 AA;  61426 MW;  65496378D4487C41 CRC64;
     MADGSDLENN HKPELDRSQP GSTSNGSQEQ KDPDEIAPEY ATGVRLILVM FTIFVSTILV
     SLEIGIIATA IPGITNEFRR LDDVGWYGSA TFILAAAASP LWGKLFKYVD VKWTYLSAVF
     IFLVGSIVAA AAPNSVSVII GRAIQGWGAS GVLGGTLIVI NYVAPPRNHP LLIGTWMAVF
     MVSTILGPVI GGGFTSGVSW RWCFWINLPV GGPIIVLLLL FLRIPKHIKK VPATWQEIIL
     ALDLPGFCLL LVSLVCLTLA LQWGGQTKAW NDGSVIATLV MWIVLSIAFL VTEWFQGQRA
     MTPFSILTLR MTWSNALFCL ISYAALYQVM FYLPIYFQSI HGQSAVKSGV NTLPFLAFFA
     LGAVVSGGVI GKTRYTQPFE LLGALIMTAG MALIYILDVD SPQAMYIGAE VLFGFGVGIC
     NQIPMTAVQG FSKQEDVSSA TGIMVMCQTL SGAYFVAIAQ SLFANRMLAT VLSGAGHLDP
     ALVLGTGASE LQHVFSGEDL TEVIAAYMVG IKDVFAFSLA CAAFAVLLSL IIPFKRLPDH
     GKKDKPATEE AAEEKSEAEG KVSGDKEENH S