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Database: UniProt
Entry: A0A2S4L6S2_9HYPO
LinkDB: A0A2S4L6S2_9HYPO
Original site: A0A2S4L6S2_9HYPO 
ID   A0A2S4L6S2_9HYPO        Unreviewed;       762 AA.
AC   A0A2S4L6S2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial {ECO:0000313|EMBL:POR38143.1};
GN   ORFNames=TPAR_01669 {ECO:0000313|EMBL:POR38143.1};
OS   Tolypocladium paradoxum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=94208 {ECO:0000313|EMBL:POR38143.1, ECO:0000313|Proteomes:UP000237481};
RN   [1] {ECO:0000313|EMBL:POR38143.1, ECO:0000313|Proteomes:UP000237481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR38143.1,
RC   ECO:0000313|Proteomes:UP000237481};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (JAN-2018) 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:POR38143.1}.
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DR   EMBL; PKSG01000166; POR38143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4L6S2; -.
DR   STRING; 94208.A0A2S4L6S2; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000237481; 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:UP000237481};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Ubiquinone {ECO:0000313|EMBL:POR38143.1}.
FT   DOMAIN          32..130
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          130..169
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          269..325
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   762 AA;  83470 MW;  146B5B30F9E8A96B CRC64;
     MLRQSLARSA WRTGRRAANA SRAFATTPQR QAEVELTVGE HPWVRAAIER LRGANTVLDG
     KKVSIEAGSA LIQACEKAGV TIPRYCYHEK LMIAGNCRMC LVEVERAPKP VASCAWPVQP
     GMVVKTNSPL THKAREGVME FLLANHPLDC PICDQGGECD LQDQSMRYGA DRGRFHEIGG
     KRAVEDKNIG PLIKTSMNRC IHCTRCVRFA NDIAGAPELG STGRGNDLQI GTYLEKNLDS
     ELSGNVIDLC PVGALTSKPY AFRARPWELK HTESIDVLDG LGSNIRVDSR GLEVMRVLPR
     LNDDVNEEWI NDKTRFACDG LKTQRLTMPL VRREGKFEPA DWEEALTEVA RAWEQKKPQG
     NEFKIISGAL TEVESLVVAK DMANRLGSDN LALDTPTGSQ PLAHGVDVRS NYLFNSRIWG
     IEDSDCILIV GSNPRHEAAV LNARIRKQWL RSDLEIGVVG ETWDSTFEFE HLGTDHAALK
     QALAGPFGKK LQAAKKPMII VGSGVTDHAD AKAFYETVGA FVDKNSANFM TEEWDGYNVL
     QREASRAGAF EVGFVTPSTT VAETKPKFVW LLGADEFSEA DIPKDAFVVY QGHHGDRGAQ
     IADIILPGAA YTEKAGTYIN TEGRVQMTRA ATSLPGAART DWKILRAASE FLGAPLPYDD
     VAAVRDRMVE ISPALAAYDV VEPVALRQLS KVQLVDQNRG SKASGSPLKK VIDNFYFTDV
     ISRSSPTMAR CSAAKATGDP RTNLMAPGME EDKPMGQIAY GV
//
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