ID C6H9Z9_AJECH Unreviewed; 479 AA.
AC C6H9Z9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE SubName: Full=NADH dehydrogenase I {ECO:0000313|EMBL:EER43132.1};
GN ORFNames=HCDG_03030 {ECO:0000313|EMBL:EER43132.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER43132.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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; GG692421; EER43132.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H9Z9; -.
DR STRING; 544712.C6H9Z9; -.
DR VEuPathDB; FungiDB:HCDG_03030; -.
DR eggNOG; KOG2870; Eukaryota.
DR HOGENOM; CLU_015134_1_1_1; -.
DR OMA; IMGTSME; -.
DR Proteomes; UP000002624; 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:UP000002624};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 209..479
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 41..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53513 MW; 992667E700CEA2F7 CRC64;
MASPLTYFAR HASKRLCLGP SSSSVLRASS IAGLRSVSTS PALNATPAYR PTRLIPTDPE
FAPGGSKHQP NKPSGSYSEP SALESDAGHG RKIRHYTVNF GPQHPAAHGV LRLILELNGE
EIIRADPHVG LLHRGTEKLI EYKTYMQALP YFDRLDYVSM MTNEQCFSLA VEKLLNVEIP
DRAKWIRTLF GEITRILNHL MSVLSHAMDV GALTPFLWGF EEREKLMEFY ERVSGARLHA
AYVRPGGVHQ DIPLGLLDDI YQWATQFSDR IDETEELLTD NRIWKARTQG VGVVTAAEAL
NYGFTGVMLR GSGVPWDIRK SQPYDAYGEV EFDVPVGVNG DCYDRYLCRM EEFRQSLRII
HQCLNKMPAG PVRVEDYKIS PPPRAAMKEN MEALIHHFLL FTKGYAVPPG ETYSAIEAPK
GEMGVYVVSD GSERPYRCKI RAPGFAHLSC FDQISRGHLL ADAVAIIGTM DLVFGEVDR
//
