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Database: UniProt
Entry: A0A397HGY5_9EURO
LinkDB: A0A397HGY5_9EURO
Original site: A0A397HGY5_9EURO 
ID   A0A397HGY5_9EURO        Unreviewed;       450 AA.
AC   A0A397HGY5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=CDV56_103984 {ECO:0000313|EMBL:RHZ60794.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ60794.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ60794.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ60794.1,
RC   ECO:0000313|Proteomes:UP000215305};
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 sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
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:RHZ60794.1}.
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DR   EMBL; NKHU02000048; RHZ60794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397HGY5; -.
DR   STRING; 41047.A0A397HGY5; -.
DR   VEuPathDB; FungiDB:CDV56_103984; -.
DR   OrthoDB; 981595at2759; -.
DR   Proteomes; UP000215305; 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; MONOOXYGENASE; 1.
DR   PANTHER; PTHR13789:SF238; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01680)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
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:UP000215305}.
FT   DOMAIN          9..214
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          317..375
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   450 AA;  50495 MW;  E42F0973BA799384 CRC64;
     MVSEEAHLRI IIAGAGLGGL AAAVSCALSG HTVEVVEQAK ELVEVGAGLQ ITPNASRLFK
     YWQLPNSIWE AAAEPTALTV HRYTGQILAN EPSFHKNIRA KYNAPFIDLH RVDLQQALYI
     RAKELGVTFH LNERVDSIDF DTTTVKTLAG NQYTGDLIIA ADGLWSRSRE CFLGKKDVPL
     PTGDLAYRIV LTADQISDPE LRAWVENPEC HFWIGPGAHV VAYSLRNGRM FNIVLLVPDN
     LPPGVSRQSG SVEEMRKLFE GWDPVLNRFL SYVDSVDKWK LMHHAEMESW VNDKSNLVFL
     YGSHRVFDTD QLTHTSGDAC HPMLPYLAQG ANSSLEDGAV LGQLLGHMKN KSHLPQILRL
     YESLRKSRGE AIVKETFKQR HDFHMPNGEE QEKRDEVFMS QLGKEIKGAF PSRWTCPEVQ
     PWLYGYDAVK EVEKAVTQHP ELFAKTSANL
//
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