ID A0A317WWC1_9EURO Unreviewed; 476 AA.
AC A0A317WWC1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 12.
DE SubName: Full=NADH dehydrogenase I, D subunit {ECO:0000313|EMBL:PWY89477.1};
GN ORFNames=BO94DRAFT_534252 {ECO:0000313|EMBL:PWY89477.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY89477.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY89477.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY89477.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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}.
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:PWY89477.1}.
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DR EMBL; MSFK01000011; PWY89477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WWC1; -.
DR STRING; 1450535.A0A317WWC1; -.
DR OrthoDB; 191at2759; -.
DR Proteomes; UP000246702; 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:UP000246702};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 206..476
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 476 AA; 53251 MW; 198F19A054D8FB0C CRC64;
MAASFTRLAG STPKRLCLRP STFSRHSAIP RCRTIATSLP RRAAEPTSYQ ATRLIPTDPT
FTSLANKEGP SEAEVAAGLE SEDVGAGRKI RHYTVNFGPQ HPAAHGVLRL ILELNGEEIV
RADPHVGLLH RGTEKLIEYK TYMQALPYFD RLDYVSMMTN EQCFSLAVEK LLNIEIPDRA
KYIRTLFGEL TRILNHLMSV LSHAMDVGAL TPFLWGFEER EKLMEFYERV SGARLHAAYV
RPGGVSQDLP LGLLDDIYQW ATQFGDRIDE TEELLTDNRI WKARTQGVGV VPAADALNMS
FTGVMLRGSG VPWDIRKSQP YDAYDQVEFD VPVGVNGDCY DRYLCRMEEF RQSLRIIHQC
LNQMPAGPVR VEDYKISPPP RAAMKENMEA LIHHFLLFTK GYAVPPGETY SAIEAPKGEM
GVFLVSDGSE RPYRCKIRAP GFAHLGGFDQ VSRGHLLADA VAIIGTMDLV FGEVDR
//
