ID T1L5I4_TETUR Unreviewed; 758 AA.
AC T1L5I4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial {ECO:0000256|ARBA:ARBA00013888};
GN Name=107370431 {ECO:0000313|EnsemblMetazoa:tetur47g00180.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur47g00180.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur47g00180.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; CAEY01001294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015793915.1; XM_015938429.1.
DR AlphaFoldDB; T1L5I4; -.
DR STRING; 32264.T1L5I4; -.
DR EnsemblMetazoa; tetur47g00180.1; tetur47g00180.1; tetur47g00180.
DR GeneID; 107370431; -.
DR KEGG; tut:107370431; -.
DR eggNOG; KOG2282; Eukaryota.
DR HOGENOM; CLU_000422_11_6_1; -.
DR OMA; QDQAMAY; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000015104; 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 Gene3D; 3.10.20.740; -; 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:UP000015104};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 55..134
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 134..173
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 275..331
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 29..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84364 MW; 652F6E525B1E4B1E CRC64;
MLRSVVNQSF YRRLLASSVK NESGFVRSFA SKSEERKQAS TASPATKESS KPQPEMIEIF
IDDKPYQVEK GITILEACTV AGVEVPRFCY HERLSIAGNC RMCLVEVEKS IKPVASCAMP
VMMPGMRVKT NSPAAKKARE GVMEFLLLNH PLDCPICDQG GECDLQDQSM AYGTDRSRLL
IAVDEKRAVE DKDIGPLVKT IMNRCIHCTR CVRFMNEIAG VSDLGTTGRG SDMQIGTYLE
NNVLATELSG NIVDLCPVGA LTSKPYTFTA RPWELRRFDS IDVMDAVGSN ISVCQRGGDL
LRVIPRANDD VNEEWLGDKS RHAPVDGLKN QRLTVPLVRP SRGSPLQQCD WEDALLTVSQ
VFNKIPPERI EIIAGPMIDA ETLVAIKDLS SSMNCNNYYV HVDSNVEPSC IPSAEDRKFR
SNYLFNTTIA GIEDEVDLIL LVGTNPRYEA PLVNARIRKA WRNHVIDDIA LIGPKDLDLS
YDYEWLGSDS KVLESVADGK HAMSQRLSKA KRPIVILGQQ ILKEGDGKSN IFETVRYICD
KYGAELNVLH TNASQVAAYD LGFKPSTERT PLAKSDEPSL LWLIGVDDEN LDLGSNPFII
YQGHNGDICA NKADLVLPGA AFTEKQVTYV NMEGRVQQTL AAITPPVMSR EDWKIVRACG
EIAGHLLPYD TLIDIRGRMA QLAPHLVQHD YRKLNLPSSP SPPKATQYRK SDKPINLMPK
LRNLIDYYQT DSISRSSPTM AKCIAAVQKE YEKRSSKW
//
