ID   ECDD_ASPRU              Reviewed;         541 AA.
AC   K0E3U9;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Major facilitator-type transporter ecdD {ECO:0000303|PubMed:22998630};
GN   Name=ecdD {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; AFT91387.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0E3U9; -.
DR   SMR; K0E3U9; -.
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   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..541
FT                   /note="Major facilitator-type transporter ecdD"
FT                   /id="PRO_0000443829"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   541 AA;  58636 MW;  FB8F6E950F8004A8 CRC64;
     MGLLFKQPEG TAGKAWPAIL ISGFVAFGGI LFGYDTGTIS GILAMPYWAR TFSTGYRDST
     GQLNVTSSQS SAIVSILSAG TFFGALGASP MGDIIGRRWG LIASNGIFVL GVVLQTIATS
     IPPFLAGRFF AGLGVGLISA LVPLYQSETA PKWIRGFIVG AYQFAITVGL LLASVLNNAT
     HHRNDSGSYR IPIAVQFAWS IILVGGMLIL PETPRYLVKK DNIQAAARSL SKLRRLPEDH
     AAIREELAEI QANHSFEMSL GRSGYMECFQ GNLLKRLVTG CLLQALQQLS GINFIMYYGT
     QFFKNSGFQN EFVITLITNC VNVGSTLPGL YAIDKWGRRP VLLTGAIGMA VSQLLVAVLG
     TTTTGQDSRG NIIVHDAAAQ KAAIAFICLY IFFFAASWGP SAWVITGEIF PLKTRAKSLS
     MTTATNWLLN WALSFSTPYL VNYGDGNANL QSKIFFIWFG CCFLCIGFVH FMIYETKGLT
     LEEVDELYME VDSARDSVKW QPRGVARGEK EAHGAETDFA VETAKGASEQ QEVIGDAGRS
     L