ID   A0A139ILE5_9PEZI        Unreviewed;       522 AA.
AC   A0A139ILE5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_9950 {ECO:0000313|EMBL:KXT15571.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT15571.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT15571.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT15571.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT15571.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LFZO01000055; KXT15571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139ILE5; -.
DR   Proteomes; UP000073492; 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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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:UP000073492}.
SQ   SEQUENCE   522 AA;  58853 MW;  558BA4D3B1C1583F CRC64;
     MGVIRQAEHA VQRLIHDPAK YFYYLLQRII SLILSPTPPS PSQELRRPKI AIIGAGITGV
     SSAAHCVGHG FDVRIFEAGG RDALGGIWAK VNNTSGLQIH SIMYRFHPDV KYDSGYPHRR
     QIVGQVEKLW NNYHLEEKTK FNTKVEKVYK NDNGQWIIND DSNGRYDAII AAVGTCGDPK
     MGHIKGAKGY QGEIFHSSQL DGKEKSIEGK EVLVVGGGAS AIEALEFATA AKASKIYILS
     RSEKWIIPRN PVIDVLLSLN IFGMETSITG IPLGWIPEFL LRMFFYRDLK DIAPPPGSGK
     GIFMETPMVN NDVLEQIRSG KASWLRGDIK GFESRGILFN HRAQGVPKGG PGREELIEGE
     VAIMATGYER PSLKFLPDDC FEKDYEPPNW YLQVFPPKHQ DVLANNCTYV NAIGTVGNYH
     IGIYTRFLLM FLVDPLARPV EKWMKRWIDM TRWVKSKAPT GAFDFFTYAE LLYWFVFVIL
     INPLRWKWCL FVLFGVGSSL PMKIVEQEDK FRASQSNNAK SD
//