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Database: UniProt
Entry: A0A0D0CQ59_9AGAR
LinkDB: A0A0D0CQ59_9AGAR
Original site: A0A0D0CQ59_9AGAR 
ID   A0A0D0CQ59_9AGAR        Unreviewed;       549 AA.
AC   A0A0D0CQ59;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIK57513.1};
GN   ORFNames=GYMLUDRAFT_46090 {ECO:0000313|EMBL:KIK57513.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK57513.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK57513.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK57513.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) 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; KN834790; KIK57513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CQ59; -.
DR   HOGENOM; CLU_006937_8_0_1; -.
DR   OrthoDB; 1612588at2759; -.
DR   Proteomes; UP000053593; 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593}.
SQ   SEQUENCE   549 AA;  61989 MW;  4F77A92C3142FC5A CRC64;
     MPALSNWNNE PDVLVVGAGF SGIYVLHHLR KLGYSVQVFE AAPQLGGVWH WNAYPGARVD
     SENPHYALSI PEIWEGWSWK ERFPGQKELR EYFEYIDQKL DVKKNISFNT RVVAAHFDVE
     TSRWVVKTED GRVARPQFFI LCVGFASKPY TPDFKGLDKF EGICHHTSQW PQEGVDLTNK
     RVGVIGTGAS AVQVIQEIGP HVSHLTVFQR TPNYALAMGQ RKLDVERERK RKVLYPTIFR
     RQFQTPTGFD IEPVAKTLSA STPEERLLHW EDAWARGGFA FLLNNYKDLM LDENTNREVY
     NFWRDKVRAR LHDPRMQEKL APTIAIHPLG AKRPCLEQTY YEVFNQPNVT LVDLNECGIS
     EITSKGLLTE DGFEHEFDAL VLATGFDSLT GSLTQIDIRG IDGVSIAEKW ANGVYTNLGM
     TCANFPNMFF PYNAQAPTAF CNGPSCIEAQ GNWIVDCIKS MKENNLTAIC STSEAEADWR
     AQVMGIGDLT LYSKAKSWYM GSNIPGKTVE HLNYAGGLHT YCNIITEIAE KGYEGFRLYR
     AGEKVSLAA
//
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