MFS1_MAGO7
ID MFS1_MAGO7 Reviewed; 615 AA.
AC G4N2A8;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=MFS-type transporter 1 {ECO:0000303|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein MFS1 {ECO:0000303|PubMed:27902426};
GN Name=MFS1 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_04850;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=27902426; DOI=10.1099/mic.0.000396;
RA Jacob S., Groetsch T., Foster A.J., Schueffler A., Rieger P.H.,
RA Sandjo L.P., Liermann J.C., Opatz T., Thines E.;
RT "Unravelling the biosynthesis of pyriculol in the rice blast fungus
RT Magnaporthe oryzae.";
RL Microbiology 163:541-553(2017).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of pyriculol and pyriculariol, two heptaketides that
CC induce lesion formation upon application on rice leaves but are
CC dispensable for pathogenicity (PubMed:27902426). With the ABC
CC transporter ABC7, is most likely responsible for pyriculol and
CC pyriculariol secretion and thereby may contribute to intrinsic
CC resistance (Probable). {ECO:0000269|PubMed:27902426,
CC ECO:0000305|PubMed:27902426}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC {ECO:0000305}.
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DR EMBL; CM001233; EHA52520.1; -; Genomic_DNA.
DR RefSeq; XP_003712327.1; XM_003712279.1.
DR AlphaFoldDB; G4N2A8; -.
DR EnsemblFungi; MGG_04850T0; MGG_04850T0; MGG_04850.
DR GeneID; 2675423; -.
DR KEGG; mgr:MGG_04850; -.
DR VEuPathDB; FungiDB:MGG_04850; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_27_5_1; -.
DR InParanoid; G4N2A8; -.
DR OMA; WVMSAYV; -.
DR OrthoDB; 850873at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
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; -; 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 Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="MFS-type transporter 1"
FT /id="PRO_0000446273"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..64
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"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 615 AA; 64730 MW; ED64C43BAD565C8A CRC64;
MTALAAVPDL QDAAGPSTTT VHSPNYSGSP ADISSSPTTR AVSRNTARQT ASAPPNHAES
SPPGNASPTG PPSPSGNNVS PHGRHQGMSK LRACLVIATL SGVSFLNTMG SGILTVSLPT
MARDVRLDDS LLLWPASVYS LAAGCTLLVF GAVGHIIGPK RVWITGACLY AAFTLGVGRS
ATGSQLIAFR SVLGVSIAMC LPTAVSLTTN GFGAGRWRNM AFAFQGMGQP LGYSTGLILG
GIFTDTVGWR FGFYISGGIN AVLAICALVV LPSPPRHDEG DGEQREVEEE ATDATVAAAA
VNRSSRSRPL ISRLAHDVDW TGTLAISASM GFLSYVFSVV SKDYDRMAAP QNIALLVAAA
LLLPTFTLWV GRQERLDRPA LIPNSLWRKA AFSSTCAAVF FTWAVFNAFQ YFSALYFERI
EHITALQTSL RFLPMVLVGA ATNIVTGYLV ETVEVRWLVV VSAIFSLFSP LIMALVRPGW
GYWKGAFFAM LLSPLHPDVL FTVSNLIISR VYDGRSQSLA GAVFNAVSQV GNSVGLGLTA
VVSSAVARSY HGSGGVGNAM DPPTGRPQHL PSSPTVEATL AGYHAAFWLM FGAAALVTVI
TFLGLRRGGK VGAVE
