ID   A0A1J7IP57_9PEZI        Unreviewed;       314 AA.
AC   A0A1J7IP57;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OIW28971.1};
GN   ORFNames=CONLIGDRAFT_645117 {ECO:0000313|EMBL:OIW28971.1};
OS   Coniochaeta ligniaria NRRL 30616.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW28971.1, ECO:0000313|Proteomes:UP000182658};
RN   [1] {ECO:0000313|EMBL:OIW28971.1, ECO:0000313|Proteomes:UP000182658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW28971.1,
RC   ECO:0000313|Proteomes:UP000182658};
RG   DOE Joint Genome Institute;
RA   Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA   Van Elsas J.D., Nichols N.N.;
RT   "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT   lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT   hydrolysates.";
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; KV875098; OIW28971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J7IP57; -.
DR   STRING; 1408157.A0A1J7IP57; -.
DR   InParanoid; A0A1J7IP57; -.
DR   OrthoDB; 1447958at2759; -.
DR   Proteomes; UP000182658; 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:UP000182658}.
FT   DOMAIN          6..295
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   314 AA;  33874 MW;  1EB6BA206C3D6C48 CRC64;
     MAKALYDCLV IGAGPAGLAA ATSLARLQHT CLVFDPGVYR NALVKHMHNV LGWDHRDPAD
     YRAQARQDIA KRYSQFVTFQ TATIQQVRKL ESGQFEAVDE SGNVYCGKKL CLATGVRDIM
     PDIPGYADCW TKGIFHCLFC HGYEDRGKQS AGVLAMPLVS EASFALHFGN NALQLADKLT
     IYTNGDSVMT TRLREALVKP DPRITLESRK IARLSMKSGD ASDVIVTFDD GSTTTEGFIA
     HHPTVEINGP FASQLLLELS PTGEIKTTPP FNRTSLEGVF ACGDAATMIR AVGQAAIMGS
     MAAAGIASQV EAEK
//