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Database: UniProt
Entry: A0A0D2DGH1_9EURO
LinkDB: A0A0D2DGH1_9EURO
Original site: A0A0D2DGH1_9EURO 
ID   A0A0D2DGH1_9EURO        Unreviewed;       588 AA.
AC   A0A0D2DGH1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_05677 {ECO:0000313|EMBL:KIW42093.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42093.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW42093.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42093.1,
RC   ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; KN847336; KIW42093.1; -; Genomic_DNA.
DR   RefSeq; XP_016262309.1; XM_016406705.1.
DR   AlphaFoldDB; A0A0D2DGH1; -.
DR   GeneID; 27357751; -.
DR   VEuPathDB; FungiDB:PV06_05677; -.
DR   HOGENOM; CLU_006937_8_0_1; -.
DR   OrthoDB; 2041362at2759; -.
DR   Proteomes; UP000053342; 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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
SQ   SEQUENCE   588 AA;  66745 MW;  E422BBE532A35FAC CRC64;
     MGLEKLIITG RSICELSRYI DLRLTLVVSQ SVGKKERPSI FQIRSDSFRM GSIQEVVDCD
     VLVVGAGLSG ISMLYKLRKQ GLVAKIFEAG DDFGGTWHWA KYPGARVDSE FPFYQLNIPE
     VWKTWGFTQR FPHQQELRDY FRHVDKQCDL RKDTYFNTRV VEAVWNEEMG RWTIYTDSGR
     WARVKYLVVA SGSLDKQYTP EIPGLADFKG EMYHSRSWPQ GTSLEGKKVA VVGAGATGIQ
     VVQETAKQAS ELTVFIRRPS TCLPMGQRDI TDEERASQIG KYPDLFRDCR SSWSGFPFKP
     GPKAVEATPE EREAVFNETW SRGGFAFLTA YSDPRTDPVA NRMVYDFWAK KVRQRISDPV
     KREILAPEIP LYYFGTKRSP LEQDYYEMLD RDNVKVVSLR SNPFQKLHTK GAVMQDGSSH
     EFDVLIMATG FESFTGSLYG LGLKNRHGID IKDVWAEEIH TFLGLLVRDL PNCFVVFGPQ
     APTTLYNAPT TIECQTDIVT DLIVKTEQRG AKSIETTKIA EQEWAQLLDS QFRQSLVKHT
     PSWWTRANVP GAKTQPLTYL GGLMEYEKLC LTAIESDTGL VYKGVVGH
//
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