ID   A0A3F3QB44_9EURO        Unreviewed;       414 AA.
AC   A0A3F3QB44;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:RDH36307.1};
GN   ORFNames=BDQ94DRAFT_167925 {ECO:0000313|EMBL:RDH36307.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH36307.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH36307.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH36307.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; KZ852038; RDH36307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QB44; -.
DR   STRING; 1341132.A0A3F3QB44; -.
DR   OrthoDB; 1815741at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR47178:SF4; FAD-DEPENDENT MONOOXYGENASE APTC; 1.
DR   PANTHER; PTHR47178; MONOOXYGENASE, FAD-BINDING; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT   DOMAIN          4..173
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          306..354
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   414 AA;  45463 MW;  3190EBED35D4E999 CRC64;
     MTPPILIIGA GLSGLTVSRI LTNASIPNIV FEASTPDRSQ GYAISLREWG YTSLLTALGD
     LPLRSLTRGV APDRILGGTG WIDQALRDNH TGNLLVAPDP EAKQCIVRAN RNALRTWIAD
     SGDEEVDIRY GHRLSSVQGS MGNVTATFEN GAKYQGSLVI AADGVHSSVR SQILPHVSPD
     IVPVVVYHGE LELPRKEFDN LIRPHSGPSN ILAGVGDGFN TPITVCNITP THVHLDWSYS
     RPSTENKENK DPLYRPHVSA AEAKQIPPAL LEEIASRDLA RPWSQLLNAE ALPTHRVFNW
     VSRCVSVTRE DVNAAQKQGV VFIGDSWHAM PIFGGEGGNH ALVDAVELAE ALAGKEGDLD
     AAVTGYYDRA WRRCQEAVRR SRQRFFQLHR PMREWMEIAE KKKMMAAMKG VEAH
//