ID A0A165D4V5_9BASI Unreviewed; 382 AA.
AC A0A165D4V5;
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:KZT52078.1};
GN ORFNames=CALCODRAFT_442115 {ECO:0000313|EMBL:KZT52078.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52078.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT52078.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52078.1,
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; KV424079; KZT52078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D4V5; -.
DR STRING; 1353952.A0A165D4V5; -.
DR InParanoid; A0A165D4V5; -.
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..350
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 382 AA; 41721 MW; DFD987C0AE1CE582 CRC64;
MKVLVIGAGI AGPILAMLLK HKGFAPEVFE KHSHPTEGGL TIMVSPQSLK VLDLVGLAHK
VIALGRPLQR LLSRSETSGQ VFIDSDLPST FVDKTGWPMV IVNRTVYHKF LVESCEAQGV
PVRWHKKLDD VKLAGEKVTA LFADGSEAVG DLLVGCDGLH SNTRDALFGK SPASFTGVVS
VSGFTPFSKS LSPPYTTMLQ IFGDGAYFLT FPTAQEKNMW AVNISANEGE VEDWGPVKES
ERQAIVDSLP PHTWKGEPGL FLKNAEEMVR FGLFLRPIPD VWHKGRVVLC GDAAHPITPF
LGQGANQASE DIYHLVRVLV QHAPLTDASL EAAFKEYTEI RKPKDEAALQ AVEEEHAKGL
ESDTWKIILE MVHGPFEGPS EI
//
