ID A0A165DDG3_9APHY Unreviewed; 517 AA.
AC A0A165DDG3;
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:KZT04630.1};
GN ORFNames=LAESUDRAFT_813992 {ECO:0000313|EMBL:KZT04630.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT04630.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT04630.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT04630.1,
RC ECO:0000313|Proteomes:UP000076871};
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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KV427635; KZT04630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DDG3; -.
DR STRING; 1314785.A0A165DDG3; -.
DR InParanoid; A0A165DDG3; -.
DR OrthoDB; 2092435at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF306; HYDROXYLASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
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:UP000076871}.
FT DOMAIN 74..428
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 517 AA; 57314 MW; 058A61060E947350 CRC64;
MQVSPTLGDT SNSAVETDLL PALIDYVAVH EARQRFSIES RVARQIQANL RVPSSPRTVA
FISRAPEFLP IEFIIVGGGV GGLTASIALS RLGHRVTVLD ENNDWDQTQG AGGCRLAPNV
TKIYYRWGME EKLKKIGVVS QYIQFADYET GRLGANGEWV EDFQIESGGE FLSLHYADFR
KLLYDTCVEL GVKVRGGAKV TQYHVRPERP SVTLASGEEV HGDVLIAADG RMSLSRQLML
GDRNYEKLQN VMVFNAVVPM TKMAEDPDLD GFLHEKQEGT VFSWFGEDRG ALGFPTAAQG
RNEFCLHTFA PSDWGEPDTM LEVGRAELVK SVQNAEPRLR KLAELASTVI AIPVVERPHI
DEWLHPDGSL LVIGEAAHPL TTGSLYAITL AVEDAMMLGR LFHHLHRRDQ IGNFLTALAE
KRQARVRTVE ITQRVNPLSI ALPPGVDQAR YLKAAVENMT AADAVSLTQD AIRVLFAYDP
EDEADDWWVQ WGLLQERHAR LLPLSPGISV DVEKKNS
//
