ID   A0A0N4ZPZ0_PARTI        Unreviewed;       782 AA.
AC   A0A0N4ZPZ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial {ECO:0000256|ARBA:ARBA00013888};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001059700.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001059700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0N4ZPZ0; -.
DR   STRING; 131310.A0A0N4ZPZ0; -.
DR   WBParaSite; PTRK_0001059700.1; PTRK_0001059700.1; PTRK_0001059700.
DR   Proteomes; UP000038045; Unplaced.
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   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          85..163
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          163..202
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          303..359
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   782 AA;  85406 MW;  D37D4DA87993EB46 CRC64;
     MCCGDPFGSH YDSPVIIRQQ AVIASPGYGQ TRIYSNGYGN LPKMLSNGGR ITSRLLKASI
     LGRGSSQQNQ TTVASQSTTP VKEPEKIEVF INDKPIMVDP GMTILQACAI ADIDIPRFCY
     HDRLSIAGNC RMCLVEVEKS IKPVASCAMP VMKGMRVKTH SDYAKKAREG VMEFLLVNHP
     LDCPICDQGG ECDLQDQSMA FGSDRSRLQS DFDGKRGVED KDIGPLVKTS MNRCIQCTRC
     VRFANEVAGI PDFGTTGRGN GLQIGTYVEK LLATELSGNV IDLCPVGALT SRPYSFMARP
     WETRKTESID VMDSLGSNIV ITHRTGEVFR IIPRMNDDVN EEWISDKTRF AVDGLKRQRL
     TQPMLKKGGQ LVPVSWEEAL FTVASKLKET PPNKSVAVAG GLNDAESMIA LKDLFNKLNS
     EGVYSEDHFP TSSGSIDIRA NYIMNDKIAG IEEADALLLV GTNPRYEAPV LNARIRKTYL
     ASPIEIGVIG SEVDLTYDYE YLGSNASILD NLSSTEFGKK LFSSKSPMII VSSDSLKGED
     GAKLLGNLQT IASKVQGQSQ KAVINVLAKT ASQTAAFDIG LKPFNALEDS SNIKLLYLLG
     ADETGLDRSK LDKDCFVIYQ GHHGDSGAEN ADVILPGAAY TEKDGIYVNT EGRPQRGFPA
     ITPPGEGRVD WKIIRAISEV AGVKLPYDTL PEVRDRLTQI APHFSKNGVV DSTGFLKQAL
     QLADTGKINK DVSVKQTKLE HFYMTNTVSR ASPTMAECVK AAINYNKDPH KDTFEEHHAV
     AN
//