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Database: UniProt
Entry: A0A0D2EJ84_9EURO
LinkDB: A0A0D2EJ84_9EURO
Original site: A0A0D2EJ84_9EURO 
ID   A0A0D2EJ84_9EURO        Unreviewed;       433 AA.
AC   A0A0D2EJ84;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=PV05_07087 {ECO:0000313|EMBL:KIW54750.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54750.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW54750.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54750.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KN847320; KIW54750.1; -; Genomic_DNA.
DR   RefSeq; XP_013315334.1; XM_013459880.1.
DR   AlphaFoldDB; A0A0D2EJ84; -.
DR   STRING; 348802.A0A0D2EJ84; -.
DR   GeneID; 25328995; -.
DR   HOGENOM; CLU_009665_19_3_1; -.
DR   OrthoDB; 981595at2759; -.
DR   Proteomes; UP000054342; 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:UP000054342}.
FT   DOMAIN          7..170
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          294..358
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   433 AA;  48141 MW;  9A59E76B73E83D56 CRC64;
     MPEFLCHIAV IGAGLGGLAA GIGILQAGHR VSIIERAPAL AEIGAGIQVP PNTTRILKRW
     GVLEQLIKVS DRPKESVLRS YRDGRILSSL DLQKCSEELY DHPYLHVHRA DYHTVLAEEF
     RRLGGSIATN SEVTSVNFND STVQIKGGPD IKADLIIGAD GVKSISRELL LGRADPPRSS
     GDMAYRLVIR EKDIRKHPNL VDLVNSGRIN NWIGPDQHVM GYKLRDGDLF NIVIACTDTL
     PETTNMALAG AQELRDRVMG WDPDLEALVA LAYEGSKGRL MRVDEMESWV HPLGRFVLLG
     DSCHATLPYL AQGAAQAIED GAVLGHLFEK VSHASQLPDI LTIYEALRKP RTSRVVRDST
     RGRRILHLPD GPAQEERDRQ LQEERPFEGF AHAWADPAMQ EFLYGYDARK EVNRAWDVYL
     SGQFPLTTNA WKL
//
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