ID A0A166BGW8_EXIGL Unreviewed; 457 AA.
AC A0A166BGW8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:KZW00990.1};
GN ORFNames=EXIGLDRAFT_638848 {ECO:0000313|EMBL:KZW00990.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW00990.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW00990.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW00990.1,
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KV425897; KZW00990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166BGW8; -.
DR STRING; 1314781.A0A166BGW8; -.
DR InParanoid; A0A166BGW8; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
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; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 35..205
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 457 AA; 49224 MW; A3768C671039E7D7 CRC64;
MAMSLDILSV LSSDQVLTPS NGEAYEAALQ RWSETSVRRA QLIVFPRTAE DVSKAVKYAV
AHDIEIAIKG GGHSCSGASA TTGIVIDLSN MDTVEVIPEK KLAKVGGGAL WAAVDAAAAK
HGFATVGGTV NHTGVGGLTV GGGFGFLSPK LGLAVDVLRE AEVVLANGDV VVCNASEHPD
LFWGIRGGGS NFGPVTSFTF ELFPQENAVW SGLLIFTPDK LAEVFSALKE WYAAAGENEA
ANLFIGCGPP DFKPALVVLP FYNGSVEEAK VKFGCLLDVG PVADFTQEMA YPAVNTIQHP
MTTHGDRKLF KATSFTSFSA DLFQPIFDNY SELVETFPDT RGSAVIMEFY PPNKITSVPT
GATAFPSRMA RCNINFVPRW KDAALDSKMY EWASAQVDFV RNAEKLPAAN RAYANYGFGD
ERARDVFGEN YERMAKVKAL YDPGNVFHKW YPVIPQA
//
