EFUF_HORCR
ID EFUF_HORCR Reviewed; 493 AA.
AC A0A2Z4HQ22;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 23-FEB-2022, entry version 10.
DE RecName: Full=MFS-type transporter efuF {ECO:0000303|PubMed:30051576};
DE AltName: Full=Enfumafungin biosynthesis cluster protein F {ECO:0000303|PubMed:30051576};
GN Name=efuF {ECO:0000303|PubMed:30051576};
OS Hormonema carpetanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX NCBI_TaxID=284138;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA Bills G.F.;
RT "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT cyclases.";
RL Environ. Microbiol. 20:3325-3342(2018).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of enfumafungin, a glycosylated fernene-type
CC triterpenoid with potent antifungal activity, mediated by its
CC interaction with beta-1,3-glucan synthase and the fungal cell wall
CC (PubMed:30051576). Might facilitate the transport of glucose units to
CC the subcellular site of enfumafungin biosynthesis (Probable).
CC {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MF611887; AWW17215.1; -; Genomic_DNA.
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 Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..493
FT /note="MFS-type transporter efuF"
FT /id="PRO_0000454463"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 493 AA; 53856 MW; 915D58562B9159BD CRC64;
MATSVEADTK SQVNLKVAND GGESASETGV VDVYDDPLIH NSIRKKLDLK LLPLLSAMYL
FNAIDRSNLG NAKTDGLEKD LHMKGNEYSI TLVLFYVTFC LLDVPANMLL KKFSGKIMLP
TLMMGWGSMT LIQCAVHNWG GLIACRLLMG AFEAGFMAGV VYYLTTFYRR NELALRISIF
YGAATIAGAF SGLLAYGVFQ INHPSIPGWK FLMIIEGSAT ILLASFAYWH LPSSVLSCKW
FTEEEKHVAE QRMLHDGSIQ TDEKFALKTA LANLLDWKIA LYAVIGISYG VASASVGNFL
PQMVQRLGFG TVKTNLYTVA PYCVGCVILL AQCTSSDHFR ERSTHLAGAM LLTFVGFILL
ITLDTEAQPG PTYFACFLLA AGAFTPSCIF HSWHNNNTPS ENGRAAVTGF MVGASNSGGI
ISSLAFASKT APKYIPALIV TATFQGVGIV LVLGFGAWFR WDNRRRDRVQ GVRIRTGDVA
TVSVDDASWR WTA