FUS6_GIBM7
ID FUS6_GIBM7 Reviewed; 563 AA.
AC W7MLD3;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Efflux pump FUS6 {ECO:0000303|PubMed:22652150};
DE AltName: Full=Fusarin biosynthesis protein 6 {ECO:0000303|PubMed:22652150};
GN Name=FUS6 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11081;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2]
RP FUNCTION.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the
CC cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin
CC production (By similarity). The other FUS cluster members are not
CC essential for fusarin C biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:S0EEY7, ECO:0000269|PubMed:22652150}.
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; DS022257; EWG52302.1; -; Genomic_DNA.
DR EMBL; DS022257; EWG52303.1; -; Genomic_DNA.
DR RefSeq; XP_018758493.1; XM_018900243.1.
DR RefSeq; XP_018758494.1; XM_018900244.1.
DR AlphaFoldDB; W7MLD3; -.
DR SMR; W7MLD3; -.
DR STRING; 117187.FVEG_11081T0; -.
DR PRIDE; W7MLD3; -.
DR EnsemblFungi; FVEG_11081T0; FVEG_11081T0; FVEG_11081.
DR GeneID; 30068617; -.
DR KEGG; fvr:FVEG_11081; -.
DR VEuPathDB; FungiDB:FVEG_11081; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_0_1; -.
DR OMA; CSFAAQG; -.
DR OrthoDB; 672661at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
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 Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..563
FT /note="Efflux pump FUS6"
FT /id="PRO_0000437360"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 563 AA; 60404 MW; 8AAF20FC0E98160D CRC64;
MPQPDKMAAV NNAMPQPAPE KSLSSDPQPE SSKKSARFWL IFVAIALTTF LAALDTSIIS
TALPTITADL GSESLYVWII DAYLLASTAT IPIFAQAANI YGRRSLTLIA VCIFTLGSGL
CGGAHNTAMM VGGRAVQGIG GGGILTMSEI VVCDMVSIRE RGMYAGIIGG VWAIAAVVAP
VMGGAFAQNI SWRWIFYINL PIAGVSLVAL GLFLKLARPP SGTVKEQMSR IDWGGSVLLI
GSVTSIVLAL SWGGSEHPWS GWQTIVPLVI GLLALVAFFA YQGAPWLREP TMPLRLFGNR
TSSTLLVISF IHSLLLYWVC YFLPVYFQAV KEASPTRSAV MLFPIACTSA PAGVAAGITI
TKTGKYRVWH FTGFVLMSIA CGLFTLLDAQ SSTGRWVGFQ ILFGVGTGTV FTSTLPPILA
SLPDSDVATA TGAWTFIRNF GSIWGVAIPA AVFNNQVNHA APKISDSTVK SLLVDGGAYE
HATQHFIKSL SPNPELKTQV IQVYLEGLKV VWQVSLAFCL LGFILCFFVR SLTLRDELNT
EFGLKEEKPN SKNMSSEEGV VRE
