ID A7E8Y9_SCLS1 Unreviewed; 742 AA.
AC A7E8Y9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial {ECO:0000313|EMBL:EDN96841.1};
GN ORFNames=SS1G_01767 {ECO:0000313|EMBL:EDN96841.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN96841.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476622; EDN96841.1; -; Genomic_DNA.
DR RefSeq; XP_001597573.1; XM_001597523.1.
DR AlphaFoldDB; A7E8Y9; -.
DR SMR; A7E8Y9; -.
DR STRING; 665079.A7E8Y9; -.
DR EnsemblFungi; EDN96841; EDN96841; SS1G_01767.
DR GeneID; 5493893; -.
DR KEGG; ssl:SS1G_01767; -.
DR eggNOG; KOG2282; Eukaryota.
DR HOGENOM; CLU_000422_11_6_1; -.
DR InParanoid; A7E8Y9; -.
DR OMA; QDQAMAY; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000001312; 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 GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
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:UP000001312};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
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"
FT REGION 715..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 80831 MW; 0BF0AD0852020E97 CRC64;
MLRSTLSRSA LRGSRQSFRV ARTFATTNRR QAEVTLTVDG KQVSIEAGSA LIQACEKAGV
TVPRQVFNGK LMIAGNCRMC LVEVEKAPKP VASCAWPVQP GMVVKTNSPL THKAREGVME
FLLANHPLDC PICDQGGECD LQDQSMRYGA DRGRFHEVGG KRAVEDKNIG PLIKTSMNRC
IQCTRCIRFA NDIAGAPELG STGRGNDLQI GTYLEQNLDS EMSGNIIDLC PVGALTSKPY
AFRARPWELK HSESIDVLDG LGSNIRVDSR GLEVMRILPR LNDDVNEEWI NDKTRFACDG
LKTQRLTTPL IKKDGKFLPV SWEQALVEIG AAYKDFAPKG NEFKAIAGEL IETESMVAMK
DLANKLGSEN LALDQPSGNA PMPHGIDVRS NYLFNSKIWG VEEADVILIV GSNTRHEAAG
LNARIRKQWL RSDLEIGVVG ETWDSTFEFE HLGTDAASLK DTLAGPFGKK LADAKRPMII
VGSGVTDHAD AKAMYETVGT FVEKHASNFL TEEWNGYNVL QRAASRAGAF EVGFTTPSQA
VAETKPKFIW LLGADEFNAA DIPKDAFVVY QGHHGDRGAQ IADVVLPGAA YTEKAGTYVN
TEGRVQMTRA ATSLPGAART DWKIIRAVSE FLGAPLPYDD VAALRDRMVE ISPSLASYDV
VEPVALKQLS KVQLVDQNKG SQPTGAPLKK VIDNFYFTDV ISRSSPTMAR CSAAKETGNP
ETNFLAPGYS SENPRGRVAY GP
//
