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Database: UniProt
Entry: A0A2S6C450_9PEZI
LinkDB: A0A2S6C450_9PEZI
Original site: A0A2S6C450_9PEZI 
ID   A0A2S6C450_9PEZI        Unreviewed;       605 AA.
AC   A0A2S6C450;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBER1_02492 {ECO:0000313|EMBL:PPJ54509.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54509.1, ECO:0000313|Proteomes:UP000237631};
RN   [1] {ECO:0000313|Proteomes:UP000237631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT   mechanisms and extends production to the genus Colletotrichum.";
RL   bioRxiv 0:0-0(2017).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:PPJ54509.1}.
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DR   EMBL; PNEN01000562; PPJ54509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6C450; -.
DR   OrthoDB; 1434032at2759; -.
DR   Proteomes; UP000237631; Unassembled WGS sequence.
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; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF292; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G01900); 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237631}.
SQ   SEQUENCE   605 AA;  68312 MW;  AA8BD393B47BB3EA CRC64;
     MTASEALWAT APSWHDDKME EMEHFEVVVV GAGMSALVAA QGHLECASQT NLVILDDKKT
     VGGVWSKENI YPGLQTNNYR GSLEYPDYPF GDDRGVPHFS SLPGEAVHQY FSDFAAEHDL
     LRRTRHETKV LEAEKIDEKL NSGWKLLIET PRGRSTMTTD KLIVGTGLHN TPLPVQVAGK
     ESFNAPILHS GQLGKEGVAV AANEKVKRVT VYGGSKYAFD SVYKFAAAGK EIDWVISSSG
     HGPTYMVNNI CKMPVLGKVW AEMLVTTRFI SWFSPCSFGG IDGSSWWRWL LHSTKLGRKI
     VAAVWAQIGH DNLEQSGYFN KPRLKPLLPD SGFFDIASNL GTLNYPTDLL DFVRSGQVKV
     HRKDISHLSD HTVHLKDGTT LQSDAYISSS GWQWRPSITF KPASLHASLG IASDNYTPDQ
     ELFWCDLNSR ADRELFSRFP IFQTRPYPPS HASSSSTTTT QPQRLHRLIA PPILSAAGDR
     TLAFTGSGAN ISHILKSTIT SIWIYAYFND KLSIDPHRNM TEEQVCYEVA LTQRWSMRRY
     TYGFGQRFVD FVWDAVPWND VLLKDLGLEG RRKKGWWFGV RWWREMFEPY TVVDYRGLGR
     EWLEK
//
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