ID   A0A421DD45_9EURO        Unreviewed;       427 AA.
AC   A0A421DD45;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=CFD26_107831 {ECO:0000313|EMBL:RLM00030.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLM00030.1, ECO:0000313|Proteomes:UP000215289};
RN   [1] {ECO:0000313|EMBL:RLM00030.1, ECO:0000313|Proteomes:UP000215289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00030.1};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLM00030.1}.
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DR   EMBL; NIDN02000021; RLM00030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421DD45; -.
DR   STRING; 1245748.A0A421DD45; -.
DR   Proteomes; UP000215289; 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:SF242; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..427
FT                   /note="FAD-binding domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019095693"
FT   DOMAIN          9..354
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   427 AA;  47241 MW;  C74940078E2432DD CRC64;
     MPHASRSLNV LVVGAGLGGL AAGLALQTDG HKVTIIDAAP EFAEAGAGIR IPPNSSRLLM
     RWGVDLERMK KSTSQRYHFI RWKDGSTIFD LPFTNIVETH GAPYWLVHRA DLHAALLDAA
     LKAGVKILTN KRVTSYDFDA PSATTQDGET FKADLIVGAD GIKSICRPLL TGQPDIPRDT
     GDVAYRILIP GEKLLADPEL AHLIRDPCTT SWCGPDAHLV GYPIRNGEMY NVVVCATSHN
     ETTDEVWVVK GDNSELCKRF ASWEPQVRKL CALTGDFMKW RLCDLPNLTR WTHPSGKAVL
     LGDSCHPMLP YLAQGAAQAF EDAAVLRQVL AQDVPMAAAL KQYEQIRMPR ASLVQAKTRE
     HQYILHVDDG QEQQDRDKKL ALDAAENPVF WGYGDRRKWL FSHDAEVIQK EGANWRDGPN
     MNGVHVS
//