ID   FUS6_GIBF5              Reviewed;         555 AA.
AC   S0EEY7;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Efflux pump FUS6 {ECO:0000303|PubMed:23932525};
DE   AltName: Full=Fusarin biosynthesis protein 6 {ECO:0000303|PubMed:23932525};
GN   Name=FUS6 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10053;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   INDUCTION.
RX   PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA   Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA   Tudzynski B.;
RT   "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT   fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL   Mol. Microbiol. 77:972-994(2010).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA   Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA   Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT   "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT   insight into the complex regulation and fusarin biosynthetic pathway.";
RL   Chem. Biol. 20:1055-1066(2013).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the
CC       cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin
CC       production (PubMed:23932525). The other FUS cluster members are not
CC       essential for fusarin C biosynthesis (PubMed:23932525).
CC       {ECO:0000269|PubMed:23932525}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC       GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC       velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC       expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC       induced under acidic conditions in a PACC-independent manner
CC       (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC       ECO:0000269|PubMed:23932525}.
CC   -!- DISRUPTION PHENOTYPE: Does not alter fusarin C production
CC       (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; HF679031; CCT73265.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EEY7; -.
DR   SMR; S0EEY7; -.
DR   EnsemblFungi; CCT73265; CCT73265; FFUJ_10053.
DR   VEuPathDB; FungiDB:FFUJ_10053; -.
DR   HOGENOM; CLU_000960_22_0_1; -.
DR   Proteomes; UP000016800; 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   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..555
FT                   /note="Efflux pump FUS6"
FT                   /id="PRO_0000437359"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   555 AA;  59538 MW;  769C1B73EA03BF3E CRC64;
     MASAKDAQPA PEKSLSSDPQ PEPSKKGARF WLIFVAISLT TFLAALDTSI ISTALPTITA
     DLGSESLYVW IIDAYLLAST ATIPIFAQAA NIYGRRSLTL IAVCIFTLGS GLCGGAHNTA
     MMVGGRAVQG IGGGGILTMS EIVVCDMVSI RERGMYAGII GGVWAIAAVV APVMGGAFAQ
     NISWRWIFYI NLPIAGVSLV ALGLFLKLSR PPSGTFKEQM SRIDWGGSVL LIGSVTSIVL
     ALSWGGSEHP WSGWQTIVPL VIGLLALVAF FAYQGAPWLR EPTMPLRLFS NRTSSTLLVI
     SFIHSLLLYW ICYFLPVYFQ AVKEASPTRS AVMLFPIACT SAPAGVAAGI TITKTGKYRV
     WHFTGFVLMS IACGLFTLLD AQSSTGRWVG FQILFGVGTG TVFTSTLPPI LASLPDSDVA
     TATGAWTFIR NFGSIWGVAI PAAVFNNHVN HAAPKISDSS VKSLLVDGGA YEHATQHFIK
     SLSPNPDLKT QVIQVYLEGL KVVWQVSLAF CLLGFILCFF VRSLTLRDEL NTEFGLKEEK
     PNSNNMSSEE GVVRD