ID   FSA7_FUSSF              Reviewed;         507 AA.
AC   A0A0E4AZP4;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=MFS transporter fsa7 {ECO:0000303|PubMed:25770422};
DE   AltName: Full=Fusarisetin A biosynthesis protein 7 {ECO:0000303|PubMed:25770422};
GN   Name=fsa7 {ECO:0000303|PubMed:25770422};
OS   Fusarium sp. (strain FN080326).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1608308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25770422; DOI=10.1016/j.bbrc.2015.03.011;
RA   Kato N., Nogawa T., Hirota H., Jang J.H., Takahashi S., Ahn J.S., Osada H.;
RT   "A new enzyme involved in the control of the stereochemistry in the decalin
RT   formation during equisetin biosynthesis.";
RL   Biochem. Biophys. Res. Commun. 460:210-215(2015).
CC   -!- FUNCTION: Efflux pump that might be required for efficient secretion of
CC       fusarisetin A or other secondary metabolies produced by the fusarisetin
CC       A gene cluster (PubMed:25770422). {ECO:0000305|PubMed:25770422}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Fairly reduces the production of fusarisetin A
CC       (PubMed:25770422). {ECO:0000269|PubMed:25770422}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; LC025956; BAR40289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E4AZP4; -.
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; -; 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   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..507
FT                   /note="MFS transporter fsa7"
FT                   /id="PRO_0000441309"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   507 AA;  54840 MW;  BF1B6BD6FBCA9C3C CRC64;
     MATKDPAVTT PDDSQLEAGR GNTGNNAGDA LEKPSSSTGT MVDEPADPNV VDWDGPDDPE
     HPLNWSKTQK NLHLVIVSLF TLAANLAATM FAPGAEELAT EFSITNSTVT AMTVSLYVLG
     FALGPLLLAP LSELYGRLIV YYGCNFVYIA FTIGCAFSTN VAMFLVFRII CGCAASGPMS
     IGGGTVADLF PQEERGKAMA LFTVGPLLGP VIGPIIGGFV SENVGWRWTF RIILIFSGLI
     GVATVIFMRE TNYTVLLQRK AQRARKETGN DKLVPKLTRN ETPKQMLVRA IVRPLKLLIF
     SPIVLLVSLY TGILFGLIFL LFTTFPSVFQ DVYGFSPGTA GLAYLGLGIG MILGLVLFSV
     LSDKMLKQKS GAARPEDRLI LMKWLGPVTP LGLFIYGWTA KYAVHWIVPI IGTFVVGFGS
     LFVVIPGQIY LVDSFGAEAA ASAMAANLLV RSPFGAFLDL TASPLYESLG LGWGNSVLGF
     ICLLFTPVPW FFYTYGERMR THFKVDL