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Database: UniProt
Entry: A0A150GAY0_GONPE
LinkDB: A0A150GAY0_GONPE
Original site: A0A150GAY0_GONPE 
ID   A0A150GAY0_GONPE        Unreviewed;       717 AA.
AC   A0A150GAY0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXZ47011.1};
GN   ORFNames=GPECTOR_39g505 {ECO:0000313|EMBL:KXZ47011.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ47011.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
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:KXZ47011.1}.
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DR   EMBL; LSYV01000040; KXZ47011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GAY0; -.
DR   STRING; 33097.A0A150GAY0; -.
DR   OrthoDB; 19999at2759; -.
DR   Proteomes; UP000075714; 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; 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; PF09326; NADH_dhqG_C; 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; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 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:UP000075714};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          45..123
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          248..304
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   717 AA;  76819 MW;  995F3F98125AAD50 CRC64;
     MVLTGLSRRA AVSLGQLWPG AQELSRTLST GSAALNQGAP PPPSDQIEVF VNEQPVKIPK
     NSTVLQACDA AGIDIPRFCY HQRLSIAGNC RMCLVEVEKV PKPVASCAMP AGPGMKIKTE
     TPMVKKAREG VMEFLLGGEC DLQDQAMIFG SDRSRFVETK RAVEDKNLGP LVKTVMNRCI
     HCTRCVRFAS EVAGTAELGV TGRGRDSEIG TYVEKLMSSE LSGNVVDLCP VGALTSKPYA
     FTARSWELKG TESIDVSDAL GANIRVDSRG TEVMRILPRL NEAVNEEWLS DRGRYQYDGL
     KRQRLDKPMV KGPKGLQPAT WSEALLAAAS ALSSVPGSAI KAVAGRLADA ESMVALMDLM
     RRLGAGNLVH EGGFADMPSD VRSTYTANTT VAGIEQADVI LLVGTNPRWE SPVFNARIRK
     TFVDGAQVGL LGAPVDLTYK YEHVGSDPAA LAALAAGSHP FLERLKKAAR PAVIVGPGVL
     RRADREAVLK AVHDLCGKAG VVKEGWNGFN VIHDTASRVA ALDMGFAPSA AARAAKQPAK
     VVYLLGADDW EEAEVPAGAF VIYQGHHGDR GASRADVVLP GAAYTEKSGL YVNFEGRVQQ
     TRPAVPLLGD AREDWRIVRA LSEVLGKRLP YDDHAAVRAR LADIAPHFAN INAVQTPVWL
     NGEYIKGVEQ LAKAAPVQAG VPLASSIDNF YMTDAISRAS RTMAKCVQAR QQAQAKA
//
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