ID   A0A2G5I500_CERBT        Unreviewed;       660 AA.
AC   A0A2G5I500;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Putative sterigmatocystin biosynthesis monooxygenase stcW {ECO:0000313|EMBL:PIA99572.1};
GN   ORFNames=CB0940_02993 {ECO:0000313|EMBL:PIA99572.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA99572.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA99572.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA99572.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIA99572.1}.
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DR   EMBL; LKMD01000101; PIA99572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I500; -.
DR   OrthoDB; 49786at2759; -.
DR   Proteomes; UP000230605; Chromosome 3.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF1; FAD-BINDING MONOOXYGENASE STCW; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:PIA99572.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   REGION          47..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  75255 MW;  179CDCE97501454A CRC64;
     MQDGMNNDLM DVPSQMCSGF DCSAFVRADT PALSTFTKDV MAPFMNESLP TEPTKQQSKQ
     NDYSQFSSNG YEVPQDRCYR DPSNRKIRVL TIGAGISGIL MAYQIQKQCE NVEHVIYEKN
     ENIGGTWLEN RYPRAGCDIP SHAYTYQFAL NPEWPRYFSF AAEIWSYLDK VCEAFDLRKY
     MNFHTEVVGC FWQEETGEWL VKLREHRPGM EPREFEDRCH MLMYGAGVLN NFKWPEIPGL
     QDTFKGRIVH TARWPKDWTE EDWKNERVAI LGSGASSIQT VPGMQPHTKH LDVFVRTGVY
     FGVLAGNSGS QAKTYSSEEK DAFRLDPDSL VAHAKEIEDQ VNGMWGGFYS GSMGQKMGSM
     FFKKRMAEHI KDERLLKGFI PTYGLGCRRI TPGDVYMDAV QQNNVDVHFT PVVRCTEDGV
     IGGDGVERKV DSIVCATGFD VSYRPRFPVI GKNGIDLRDQ WKVCPEAYLG LAIPNMPNFV
     TFIGPSWPIE NGSVMAPLHS VSEYALQLIS KMQNENVRSF APRQDVTDKF NEHVQEWVKH
     TVWKDDCRSW YKNNETGRVN AIWPGSSLHY QQVIEKPRYE DFQIDYFDSN PWAHLGMGWT
     IEDRLGPKKA DVSPYLCKEN IDPRWFAAIG GDVNALSKEK ASAKPAKDDC QTCERKAVAF
//