ID   A0A2B7WUU0_9EURO        Unreviewed;       326 AA.
AC   A0A2B7WUU0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN   ORFNames=GX51_05915 {ECO:0000313|EMBL:PGH00218.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH00218.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH00218.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH00218.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:PGH00218.1}.
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DR   EMBL; PDNC01000089; PGH00218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WUU0; -.
DR   STRING; 2060905.A0A2B7WUU0; -.
DR   OrthoDB; 1447958at2759; -.
DR   Proteomes; UP000224080; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097237; P:cellular response to toxic substance; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT   DOMAIN          8..304
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   326 AA;  35014 MW;  F245213DB80EA71F CRC64;
     MASPEPVDVL IIGGGPAGLT AALSLVRQGH TAILFDSGRY RNVDVKHMHM IPTWDHQDPA
     EFRQKARSEI LNHYASVKIE DVELTAARKI NDSLFEVTDS KGGVRKGKKI ILATGSADIY
     PDIPGYADCW AKRIYHCLYC KGFEDRGTAR SGVLAVQTAS IAPMAIHVAE AAANLSSRVT
     IYTHGSEELS SQIQTSLGTT NQEKFTVDSR KISHLRLVED DGKPAGVELT FADGTSVTEG
     FLVHNPLTKV QGPFVEQLGI ETTTPEVGDI VANFPAYQTS VRGVFAAGDC ITQYKVIAGA
     ISSGCNAAVA ASAQLLAEKY QHQSLI
//