ID A0A165DVE0_9BASI Unreviewed; 402 AA.
AC A0A165DVE0;
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:KZT53620.1};
GN ORFNames=CALCODRAFT_500865 {ECO:0000313|EMBL:KZT53620.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT53620.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT53620.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT53620.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV424032; KZT53620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165DVE0; -.
DR STRING; 1353952.A0A165DVE0; -.
DR InParanoid; A0A165DVE0; -.
DR OrthoDB; 1699331at2759; -.
DR Proteomes; UP000076842; 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; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF309; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14510)-RELATED; 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:UP000076842}.
FT DOMAIN 2..352
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 402 AA; 43437 MW; E0B2E7FEDED957DE CRC64;
MKVIIVGAGV AGPILAMLLQ HKGFSPVIYE AAPSIPSGGG GVQLSPQTFK VLNIVGLAER
AIAAGQAQET LEFRSEPSGR VLFSWDIPAL IRAETGWPVC HIRRITYVRL LVDAVRERGI
EVQFGKKVVR VEQEGEKVRV EFEDGTEDEG DLLVGCDGMS SDVRELVFPP GKEHYTGIIV
IGGIARRHPS AVPPTVLQVF GDAAHFLSAP FSPTEIGFQC ALPEPRVSSD RWRSIPPTTT
QGQAMLMALP QARWGGGPSR MIGEATSAYR HAVSLREPLD TWHEGRVVLV GDSAHPATPH
LGQGGNQAAE DAYHLVRLLC RPGHIPLSPP ELAAALAEYT AVRVPHAKDV VASSIAEGRV
RVLAGPEKCK KRDEALGKSL AEGRWRDVVR RMRGPFEGES EI
//
