FMQE_ASPFU
ID FMQE_ASPFU Reviewed; 534 AA.
AC Q4WLW9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=MFS transporter fmqE {ECO:0000303|PubMed:24612080};
DE AltName: Full=Fumiquinazoline biosynthesis cluster protein E {ECO:0000303|PubMed:24612080};
GN Name=fmqE {ECO:0000303|PubMed:24612080}; ORFNames=AFUA_6G12040;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
RX PubMed=20804163; DOI=10.1021/bi1012029;
RA Ames B.D., Liu X., Walsh C.T.;
RT "Enzymatic processing of fumiquinazoline F: a tandem oxidative-acylation
RT strategy for the generation of multicyclic scaffolds in fungal indole
RT alkaloid biosynthesis.";
RL Biochemistry 49:8564-8576(2010).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=24612080; DOI=10.1111/cmi.12284;
RA Lim F.Y., Ames B., Walsh C.T., Keller N.P.;
RT "Co-ordination between BrlA regulation and secretion of the oxidoreductase
RT FmqD directs selective accumulation of fumiquinazoline C to conidial
RT tissues in Aspergillus fumigatus.";
RL Cell. Microbiol. 16:1267-1283(2014).
RN [4]
RP FUNCTION.
RX PubMed=33705521; DOI=10.1093/genetics/iyab036;
RA Rocha M.C., Fabri J.H.T.M., da Silva L.P., Angolini C.F.F., Bertolini M.C.,
RA da Cunha A.F., Valiante V., Goldman G.H., Fill T.P., Malavazi I.;
RT "Transcriptional control of the production of Aspergillus fumigatus
RT conidia-borne secondary metabolite fumiquinazoline C important for
RT phagocytosis protection.";
RL Genetics 0:0-0(2021).
CC -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC biosynthesis of the antitumor cytotoxic peptidyl alkaloids
CC fumiquinazolines that confer a dual-usage capability to defend against
CC phagocytes in the environment and animal hosts (PubMed:20804163,
CC PubMed:24612080, PubMed:33705521). Probably involved in
CC fumiquinazolines metabolism and transport (PubMed:24612080).
CC {ECO:0000269|PubMed:20804163, ECO:0000269|PubMed:24612080,
CC ECO:0000269|PubMed:33705521}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:24612080}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by brlA, a conidiation-
CC specific transcription factor involved in the early stage of asexual
CC development and necessary for conidiophore formation (PubMed:24612080).
CC {ECO:0000269|PubMed:24612080}.
CC -!- DISRUPTION PHENOTYPE: Seems not to affect fumiquinazolines production
CC (PubMed:24612080). {ECO:0000269|PubMed:24612080}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL89045.1; -; Genomic_DNA.
DR RefSeq; XP_751083.1; XM_745990.1.
DR AlphaFoldDB; Q4WLW9; -.
DR SMR; Q4WLW9; -.
DR STRING; 746128.CADAFUBP00007606; -.
DR EnsemblFungi; EAL89045; EAL89045; AFUA_6G12040.
DR GeneID; 3508388; -.
DR KEGG; afm:AFUA_6G12040; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_11_0_1; -.
DR InParanoid; Q4WLW9; -.
DR OMA; WTICPEI; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:1900781; P:fumiquinazoline C biosynthetic process; IMP:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..534
FT /note="MFS transporter fmqE"
FT /id="PRO_0000444453"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 534 AA; 58071 MW; DDD7BCED9CC4E443 CRC64;
MPEDKVEAIE HVESSRHDAT VNEKAIADFL NAEKEMTTWQ AVRAHRRLLL FAAYRVTHLA
ILPFVCASNY GYDTVSNGSS IAMPAFIMSF GAMNHATGSM YLPSIWTSLW TSMTNLGQAL
GSLIAGFLAE RIGRRWTAVS LAILSIVGTF ILVFSSTRGM LLVGKTMNGA VVGGLMAIGT
TYAADVAPIK LRGALLQAIV FFGVAMQGVS LGIVRAFILD MRPLAWKIVF GIQWAFATLV
LIAAFLVPES PVFYVAHGKH DKAQSALRRL HGSSDQYLHI RYGAIVHALD EERKQQSESV
SWAELFKGCN LKRTITIGFI MFSTSAIGVP FLTQNIYFLI TVGLNVTSVF DIGIGGFFLG
CLFVMLGWLS NEGIGRRRLW LWGLIGNFLC MVTIGALGFS TTKASQLAIA VIMNVLISYG
VYATVGVAWT ICPEISSHRL RQYSQSVAFI VGAVGGWLFN FITPYMYNVD SGNLGAKTGF
VYAGLTVVVA VISWFLVPET AGLSVEDIDR AYEMGTAPRH FKSAKATVSA ESGH
