ID A0A165ZQS4_EXIGL Unreviewed; 551 AA.
AC A0A165ZQS4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZV85019.1};
GN ORFNames=EXIGLDRAFT_726557 {ECO:0000313|EMBL:KZV85019.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV85019.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV85019.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV85019.1,
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; KV426202; KZV85019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZQS4; -.
DR STRING; 1314781.A0A165ZQS4; -.
DR InParanoid; A0A165ZQS4; -.
DR OrthoDB; 1657112at2759; -.
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; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
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:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..551
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007870168"
SQ SEQUENCE 551 AA; 61533 MW; 6315271C6467CE3F CRC64;
MSMATLWALL LYACATAAFP DVQLPLASTW THGSTSTKRI AVVGTGSGGL AVLKALVELP
MEMRQGWEIV AFEKREDVGG VWLPDWDVSP TRRPQSPLYP TLRTNAPHPS MTIPWYPFPP
DTPLLARHQD VLQYHRNIVS DFGLAPYIKF QHSVESASWT GNAWNLTVLN VAHNSTEFFE
FDHLIAAPGF NAYPRVPHLE GQEAWLEADS SRSIIHCMWY RDPTAFKGKN VAVLGGGPSG
WDMVRKIEPY ANAMYWSRDN KTEAPAAPPF PSIPGVPDVK HVASLHANGS VLLTDGNWLE
NVDTFILATG YEMRIPFLTA GGVLDEVKDP QPADRLTTNL RYIHPLYEQT LSLDPSYPLG
ALYFGGVLTY NPTGSTNAAQ GLFIAYTIAQ PELLKSRDEL YALLKRREAF IRAEGFEPSR
LGPKYGHGYG PFTGHLGNGS YEQLIVDYLV ERSDGKLAGY PGFPPNGQNY TEGWRLWTMK
RGMDIVFGFH DGIAREGADA WDRRWTKGLN SEADYVHAMH EFIDWLAEQK KNDTTRAFVD
NPTDSGALWW L
//
