ID A0A166A2N6_EXIGL Unreviewed; 470 AA.
AC A0A166A2N6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZV88009.1};
GN ORFNames=EXIGLDRAFT_651598 {ECO:0000313|EMBL:KZV88009.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88009.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88009.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88009.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KV426109; KZV88009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166A2N6; -.
DR STRING; 1314781.A0A166A2N6; -.
DR InParanoid; A0A166A2N6; -.
DR OrthoDB; 2079054at2759; -.
DR Proteomes; UP000077266; 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:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
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:UP000077266}.
SQ SEQUENCE 470 AA; 52169 MW; 02AC703E7C25A8C6 CRC64;
MSRIENVKRV AIVGGGASGL VALKALLEQG AFDELVLFER REDVGGVWFF DPKVASEEAR
RYAQDASTQY PVVLEDGGAP KYPSPAYEGM IGNIAHELIS ISGRPFDKPL STGPVQEGER
EESDLFPSLD STIAYLRAFA DAYGLHNHIR LNTEVVSTRF VDGKWKVVTK NLLNGEETSS
TYDAVVYAAG LWDRRHLPAI AGIDTLPKER LLHARFYRSP SIFAGKRILV LGNGNSANDI
AAHAAPVALE PVYRSIRHPS YYSYVPDARI HDVKPVRQFS LDPASGKVIA ELGDETVIRD
IDLVVAATGY RYDVPSLRVP SGDDSAQDEP VTPPDGHRML GLYRHLLHAR FPTLAFIGYS
IAWSPFANSE AQASVVARAW AGRIDVPAVK EMIKDEEDSV KEVGDHNLFH VLALYKKREY
GYGNELRDWA LQGGTEGTVG VHWDERRIWL LQNVVRLKTL QLQRERGLIT
//
