ID   A0A2V5I1U1_9EURO        Unreviewed;       464 AA.
AC   A0A2V5I1U1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PYI30755.1};
GN   ORFNames=BP00DRAFT_436570 {ECO:0000313|EMBL:PYI30755.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI30755.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI30755.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI30755.1,
RC   ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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; KZ825511; PYI30755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5I1U1; -.
DR   Proteomes; UP000248817; 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; PTHR13789:SF311; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10180)-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..334
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   464 AA;  50780 MW;  9395CB3BBD9B1E9C CRC64;
     MKVIIIGAEV DGLICAIACQ REQLDVIVLE QEAEIEVNAG IQIPPNGARI LHQLGLLEAV
     ARKGTSTEYL DLRRFHDGAL IRSMPWGEPV RQAYGRPWLN ITRADFLDVL LDKARQLEID
     IRHHAVVEEI HCGSAEVVLK DGARIQGDVV IGADGIYSKL RDTVLNQPCP PSPANDIAYQ
     ATISRSALKA LNDGQLDELC SKTKITTWLG SAQHTVFFPV RQGEEYMLVT YHTHSAPPAA
     AAAAAARQPT ISSADGLSQM QALHQGWDIR LQTILAHATF SSQTTQHTLH ALPTWTKARL
     ILLGPASRII PPYQAQDLAA TLEDAAVLST LLGLLAHHTP EPHQLPRLLP EILALHETLR
     KPAAVQAVRD GVLSRRVLQV GNPVGQALRN WFLGGAGITR DTDAGWLKLV SAQQEPRLGG
     GLLGETRARF EAWRTERLPL LLAAESRSSA GYGIGRKRLR CWTY
//