ID A0A1D2VH21_9ASCO Unreviewed; 484 AA.
AC A0A1D2VH21;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=NADH dehydrogenase I, D subunit {ECO:0000313|EMBL:ODV60899.1};
GN ORFNames=ASCRUDRAFT_76248 {ECO:0000313|EMBL:ODV60899.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV60899.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}.
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DR EMBL; KV454481; ODV60899.1; -; Genomic_DNA.
DR RefSeq; XP_020047206.1; XM_020193396.1.
DR AlphaFoldDB; A0A1D2VH21; -.
DR STRING; 1344418.A0A1D2VH21; -.
DR GeneID; 30967032; -.
DR InParanoid; A0A1D2VH21; -.
DR OrthoDB; 191at2759; -.
DR Proteomes; UP000095038; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685};
KW Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 214..484
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 484 AA; 55121 MW; CD307B1493544DB2 CRC64;
MLSSINCRSI TNSLKFISTR NDKAKFFIQS KRFFNKCSNS VILQKSHHHP FLDVENINNS
FGDFKPITTT LNEEFNLDNP DAINFTEDSL DAKNNSKIRH FTVNFGPQHP AAHGVLRLIL
ELKGEEIVRS DPHVGLLHRG TEKLIESKTY MQALPYFDRL DYVSMMTNEL VFCLATEKLL
NIEVPIRAKY IRTLFGEITR VLNHCMSVLS HAMDVGALTP FLWGFEEREK LMEFYERVSG
ARLHAAYFRP GGVSQDLPEG LLDDIYMWAT QFGDRIDETE ELLTDNRIWI NRLKNVGLLT
AEDALNYSCT GVMLRGSGIP YDIRKAQPYD AYELVDFDIP VGYNGDCYDR YLCRMAEFRQ
SLRIIEQCIN QMPAGPVKVE DFKINPPPRS LMKQDMEALI HHFLLFTKGY AVPQGETYTA
IEAPKGEMGV YLISDGSERP YRCKIRAPGF AHLAAFDHIA RGNSLADAVA IIGTMDLVFG
EVDR
//
