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Database: UniProt
Entry: A1C4P7_ASPCL
LinkDB: A1C4P7_ASPCL
Original site: A1C4P7_ASPCL 
ID   A1C4P7_ASPCL            Unreviewed;       732 AA.
AC   A1C4P7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=NADH-ubiquinone oxidoreductase {ECO:0000313|EMBL:EAW14665.1};
GN   ORFNames=ACLA_000760 {ECO:0000313|EMBL:EAW14665.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14665.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW14665.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
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DR   EMBL; DS027004; EAW14665.1; -; Genomic_DNA.
DR   RefSeq; XP_001276091.1; XM_001276090.1.
DR   AlphaFoldDB; A1C4P7; -.
DR   STRING; 344612.A1C4P7; -.
DR   EnsemblFungi; EAW14665; EAW14665; ACLA_000760.
DR   GeneID; 4708398; -.
DR   KEGG; act:ACLA_000760; -.
DR   VEuPathDB; FungiDB:ACLA_000760; -.
DR   eggNOG; KOG2282; Eukaryota.
DR   HOGENOM; CLU_000422_11_6_1; -.
DR   OMA; QDQAMAY; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR   InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   InterPro; IPR015405; NDUFS1-like_C.
DR   NCBIfam; TIGR01973; NuoG; 1.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   Pfam; PF09326; NADH_dhqG_C; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR   PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          32..105
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          105..144
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          244..300
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   732 AA;  80087 MW;  1AA81DDF9081C79F CRC64;
     MRPQLFRAAA RSFRVPKSNN FRTFATTTPR SAEVELTIDG KKVSVEAGSA LIQACEKAGV
     TVPRKLMIAG NCRMCLVEVE RAPKPVASCA WPVQPGMNVK TNSPLVHKAR EGVMEFLLAN
     HPLDCPVCDQ GGECDLQDQS MRYGADRGRF HEVGGKRAVE DKNIGPLVKT SMNRCIHCTR
     CVRFMNDVAG APDLGTTGRG NDMQIGTYLE KNLDSELSGN IIDLCPVGAL TSKPYAFRAR
     PWELKHTESI DVHDALGSNV RIDTRGMEVM RVLPRLNDDI NEEWIDDKSR FACDGLKTQR
     LTTPLIRKEG KFAPATWEQA LTEISNAQQK LQLKENEFKA VAGHLVDAET LVAMKDLANK
     LGSDNLALDQ PGGSSPIAHG IDVRANYLFN SKIYGIEEAD VILLVATNPR HEAAVLNARI
     RKQYLRSDLE IGLIGEDFES TFDYEHLGSD VSSLKAALSG KFGEKLASAK RPMIIVGSAA
     AEHQDAKAVF ETVGSFVDKH AKNFNTSEWQ GYNVLQRAAS RAAAYEVGFT TPSAEVAKTT
     PKMVWLLGAD EISQSELPSD AFVIYQGHHG DRGAQLADVV LPGAAYTEKS GTYINTEGRV
     QITRAATSLP GAARDDWKII RAASEFLDSP LPYDDIEALR DRMEEISPIM RRYDVVEPTS
     LSSLSKVQLI DQNKGAQPSG TPFKNVIEDF YFTNPIARSS PTMARCSAAK ATGNPETNFM
     AAGEMSPQAL YG
//
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