ID A0A0W0FMG0_9AGAR Unreviewed; 510 AA.
AC A0A0W0FMG0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KTB37473.1};
GN ORFNames=WG66_9957 {ECO:0000313|EMBL:KTB37473.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB37473.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB37473.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB37473.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-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:KTB37473.1}.
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DR EMBL; LATX01001846; KTB37473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FMG0; -.
DR eggNOG; KOG1399; Eukaryota.
DR Proteomes; UP000054988; 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:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..510
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006901930"
SQ SEQUENCE 510 AA; 58103 MW; B6C4B743279C5865 CRC64;
MEWTWNPLLL AYQIIQILLS KLFSPAPPPP HAERCRRPRI AVIGAGLTGV SSAAHCIGHG
FDVVMFESGG PDELGGIWAR VNNTSGLQIH SLMYRFHPRV QWQSGYPSKQ QILDAVQDIW
KAYLLEDKTK FNTKIERVWQ DEDGKWYLNS EEYGKFDGII AAIGTCGEPK MPHIAGQESF
KGEIYHSSKL DGKDAKGKKV VIIGGGASAV EALEFVTAAQ AGKTTILARS DKWIIPRNAI
VDMLLATNIF GQEIYLSWIP EFLLRRFFYR DLADLAPSHQ GIFTETPMVN SDVLNKIRDG
SAEWLRGDID SFTENGVLFN KRAKNVPKGG PGREILVEAD MVIMATGFKR PKLDFLPDNC
FDEPYNPPNW YLQTFPPPYP SVSCINCTYI NAIGTVGNYH IGIYTRILLM FLVDPLTRPH
EWLMKKWIDM TRLLKARSPT PAFDFFTYTE LLWWYFFCVA INPFRWKWAL FVFFGIGRDL
PLSIVQKEEK IRQYLGQDND KEEITKKKTA
//
