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Database: UniProt
Entry: A0A319C6T2_9EURO
LinkDB: A0A319C6T2_9EURO
Original site: A0A319C6T2_9EURO 
ID   A0A319C6T2_9EURO        Unreviewed;       737 AA.
AC   A0A319C6T2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NADH-ubiquinone oxidoreductase, subunit G {ECO:0000313|EMBL:PYH79617.1};
GN   ORFNames=BO82DRAFT_356225 {ECO:0000313|EMBL:PYH79617.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH79617.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH79617.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH79617.1,
RC   ECO:0000313|Proteomes:UP000248340};
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   -!- 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; KZ821717; PYH79617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319C6T2; -.
DR   STRING; 1448315.A0A319C6T2; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_356225; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000248340; 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; PS00641; COMPLEX1_75K_1; 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:UP000248340};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Ubiquinone {ECO:0000313|EMBL:PYH79617.1}.
FT   DOMAIN          32..110
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          110..149
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          249..305
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   737 AA;  81022 MW;  2610D19E32236158 CRC64;
     MRPQLYRAAA RLIRVPKVNH LRTFATTFPR SAEVELTIDG KKVSVEAGSA LIQACEKAGA
     TVPRYCYHEK LLIAGNCRMC LVEVERAPKP VASCAWPVQP GMNVKTNSPL VHKAREGVME
     FLLANHPLDC PICDQGGECD LQDQSMRYGA DRGRFHEVGG KRAVEDKNIG PLVKTSMNRC
     IHCTRCVRFM NDVAGAPELG TSGRGNDMQI GTYLEKNLDS ELSGNIIDLC PVGALTSKPY
     AFRARPWELK HTESIDVHDA LGSNIRIDTR GMEVMRILPR LNDDINEEWI NDKSRFACDG
     LKTQRLTTPL IRREGKFVPA TWEQALTEIS SAHQRLHVTE NEFKAVAGHL VDAETLVAMK
     DLANKLGSDN LALDQPGGGS PVAHGVDVRS NYLFNSKIYG IEEADAILLV ATNPRHEASV
     LNARIRKQYL RSDLEIGLVG EEFESTFEFE HLGADVSALK AALSGKFGEK LSTAKRPMII
     VGSAAAEHPD AKVIFESIGN FVEKHANNFN TSEWQGYNVL QRAASRAAAY EVGFTTPSLE
     VTRSKPKMVW LLGADEVAQS EIPSDAFVIY QGHHGDRGAQ LADVVLPGAA YTEKSGTYIN
     TEGRVQVTRA ATSLPGAARD DWKIIRAASE FLNIPLPYDD IEALRDRMEE ISPVMRRYDV
     VEPTSLSSLS KVQLVDQNKG IQSTNTPFKK VINDFYFTDS ISRSSPTMAR CSAAKATGNP
     ETNFMAAGEM SPKALYG
//
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