ID   ECDC_ASPRU              Reviewed;         556 AA.
AC   K0DZ95;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Major facilitator-type transporter ecdC {ECO:0000303|PubMed:22998630};
GN   Name=ecdC {ECO:0000303|PubMed:22998630};
OS   Aspergillus rugulosus (Emericella rugulosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58397 / NRRL 11440;
RX   PubMed=22998630; DOI=10.1021/ja307220z;
RA   Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT   "Identification and characterization of the echinocandin B biosynthetic
RT   gene cluster from Emericella rugulosa NRRL 11440.";
RL   J. Am. Chem. Soc. 134:16781-16790(2012).
RN   [2]
RP   CLUSTER REVISION.
RX   PubMed=27502607; DOI=10.1186/s12864-016-2885-x;
RA   Huettel W., Youssar L., Gruening B.A., Guenther S., Hugentobler K.G.;
RT   "Echinocandin B biosynthesis: a biosynthetic cluster from Aspergillus
RT   nidulans NRRL 8112 and reassembly of the subclusters Ecd and Hty from
RT   Aspergillus pachycristatus NRRL 11440 reveals a single coherent gene
RT   cluster.";
RL   BMC Genomics 17:570-570(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC   -!- CAUTION: EcdB, ecdC, ecdD, ecdE and ecdF have previously been
CC       identified as being part of the echinocandin B biosynthetic cluster,
CC       but it was later realized that this was due to a genome misassembly and
CC       these 5 proteins are now considered as artifacts and not part of the
CC       cluster. {ECO:0000269|PubMed:27502607}.
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DR   EMBL; JX421684; AFT91386.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0DZ95; -.
DR   SMR; K0DZ95; -.
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; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF00083; Sugar_tr; 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..556
FT                   /note="Major facilitator-type transporter ecdC"
FT                   /id="PRO_0000443828"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   556 AA;  61391 MW;  577735F8209977E1 CRC64;
     MRRNADLQVD GVDYSTTRLS HRWRMLKSQQ RFFAWCQTLE RPAPTVLTDR IMAGLWISTG
     VVMQGFDMVA GGQLAALPAF QKQFGAPVPD GSYMIPAHYL STWNAIAPAC EILSTFICAP
     LLERYGRKPG ILAASIVSVA GVVLQQLATD WRVHLAGRGV NGETCRPELR GFFLCFFNTS
     IVFGQFAMSV APGGWLAVYS LVCSAAVSRG SSLLSGKWQW WLPVVGMYTF PAILITGWPL
     FPESPYWLVR QGKVSEAQTS LRRIYGLHND ELCSVEVRRM EAEHQQARSI QGRLEQSNRR
     SILGFDSCAG VECFGYMHRK RTLTAILAAS GQQMIGATFV IGYATYFLNL LHVRDYFDAS
     IALYLVMLLA SIAAFPLSEM VGRRAMIVIP QFVLCCMLLL IGVLGCVPDQ RKASWGIVAC
     IYIWAFIYEI SIGAVGFVLA SEIATARLRS ATQGLVTATN AAWGLILQFT VPYMINPDAG
     NLGGRVGFIF FGTGLIAAIG GWYLYPETRG IPFAVLDELY ASGTAPRRFR AVREQMMGVR
     RDPEADIPIH PQQLIA