ID   OPAD_ASPUT              Reviewed;         587 AA.
AC   A0A0C1C354;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=MFS-type transporter opaD {ECO:0000303|PubMed:33004788};
DE   AltName: Full=Oxepinamide F biosynthesis cluster protein D {ECO:0000303|PubMed:33004788};
GN   Name=opaD {ECO:0000303|PubMed:33004788}; ORFNames=HK57_00062;
OS   Aspergillus ustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=40382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC   STRAIN=3.3904;
RX   PubMed=25706180; DOI=10.1371/journal.pone.0116089;
RA   Pi B., Yu D., Dai F., Song X., Zhu C., Li H., Yu Y.;
RT   "A genomics based discovery of secondary metabolite biosynthetic gene
RT   clusters in Aspergillus ustus.";
RL   PLoS ONE 10:e0116089-e0116089(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=33004788; DOI=10.1038/s41467-020-18713-0;
RA   Zheng L., Wang H., Fan A., Li S.M.;
RT   "Oxepinamide F biosynthesis involves enzymatic D-aminoacyl epimerization,
RT   3H-oxepin formation, and hydroxylation induced double bond migration.";
RL   Nat. Commun. 11:4914-4914(2020).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of oxepinamides, derivatives of anthranilyl-containing
CC       tripeptides that share an oxepin ring and a fused pyrimidinone moiety.
CC       {ECO:0000269|PubMed:33004788}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; JOMC01000153; KIA75455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1C354; -.
DR   SMR; A0A0C1C354; -.
DR   EnsemblFungi; KIA75455; KIA75455; HK57_00062.
DR   Proteomes; UP000053475; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..587
FT                   /note="MFS-type transporter opaD"
FT                   /id="PRO_0000452996"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   587 AA;  63189 MW;  3067C1154EE3EB65 CRC64;
     MARKFGRRFR RNSRASLPSL KFLTLGSTDS VFGPHNQQHR EEEANAPQEI ALKPVEENVQ
     TLLGSEGDVE CRAPPQQQDY APTWKCVAIM IALCLAVLCM ALDNTILATA IPKITEEFNS
     VHDMGWYVSA YMLAQSSMTL VYGKLLTYYT VKWVYIAALL LFEGGSLICG VSPNSIALII
     GRAISGTGGS GILVSSFLIV TIIVPVEKRP LYNGILSSLY AISGVFGPLL GGAFTDYATW
     RWCFYINLPV GGVTGFFILL LFRADKPTKQ WPTGAVSQLL ELDIIGLFLF IPALVSLLLV
     LQWGGSKYPW DDAHIIALIA VFGVTILAFA AVEYWQQDRA TIPPSMIRNR DIWGSLLFTF
     CLSGSVIIFN YYLPIWFQSI KNASATMSGV MNIPLILAVA LTSILSGWAV TTLGYYIPFM
     YATPVIASVG AGLLSTFKVS SAHPAWIGFQ ILYGIGVGLG FGLPLVVVQA TLTAHTISSG
     TALVTLTQGL AGALFNFVAQ SVFQTKLVQA LFAEAPSLDA GKIAEAGATV VRDIVDPDMV
     PAVLRAYNYA ITRVYLVGAA LAAAALLGVV PIRWGSVKGK KIEAGAA