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Database: UniProt
Entry: A0A2G7FHS5_9EURO
LinkDB: A0A2G7FHS5_9EURO
Original site: A0A2G7FHS5_9EURO 
ID   A0A2G7FHS5_9EURO        Unreviewed;       522 AA.
AC   A0A2G7FHS5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:PIG80172.1};
GN   ORFNames=AARAC_003751 {ECO:0000313|EMBL:PIG80172.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG80172.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG80172.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG80172.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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:PIG80172.1}.
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DR   EMBL; NEXV01000632; PIG80172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G7FHS5; -.
DR   STRING; 656916.A0A2G7FHS5; -.
DR   OrthoDB; 845at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF17; NADH DEHYDROGENASE (EUROFUNG); 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:UP000231358}.
FT   DOMAIN          36..352
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   REGION          126..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  58479 MW;  E853C4801092D3EF CRC64;
     MPRSSENYQI YASTCAVAEL SRRDSGAEAL REGKERVVIL GSGWGGYTLS RKLSPKSFSP
     VVISPRSYFV FTPLLTDAAG GSLDFSNIVE PVRDPHAKVD FIQAAARAVN LEKKTILCES
     TVVTSGVTET PRTHENERES EEGPDTTSMR PMQEARRWEK GDFFEVPYDK LVIAVGAVSK
     TFNTPGVRHN AMFFKDIGDA RRVRRRVREC FELAVLPTTT PEMRKWLLHF AIVGAGPTGT
     ELAASLRDFI YKDMTILYPA LKNLPRITLY DVAPKVLSMF DESLSKYAME TMKKEGIDIK
     TSHHVEGLRW GEPGAEPPYE MDPKRCLTIT TKEEGEVGIG MCVWVTGNAM NKFVNKALQD
     VETFPSASTL LKDGTQPPPE LTTDTTWHIK KAPKVGALLV DGQLRVQLET PTAKSPFSKT
     SSLSATTQEA KWLATRLNKG DLQTSQPFSF HNMGTLAYIG DANALMQFPT EDDKPPKYLT
     GRMAWFVWNS AYLTMSMSWR NKLRIAFRWL LNNIFGRDVS RY
//
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