ID   A0A395H821_9EURO        Unreviewed;       659 AA.
AC   A0A395H821;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:RAL04057.1};
GN   ORFNames=BO80DRAFT_462203 {ECO:0000313|EMBL:RAL04057.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL04057.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL04057.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL04057.1,
RC   ECO:0000313|Proteomes:UP000249402};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036596};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KZ824425; RAL04057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395H821; -.
DR   STRING; 1448316.A0A395H821; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_462203; -.
DR   OrthoDB; 9164at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 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:UP000249402}.
FT   DOMAIN          238..505
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          39..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  72330 MW;  CB9452B04A7CD709 CRC64;
     MGMVDDIGCL SLIAFHAVLP PSRPATSRTS FAPNVEHASI PLSSTSHPDN PVPEEPRGVR
     SLSITDMNFT NFTISAPSSP ETDTAGSESA SSVQTPATEI QSDAEELTAD GPEKQRRAST
     VLISQNSDDM RRILENVGSS GTQKLQPLCC GGGCCRSQPL RGITAPVVGV KPVTPPDNKA
     YQCLNLRVDY LTLDSELSNV APLPEKTVSF SPVPASAVDM KLGPADHPPT FVQPHPPYNV
     YRAPLYHARE LTQAGAEKRT YHFDIDVTDY PAESGNVDFI VGGAIGVCPK NKEEEVDDIF
     NQLGVPKFMR DKKITVRTEK GRWPTIWGDD QPRELITTRR ELLNWCSDIQ SYAPTKDLFR
     LLGEYASEPN EKKILMFLAS AQGQGAFCDL RTSSHITVSQ LLHAFPSSHP PLDHLLSVLN
     TLMPRFYSLS QDPLLSCKQK GSETRRVVEV AVSVAESKDW KGGLRTGVGS GYLERVARQL
     IEAEKKGIDP RTLNLTVPMF RGLMANPLAK RFASDGPMLL IGAGVGIAPF RGFVQRRLQS
     ANCANKVWVL QGVRDSLLDE LYRGEWGVEE EKVRTVVQSR RGESKYVQEE VRNQADLVWY
     VINALDGRVF VCGSGKGMGE GVEAALIDVA MAKGNLNMEE ATLFWDNKKE AGQYIAETW
//