ID A0A2G5I605_CERBT Unreviewed; 752 AA.
AC A0A2G5I605;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial {ECO:0000313|EMBL:PIB00192.1};
GN ORFNames=CB0940_02905 {ECO:0000313|EMBL:PIB00192.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB00192.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB00192.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB00192.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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}.
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:PIB00192.1}.
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DR EMBL; LKMD01000101; PIB00192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I605; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000230605; Chromosome 3.
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; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Ubiquinone {ECO:0000313|EMBL:PIB00192.1}.
FT DOMAIN 35..113
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 113..152
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 252..308
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 721..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 82089 MW; 948A429456364FCE CRC64;
MRSHLLRSIP RTPALAARNG SRAARTFATT AQRQADVELT VDGRKVSVPA GTALIQACEK
AGATVPRYCY HEKLMIAGNC RMCLVEVERA PKPVASCAWP VQPGMVVKTD SPLAHKAREG
VMEFLLANHP LDCPICDQGG ECDLQDQSMR YGADRGRFHE LSGKRAVEDK NIGPLVKTSM
NRCIHCTRCV RFANDVAGAP ELGSAGRGND IQIGTYLETA LDTELSGNVI DLCPVGALTS
KPYAFRARPW ELGHTETIDV MNGLGSNIRA DSRGLQVMRI LPRLNDDVNE EWIDDRSRFA
CDGLSTQRLT TPLIRRDNQF QPATWENVLV EIKDKFDELQ PKGDEIKFVA GELVETETLV
AAKDLANKLG SENLALDFTQ GSSPVAHGVD VKTNFSFNSK IVGVEEADVI LLVGTNPRHE
AAVLNARIRK QWLRSDLEVG LVGEDFESTF EYENLGANAK DLKSALSGPF GEKLKNAQRP
LIIVGSGVTE HKDAKSIYET VGSYVEKNKA NFQTPEWNGY NVLQRAASRA GAYEVGFTVH
NPETTNTKAK VMWLLGADEI DAADIPKDTF VIYQGHHGDR GAALADVVLP GAAYTEKGAT
YVNTEGRVQM SRAVTSVYGA AREDWKIIRA VSEALGQPLP YDDVEALRDR MEEISPALRR
YDIVEPTSKE LQALSKVQLV EQNKGATVSG EPLKKPIENF YFTNTITRSS PTMARCSAAK
AAKDPSTNFQ APGEPNVTPY YGPPELAAGA SA
//
