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Database: UniProt
Entry: A0A0D2DL11_9EURO
LinkDB: A0A0D2DL11_9EURO
Original site: A0A0D2DL11_9EURO 
ID   A0A0D2DL11_9EURO        Unreviewed;       538 AA.
AC   A0A0D2DL11;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV04_09935 {ECO:0000313|EMBL:KIW63057.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW63057.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW63057.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW63057.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; KN846962; KIW63057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2DL11; -.
DR   HOGENOM; CLU_006909_8_1_1; -.
DR   OrthoDB; 445965at2759; -.
DR   Proteomes; UP000054266; 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; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
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}.
SQ   SEQUENCE   538 AA;  60110 MW;  F6E097A55ABF534D CRC64;
     MAQPSVAVIG LGAQGVNTVK NLLEQGFTVT GFDRNSYIGG IWHFSAEPHV SALPTTVVNI
     SRERGCFTDF AFPPGTDSYP SSAQVDKYLN DYVDAFELRP HLRLSTRVDA IERDDTQNCW
     HITVSGPGSV APERLRFDKV VMATGPHNKP VIPDLPGQEH FKGEMLHSIA FKDPNPFQGK
     RVMVIGASNS AADTATSLIG VASKIYLSHR HGANVMPRHL KNGKSLDHAL SYRQFQIKDT
     TDSLAPWLSM RFLDAFVSKT QREEFGTFDP QWRLQPAASL LHQNPTISET LIPALREGAI
     TSTHAPKCVT SDWTVELQDG SILTLDSIIF CTGYSLDYSI LGRYDPTLNA SVTGGHTNDT
     PRLYQNIFSL DYPESLAFVG VAIIIFPAFL LSDLASMAIA ALWSNRPESP SLPSQQEMEQ
     WYAGHLTWVS NIRALSPDRK FVRLSVRSRQ WLPWVTDMGG CNIDHHLGYF SPGSWKLWWH
     DRPLYNLLVY GIYSPHVFRL FESSRPGGRK KWDGARDAIV RVNEDIRAGL EKRRKEGA
//
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