ID   ASC6_DIDFA              Reviewed;         517 AA.
AC   A0A5C1RGE8;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Ascochitine biosynthesis cluster MFS transporter {ECO:0000303|PubMed:31554725};
DE   AltName: Full=Ascochitine biosynthesis cluster protein 6 {ECO:0000303|PubMed:31554725};
GN   ORFNames=orf6 {ECO:0000303|PubMed:31554725};
OS   Didymella fabae (Leaf and pod spot disease fungus) (Ascochyta fabae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=372025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AF247/15;
RX   PubMed=31554725; DOI=10.1128/msphere.00622-19;
RA   Kim W., Lichtenzveig J., Syme R.A., Williams A.H., Peever T.L., Chen W.;
RT   "Identification of a polyketide synthase gene responsible for ascochitine
RT   biosynthesis in Ascochyta fabae and its abrogation in sister taxa.";
RL   MSphere 4:0-0(2019).
CC   -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC       biosynthesis the mycotoxin ascochitine, an o-quinone methide that plays
CC       a possible protective role against other microbial competitors in
CC       nature and is considered to be important for pathogenicity of legume-
CC       associated Didymella species. {ECO:0000305|PubMed:31554725}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC       {ECO:0000255}.
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DR   EMBL; MN052627; QEN17974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C1RGE8; -.
DR   SMR; A0A5C1RGE8; -.
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; Transmembrane; Transmembrane helix; Transport;
KW   Virulence.
FT   CHAIN           1..517
FT                   /note="Ascochitine biosynthesis cluster MFS transporter"
FT                   /id="PRO_0000448993"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   517 AA;  56789 MW;  150A4BE84D1B1836 CRC64;
     MSPDSRDPEA QRDVGLTKNT SSVNIPLESV KTDKTSNASP IMGPGEGPKI DDTLVSWSGP
     DDSQNPQNMP QWKKWVITWL LSFLNVWVTF SSTIFASAVR TTSLEYGVSR VVMTLGVSLT
     VLGFAVGPLI WGPMSEVIGR LTPFYFGYAV FCIFQIPVGV AQNVYTILIC RFFIGFFGTS
     AMAVTPGVLA DIFSPKDRGV AVSVYAAAAF IGPIFGPIVG GFVVDSSLGW RWTAWITLIL
     ASAFGLAALV FVPETYGPII LQRRAARLRQ ETRNFAYHSA LDENPPTLND IIFKYFLRPF
     QMLIKEPILL LVTLYISLVY GVLYLFFVAY PIEFLEVRRW THAGVAALPL LAVMLGTLAG
     CLTILFVTGH TYPRKMAKMG RVPPEERLKL MMVGSVSLPI GLFWFGWTSS RSVHWFAQTA
     AGFPIGIGLA LIWVQGLSFL IDVYLMFANS ALAGNTLIRS AVGAAFPLFG APMYHKLGVN
     WASSLLGFLS VAMIPIPVAF YYYGPKIRAM SKFSPKL