ID A7SAD2_NEMVE Unreviewed; 412 AA.
AC A7SAD2;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Complex I-49kD {ECO:0000256|ARBA:ARBA00030505};
DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit {ECO:0000256|ARBA:ARBA00031562};
GN ORFNames=NEMVEDRAFT_v1g110807 {ECO:0000313|EMBL:EDO39377.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO39377.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO39377.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}.
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DR EMBL; DS469608; EDO39377.1; -; Genomic_DNA.
DR RefSeq; XP_001631440.1; XM_001631390.1.
DR AlphaFoldDB; A7SAD2; -.
DR STRING; 45351.A7SAD2; -.
DR EnsemblMetazoa; EDO39377; EDO39377; NEMVEDRAFT_v1g110807.
DR GeneID; 5511017; -.
DR KEGG; nve:5511017; -.
DR eggNOG; KOG2870; Eukaryota.
DR HOGENOM; CLU_015134_1_1_1; -.
DR InParanoid; A7SAD2; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 191at2759; -.
DR PhylomeDB; A7SAD2; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 142..412
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 412 AA; 46834 MW; E6C4F01A43EE5DF1 CRC64;
MTGTVMYPDE NSAKWDIDEP IPEKGVTNMT INFGPQHPAA HGVLRLVLEL DGEVVVRADP
HIGLLHRGTE KLIEYKTYLQ ALPYFDRLDY VSMMTNEQAY SLAVEKLLNI DIPERAKWIR
VLFGEITRLL NHIMGVTTHA LDVGAMTPFF WMFEEREKLM EFYERVSGAR MHAAYVRPGG
VSQDMPLGLM DDIYQFIQTF PQRLDDVEEM LTNNRIWKQR TVDIGVVSVE DALNYGFSGV
MLRGSGIKWD LRKAQPYDRY DQVEFDVPIG KNGDCYDRYL CRMEEMRESL KIILQCLNKM
PPGEIKVDDA KISPPKRSEM KDSMESLIHH FKLYTEGYQV PPGGTYTAIE APKGEFGVYL
VADGTSKPYR CKIKAPGFAH LAGTDFITKG HMLADVVAVI GTLDVVFGEV DR
//
