ID   CLZ4_COCLU              Reviewed;         557 AA.
AC   A0A345BJP3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=MFS-type transporter clz4 {ECO:0000303|PubMed:28605916};
DE   AltName: Full=Squalestatin S1 biosynthesis cluster protein clz4 {ECO:0000303|PubMed:28605916};
DE   AltName: Full=Zaragozic acid A biosynthesis cluster protein 4 {ECO:0000303|PubMed:28605916};
GN   Name=clz4 {ECO:0000303|PubMed:28605916};
OS   Cochliobolus lunatus (Filamentous fungus) (Curvularia lunata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=5503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 74067;
RX   PubMed=28605916; DOI=10.1021/acs.orglett.7b01534;
RA   Liu N., Hung Y.S., Gao S.S., Hang L., Zou Y., Chooi Y.H., Tang Y.;
RT   "Identification and heterologous production of a benzoyl-primed
RT   tricarboxylic acid polyketide intermediate from the zaragozic acid A
RT   biosynthetic pathway.";
RL   Org. Lett. 19:3560-3563(2017).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid
CC       A), a heavily oxidized fungal polyketide that offers potent cholesterol
CC       lowering activity by targeting squalene synthase (SS).
CC       {ECO:0000305|PubMed:28605916}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; MF806533; AXF50656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345BJP3; -.
DR   SMR; A0A345BJP3; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
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   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..557
FT                   /note="MFS-type transporter clz4"
FT                   /id="PRO_0000452627"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          505..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  59837 MW;  5638D99A9CAD359F CRC64;
     MAHTKIPTAL HEQENFLPKK KLIIVILTLG VVLFVINIDH NGLSTLLPTI AEDLGAQKSI
     TWAGSSQLIA TTVFSVLYGR LSDIFGRKAL FVSALWVFSI AELGCGFATS PKMLYAMRAL
     TGASGGGIGN LSIIIATDVV SLRHRGQYMA VVAPFMVLGN ICGPLVAAGV AKSPLTWRGL
     FWLISPLGVL SAVLAGYILP STTPTDTFKQ NLVKVDWLGS FTSTIAIVGF MVAVSGPGAY
     HAGYSLLVIS LLSVSGVAFL AFLFIEWKLA TLPVIPLTIF AIPDVSALLM QTFTLGWVNQ
     ANVYFVPIYA QNLRQWSPVI SGVLLFPIIA VQVVVSMIAG RWMSKSGQYG LTIRLGVALL
     LIGSLLETKF GRETHPAYVI IVLLVIGIGV GAANQPMVIA MQAHTKKSER AVVTSSRNFF
     RFLGSACGVV MSAAILQSTL RTSLPAAYKH LADSPYALAG LNPRERDAIA PAYERAIRHV
     YIASAAASVL CSLGLFVWKD DGYESRPTEN NDDIEHAPAR GIEREDEQSS LIYDREPSAV
     SYGTVEAGEP NRLRRGG