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Database: UniProt
Entry: A0A166MBE4_EXIGL
LinkDB: A0A166MBE4_EXIGL
Original site: A0A166MBE4_EXIGL 
ID   A0A166MBE4_EXIGL        Unreviewed;       299 AA.
AC   A0A166MBE4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:KZV77848.1};
DE   Flags: Fragment;
GN   ORFNames=EXIGLDRAFT_784701 {ECO:0000313|EMBL:KZV77848.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV77848.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV77848.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV77848.1,
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).
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DR   EMBL; KV427471; KZV77848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166MBE4; -.
DR   STRING; 1314781.A0A166MBE4; -.
DR   InParanoid; A0A166MBE4; -.
DR   OrthoDB; 2898931at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR010031; FAD_lactone_oxidase-like.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 2.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          83..270
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         299
FT                   /evidence="ECO:0000313|EMBL:KZV77848.1"
SQ   SEQUENCE   299 AA;  31618 MW;  6DB990F2DCC986D9 CRC64;
     MLSPTVTAVE EAERTLAPLL HAFHTEVEED VHALHDLQAK YAPRVLSILH QTGIAAMTAF
     KAGLHHTLDA ALGSGGGQAV NGLNPFPNAL HLPESIADVQ RLVGEARRSG RKLRVIGAAH
     TRPKEAILDD EDKDRVVLVS LKKYRGVTLD PVSGIALVKA GTNLGVDPNV PESTLENSLC
     FIIDEAGWML PEVGGIIHQT VGGFLATASA GGSLKYSFHD AVVGYTLVDG NGDVRTLSKD
     DPDSPLFDAA ACCAGLCGVI TDIRLQLIPK ADVQGVQQTY SAQIQEGCPV NLFGDVDHT
//
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