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Database: UniProt
Entry: A0A1Y2VXN7_9PEZI
LinkDB: A0A1Y2VXN7_9PEZI
Original site: A0A1Y2VXN7_9PEZI 
ID   A0A1Y2VXN7_9PEZI        Unreviewed;       422 AA.
AC   A0A1Y2VXN7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=M426DRAFT_25407 {ECO:0000313|EMBL:OTB01641.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB01641.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB01641.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB01641.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; KZ111579; OTB01641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VXN7; -.
DR   STRING; 1001833.A0A1Y2VXN7; -.
DR   InParanoid; A0A1Y2VXN7; -.
DR   OrthoDB; 1849844at2759; -.
DR   Proteomes; UP000242955; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.9.60; -; 1.
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; PTHR47469; MONOOXYGENASE-LIKE; 1.
DR   PANTHER; PTHR47469:SF2; OS06G0597600 PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242955}.
FT   DOMAIN          139..257
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   422 AA;  47079 MW;  7DF96F7DC7866866 CRC64;
     MAPQKVIIIG GSVAGLLQGL QLKRQGSHVV VLEQDPSKDR ASHESGVSIG KTVVSILDKY
     DATGRPAAIP AEYMSASWRQ LRRIANMSWK HNMSNWGTLY LILRANFDGL KSTCVSNPPE
     PKPTDGKVEY HAGKQVYGVS YNQDEGLVTV SYSDVVTGEK DSINAEMVIA ADGVHSTVRQ
     LMQAPTRKEY SGYIGWRGTV RESLLSKETI EFFSNRLNFT LLGGHYFISY LIPTETGHTE
     PGHRLLNWVW YYVVPDGSPE MEAIFTDVNG KVHPNTVPQG LVNPVVWKAQ IARWMPLMTA
     PLAEVVSNTP QPFVTKVIEA QTKKASFFDG RLVLVGDAFT GFRSHLGWAS EQAARHAVAL
     DRVWKGEITM KQRDEEAALY AQRFIHLNRM MGFTGMGWVA SFLRNALAYM WLMISHYIST
     LV
//
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