ID A0A165I1J2_EXIGL Unreviewed; 383 AA.
AC A0A165I1J2;
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:KZV92768.1};
DE Flags: Fragment;
GN ORFNames=EXIGLDRAFT_718037 {ECO:0000313|EMBL:KZV92768.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV92768.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV92768.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV92768.1,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV426002; KZV92768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I1J2; -.
DR STRING; 1314781.A0A165I1J2; -.
DR InParanoid; A0A165I1J2; -.
DR OrthoDB; 5491711at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; PTHR46972; MONOOXYGENASE ASQM-RELATED; 1.
DR PANTHER; PTHR46972:SF1; RHODANESE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 9..167
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 290..337
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT NON_TER 383
FT /evidence="ECO:0000313|EMBL:KZV92768.1"
SQ SEQUENCE 383 AA; 41038 MW; C5A984AA4BDC920B CRC64;
MSTTFSPRIA IIGGGPAGLV LVNVLARNNI AATLYERDAE FSSRAHLGET GQAAMKGAGV
WETFQKNSRP EGEETKMLDK DGNVVYHHVP PPDNTSPSRP EIDRSMLRKI LLDAAPAGSV
KFGHAFVSAT PVTGTAQWEL VFANGHKTVV DLVVGADGAH SRIRPLVSDV RIRYVGLTGV
EVSMSPDVGA AHKELLARIG SGSAYALDGP KFLAAQINGD GRVRMYAWFH SDDPDVVPSD
PAAAIPFILS HYEGWAPWMR QLIELADPQA VYRRPLYMLP VGHSWTHRAG VTLVGDAMNL
MTPFAGQGAN IAVWAALQLA LKIIGVRESG GGLQEMDAAV AAYEQEAGKR AKEEAFVTEV
NMNRVLNGEG AQGMAEALRL IEG
//
