ID H6BP42_EXODN Unreviewed; 589 AA.
AC H6BP42;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:EHY53269.1};
GN ORFNames=HMPREF1120_01463 {ECO:0000313|EMBL:EHY53269.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53269.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53269.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53269.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; JH226130; EHY53269.1; -; Genomic_DNA.
DR RefSeq; XP_009153730.1; XM_009155482.1.
DR AlphaFoldDB; H6BP42; -.
DR STRING; 858893.H6BP42; -.
DR GeneID; 20306102; -.
DR VEuPathDB; FungiDB:HMPREF1120_01463; -.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; H6BP42; -.
DR OMA; QIPAQKD; -.
DR OrthoDB; 1434722at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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:SF42; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 125..459
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 589 AA; 66059 MW; 4952A6C631C85174 CRC64;
MASKLPLRMK PASFASASRR SLASLASSSV RKTASSPFVS RQSPILPRAV FRQSFRRTYA
ENAAPQAPQA ILSPAAKPKK RFRFFRTIWR VTYLSLLAAA GYTGYKIWEH NNPIEQADPD
PNKKTLVILG TGWGSVSLLK NLDTENYNVV VVSPRNYFLF TPLLPSCTTG TIEHRSIMEP
IRNILRHKKA KVTFYEAECT KIDYEKKVVH VKDNSEIKGD TMETEIPFDM LVVGVGAENA
TFGIPGVREH ACFLKEVGDA QKIRKRIMDC VETATFKDQP PEEVKRLLHM VVVGGGPTGV
EFAGELQDFF QEDLLKWVPQ IKDDFHVTLV EALPNLLPMF SKQLIEYTES SFKEEHIEIR
TKTMVKNVTD KYIEAEVQQP DGTKQIEKIP YGLLVWATGN ALRPVVKDLM SQIPAQAKAR
RGLEVNEYLV VNGTENIWAV GDCAVANYAP TAQVAAQEGA FLARLFNTMA KTDAIEAELR
ELSAKQAAAT GDERNAILNE IRERQRQLRR IKQIGPFQYS HQGSLAYIGA EKAVADVSWF
SGNIASGGTL TYLFWKSAYL SMCFSARNRI LVAFDWTKAK FFGRDVSRE
//