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Database: UniProt
Entry: A0A423VGC2_9PEZI
LinkDB: A0A423VGC2_9PEZI
Original site: A0A423VGC2_9PEZI 
ID   A0A423VGC2_9PEZI        Unreviewed;       477 AA.
AC   A0A423VGC2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VSDG_08356 {ECO:0000313|EMBL:ROV90047.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV90047.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROV90047.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROV90047.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-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:ROV90047.1}.
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DR   EMBL; LJZO01000053; ROV90047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423VGC2; -.
DR   STRING; 252740.A0A423VGC2; -.
DR   Proteomes; UP000284375; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF296; YALI0D21076P; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00419; ADXRDTASE.
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:UP000284375}.
SQ   SEQUENCE   477 AA;  53848 MW;  554701E9763C8EB9 CRC64;
     MNVRSVAVIG AGPAGAAAAD ALAKEQRFET VRVFDRRSLA GGTWVYTPDA SLKIPDLRDL
     LEGNADSPVP VPSKLPAETP KCDAVNNQEV RYADTALHEH LHGNHVPSLF GGIAEPRGDG
     PGAPFKHREV VREWIEGVFV HNKLQKFLEL NTTVERAEKK GSKWVLTLRK ELGQRNYWWE
     EKFDALIVAS GHYNVPWMPK IDGLVEYDAE FPGRILHAKH FRDGSRYHGK RVIVVGGSVS
     AYEIIGEVLP YAQQPVYASL RGDPDPAFGW KPWKDPHITV KKQITRLDSK SGRIYFEDDT
     YLDDVDHVIF GTGYTFSLPF LPVVQERIKH AYRRIPGIWQ HTWNIDDPTL ALIGMLNGGF
     TFRVYEWQAV AVARFFAGRS KPLPPVEEQR EWERKRVAAL RGGKAYYSIA PHHAEFFELL
     RDIAGKPGPG MPGRPFPSFD KAWADVWTGK VAENVQGWEQ ARKRSREGMD CKVRAKL
//
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