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Database: UniProt
Entry: A0A2P6TYS6_CHLSO
LinkDB: A0A2P6TYS6_CHLSO
Original site: A0A2P6TYS6_CHLSO 
ID   A0A2P6TYS6_CHLSO        Unreviewed;      1446 AA.
AC   A0A2P6TYS6;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=NADH:ubiquinone oxidoreductase 76 kDa subunit {ECO:0000313|EMBL:PRW59214.1};
GN   ORFNames=C2E21_2074 {ECO:0000313|EMBL:PRW59214.1};
OS   Chlorella sorokiniana (Freshwater green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW59214.1, ECO:0000313|Proteomes:UP000239899};
RN   [1] {ECO:0000313|EMBL:PRW59214.1, ECO:0000313|Proteomes:UP000239899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX   PubMed=29178410; DOI=10.1111/tpj.13789;
RA   Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA   Barney B.M.;
RT   "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT   conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL   Plant J. 93:566-586(2018).
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:PRW59214.1}.
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DR   EMBL; LHPG02000004; PRW59214.1; -; Genomic_DNA.
DR   STRING; 3076.A0A2P6TYS6; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000239899; 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   CDD; cd00464; SK; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 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   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
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   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000239899};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Ubiquinone {ECO:0000313|EMBL:PRW59214.1}.
FT   DOMAIN          349..427
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          427..466
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          564..620
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          219..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1251..1265
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1293..1313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1403..1417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1446 AA;  152683 MW;  38AC77F68B2DFDF2 CRC64;
     MQAVITAQPP AAAAPCHSRR LQPAAALCSP AASSQRSAAA LPRRQLARQA VCSWQRQRAA
     RPVAAAAAPR DFDKDRFESA NKDYAKLTQQ IEDTATEVVE GLQGTSLFLV GMMGSGKSTV
     GKLVAQAIGY CFFDTDVLIE SVTNKQVREI FAEDGEDNFR EIETQVLAEL SPFKNCVIAT
     GGGVPTRAEN WGHMQGGITV WLNGQPTLLA HRVVGDGTES RPLLSQSGEQ SDAEQQQQVD
     EYTAAVARLT ALLDERRPLY QDADITVSLE GSGPDADIGA PAMEVAYRVL SAINQRIKDD
     AEERKRRMDF EIVREDLPAT MTRLRQLRGV QGWQLRGLAA AAQPAPADDL IECIVDGKPV
     KVPKGANVLS ACTAAGVDVP RFCYHERLSI AGNCRMCLVE VEKSPKPVAS CAMPAAPGMN
     IKTDTPLVKK AREGVMEFLL INHPLDCPIC DQGGECDLQD QSMVFGSDRS RFTEVKRAVS
     DKNLGPLVKT VMTRCIHCTR CIRFAKEIAG TDDLGITGRG RDAEVGTYVE KLMTSELSGN
     VIDLCPVGAL TSKPAAFTYR NWELKTTESV DTSDAMGANI RVDSRGVEVI RIVPRLNEEV
     NQEWISDKAR FQYDALRYQR LNMPYVKGDK GLQQATWPEA FAAIQKAVAG MKGGEMRAIA
     GKLADAESMV ALKDLFNRLG AGDLRSEGGF PDFDADVRSN YLFNSSIAGI DSADAILLIG
     TNPRIEAPVL NARIRASNLA GVPVAVVGQQ YDLTYPVEHL GEGADALDKL LKGDYLKRLK
     GAQRPLVVVG PGVLQRNDRD AVLQKVHKVV EKADVVREGW NGFNVLHDTA SRVAALDIGF
     LPSARARASS TAPKLVYLLG ADDFSEADVP ADAFVIYQGH HGDRGAARAN VVLPATAYTE
     KFATYVNFEG RPQSTKTAVP SVGDARDDWK IVRAVSEVVG APLPYNSLED VRRRLADVAP
     HFGRRDAVEA PLWLNGEYFK AFAERAKAAK TGGQPLATSI PQFYQTDAIS RASKVMAKCI
     KARQSPVPGL HQAAMWRRAA VLLALVLALA ASSAAARPGP TLDEAGDGLL TDARGGATAG
     DDTAADSTVQ PSGSGDTTSD DDAWWTTSRG TQASSAAAAT GGAAAQADSE GSLFLQQQLN
     ALDAAAESQP AGGSDAAAGQ AQLNQGGAQQ AQQASLGGLA SGSADVDTSG YAQPSGTGTR
     AASTVQPLQA ASAQQQHTNT QQQQLDAEGE GDADAAQDDY DTGSTASGSD AEEGEQEEAE
     EGEEEGGSQA ATKAGSVYEN DYLDGDDDSG AGSGSSDGGS DESGSNSGSG DGEEEQHSVL
     AAAGGGSSLG AAVEQRQLIQ DWDGGASRGS AGSDSELGTE VGELHDGSEG QEAEGDGEDE
     DEDMEYSRSS SKGSGSGSMR QEGVGDDKWD ANEDSEPSER VSVQGGAATF DSAAGDDRFT
     HGLPGN
//
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