ID A0A091G056_9AVES Unreviewed; 728 AA.
AC A0A091G056;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial {ECO:0000256|ARBA:ARBA00013888};
GN ORFNames=N303_08473 {ECO:0000313|EMBL:KFO75313.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO75313.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO75313.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO75313.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL447622; KFO75313.1; -; Genomic_DNA.
DR RefSeq; XP_009558055.1; XM_009559760.1.
DR AlphaFoldDB; A0A091G056; -.
DR STRING; 55661.A0A091G056; -.
DR KEGG; cuca:104058273; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:UP000053760};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 31..109
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 109..148
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 246..302
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 728 AA; 79683 MW; 4078EB9EF30C6860 CRC64;
MFRLPAVHRT LAGVAQSHRV CGRTTATAAN NQIEVFVDGH PVLVNPGTTV LQACEKAGIQ
IPRFCYHDRL SVAGNCRMCL VEIEKAPKPV AACAMPVMKG WNILTNSEKS RKAREGVMEF
LLANHPLDCP ICDQGGECDL QDQSMMFGSD RSRFREGKRA VEDKNIGPLV KTIMTRCIQC
TRCIRFASEI AGVDDLGTTG RGNDMQVGTY VEKMFMSELS GNIIDICPVG ALTSKPYAFT
ARPWETRKVE SIDVLDAVGS NIVVSTRTGE VMRILPRLHE DINEEWISDK TRFAYDGLKR
QRLTQPMIKN EKGLFAYASW EDVLTRVARV LQAANGKEVA AIVGGLVDAE ALIALKDLLN
RVNSDTLCTE EFFPTAGAGT DLRSNYLLNT KIAGVEEADV LLLVGTNPRF EAPLFNARIR
KSWLHNDLQV ALVGSPVNLT YTYDHLGDSP QILQDIASGK HAFCKVLDQA KKPMVVVGSA
ALQRSDGAAI HAAVSTISQS ARTKSGVGSD WKVMNILHRV ASQVAALDLG FKPGVEAIRK
NPPKVLYLLG ADSGCITRQD LPKDCFIIYQ GHHGDVGAPM ADVILPGAAY TEKAATYVNT
EGRAQQTRVA VTPPGMARED WKIIRAVSEL AGITLPYENL DQIRKRLEEV SPNLVRYDDV
EEANYFSQAN ELSKLVKQQL LTDPLVPPQL TIKDFYMTDS ISRASQTMAK CVKAVVEGAH
AVDEPASC
//
