ID   A0A2G5HAR8_CERBT        Unreviewed;       516 AA.
AC   A0A2G5HAR8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Dimethyl-sulfide monooxygenase {ECO:0000313|EMBL:PIA89619.1};
GN   ORFNames=CB0940_07545 {ECO:0000313|EMBL:PIA89619.1};
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:PIA89619.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA89619.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA89619.1,
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   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00033748}.
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:PIA89619.1}.
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DR   EMBL; LKMD01000108; PIA89619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HAR8; -.
DR   OrthoDB; 1428562at2759; -.
DR   Proteomes; UP000230605; Chromosome 5.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR016215; NTA_MOA.
DR   NCBIfam; TIGR03860; FMN_nitrolo; 1.
DR   PANTHER; PTHR30011; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR30011:SF16; C2H2 FINGER DOMAIN TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:PIA89619.1};
KW   Oxidoreductase {ECO:0000313|EMBL:PIA89619.1}.
FT   DOMAIN          103..475
FT                   /note="Luciferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00296"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  56470 MW;  B89A0B657225144B CRC64;
     MAANGVVRNG WSGHDAQPNG TPPRRQAQWS ELRPKKSPLS KLVQFESKDF AHANGTKHES
     TQVNGRHHAT ITSESQPIPA RRKKLILNAF VEMCSGHQSP GLWRHPLDQS SNFNDLSHWT
     SLAQLLERGH FHGIFIADVL GGYDVYGGPQ NLLPAIRSGA QWPVNEPLSV VPAMAAATKS
     IGFGVTVSTS YEQPYHLARR LSTLDHLTKG RVGWNVVTGY LDSAARNLTN GGSQPEHDER
     YAICEEYMDV VYKLWNSSWR SDSVKLDRTS GVYTDPSLVR EINHKGKYFD VPGPHFCQPS
     PQRTPVILQA GTSRAGKNFA AKNAEVIFVS AHAPSSVAKS IADIRGQAEK LGRDPSKIKF
     LAKFCPVLGR THAEAEAKYR DYLQYGSYEG ALALFGGWTG VDMAPYGDDE ELRYVESNAI
     RSYIEGLLKS APDVNGGKWT KKTLAEHIMV GGLGATSVGT PQEVADEMER WVKEGDVDGF
     NIVSCAYAKT GCILILRPGI CADAADIRGR DRAVGS
//