ID   A0A139GYV6_9PEZI        Unreviewed;       578 AA.
AC   A0A139GYV6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC578_1905 {ECO:0000313|EMBL:KXS95385.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95385.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS95385.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95385.1,
RC   ECO:0000313|Proteomes:UP000070133};
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:KXS95385.1}.
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DR   EMBL; LFZN01000218; KXS95385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139GYV6; -.
DR   OrthoDB; 1434032at2759; -.
DR   Proteomes; UP000070133; 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   PRINTS; PR00411; PNDRDTASEI.
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:UP000070133}.
SQ   SEQUENCE   578 AA;  66399 MW;  90A451E82FF4D8B6 CRC64;
     MDEKREFKDV IVVGAGIGGL CAAKTYLELS PGTDVTILES RPTLGGVWAE QNLYEGLCTN
     NLYGTYEYSD FPMYAEKYGL KKDMHISGEV MYRYLTDYAN HFDIFRRINF STKVTEVEKL
     ESGWKITTTA THDDSFKDVH YTRKLIMCNG LASNPSPITI PGHENFDKPI FNHGGLKDKA
     EALARDPNVK HVTVIGASKI GYDAVWLFAH HGKKVEWIIR KSGAGAVWMS KPYVKIGPWD
     VMLEHVVCTR FFTWFSPCIW GSYDGFGWIR RFLNKTRIGR WLMDGLWENT RNGTIEVAGY
     RREERLKHLE PPESLFWTAR VGIHNYPTDV HEFVRSGQVA IKHTDIDSLS SGGAVNFADG
     TWQQTDVLVQ ITGWQLIPTI KWKPEGIDAS IGVPSQSYSR GELDFWSDLD KRADAQILRQ
     FPRLADPPKN KLPYTQPVTP FRLYRGIAPP GLTAHGDRSL AFVKMVHCTS NILLAETQSL
     WLYAYMNNKL KIDERDVYWQ TALSSRFGAW RYPWGFSKWW PEFVYDAIPY VDMLLTDLGL
     RKHRKSSWLK EMFEGYTIHD YQGINGEWRA KYGKSKSQ
//