EQXG_FUSHE
ID EQXG_FUSHE Reviewed; 481 AA.
AC S4W288;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=MFS transporter eqxG {ECO:0000303|PubMed:23614392};
DE AltName: Full=Equisetin biosynthesis protein G {ECO:0000303|PubMed:23614392};
GN Name=eqxG {ECO:0000303|PubMed:23614392};
OS Fusarium heterosporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium heterosporum species complex.
OX NCBI_TaxID=42747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 74349 / MF6069;
RX PubMed=23614392; DOI=10.1021/cb400159f;
RA Kakule T.B., Sardar D., Lin Z., Schmidt E.W.;
RT "Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC
RT 74349 produce divergent metabolites.";
RL ACS Chem. Biol. 8:1549-1557(2013).
CC -!- FUNCTION: Efflux pump that might be required for efficient secretion of
CC equisetin or other secondary metabolies produced by the equisetin gene
CC cluster (PubMed:23614392). {ECO:0000305|PubMed:23614392}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; KC439347; AGO86666.1; -; Genomic_DNA.
DR AlphaFoldDB; S4W288; -.
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; 2.
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..481
FT /note="MFS transporter eqxG"
FT /id="PRO_0000441310"
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 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
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"
SQ SEQUENCE 481 AA; 51979 MW; 9C38D4DBD8D0C570 CRC64;
MATTDPAIAA PDDSQLEAGR ENIRANVGDA LEKPSSSTGT MVDEPTDPNV VDWDGPHDPE
HPLNWSKTQK NLHLVIVSLF TLAANLAATM FAPGAEELAT EFSITNSTVT AMTVSLYVLG
FALGPLLLAP LSELYGRLVI YYGCNFVYVV FTIGCAFSTN VAMFLVFRII CGCAASGPMS
IGGGTVADLF PQEERGKAMA LFTVGPLLGP SGLIGVATVI FMRETNYMVL LQRKAQRARK
ETGNDKLVPK LTRNETPKQM LARAIVRPLK LLIFSPIVLL ISLYTGILFG LIFLLFTTFP
SVFQDVYGFS PGTAGLAYLG LGIGMILGLV LFSVLSDKML KQKSGAARPE DRLILMKWLG
PITPLGLFIY GWTAKYAVHW IVPIIGTFVV GFGSLFVVIP GQIYLVDAFG AEAAASAMAA
NLLVRSPFGA FLDLTASPLY VSLGLGWGNS VLGFICLLFT PVPWLFYTYG ERMRTHFKVD
L
