ID A0A0N0NMD7_9EURO Unreviewed; 438 AA.
AC A0A0N0NMD7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=AB675_7467 {ECO:0000313|EMBL:KPI40341.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI40341.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI40341.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI40341.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI40341.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000012; KPI40341.1; -; Genomic_DNA.
DR RefSeq; XP_018000304.1; XM_018147836.1.
DR AlphaFoldDB; A0A0N0NMD7; -.
DR STRING; 1664694.A0A0N0NMD7; -.
DR GeneID; 28739716; -.
DR OrthoDB; 2069230at2759; -.
DR Proteomes; UP000038010; 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:SF29; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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:UP000038010};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..438
FT /note="FAD/NAD(P)-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005856853"
FT DOMAIN 36..181
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 438 AA; 47810 MW; 61DA2B3B02206202 CRC64;
MMVFALAWQL ACLFASFSTL TFTHPISGQA WTDAWDVVVI GGGPAGLSAT SGLARVRRNV
LMLDSGEYRN GQTRHMHDVI GNDGTVPAAF RALARQQILR YPTVQMANAT VTNITGNAST
KFTIQTSDGN VFTASKVVIA TGIKDVMPST PGIAENWGKG IYWCPWCDGY EHRDQPYGII
GSYADVLDSV FEVHTLESDI IAFVNGTQTA ETIAKVNSNP PAGYGDWEKK LQKYGIKIEN
RTMASVTRLQ DGSVVQSADG MTEYDKFLVT FTDGSTIERG AFIANFPSVQ RSGLGASLGI
PYNAKQHLKT DGQMESVVPG VFVVGDANAD NSTNVPHAMW SGKRAAVQIH NALEQERSDD
LIKKRSRLSE EEVDRIMGRD LLDIYSSEHT RIIEHIIVVT FAHAILEAAV LIMSFQRMDE
LEAAHNGPRV RGAGIRPV
//
