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Database: UniProt
Entry: A0A161ZNR2_DAUCS
LinkDB: A0A161ZNR2_DAUCS
Original site: A0A161ZNR2_DAUCS 
ID   A0A161ZNR2_DAUCS        Unreviewed;       476 AA.
AC   A0A161ZNR2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325};
GN   ORFNames=DCAR_026177 {ECO:0000313|EMBL:KZM89102.1};
OS   Daucus carota subsp. sativus (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM89102.1};
RN   [1] {ECO:0000313|EMBL:KZM89102.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZM89102.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA   Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC       ECO:0000256|RuleBase:RU000325}.
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:KZM89102.1}.
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DR   EMBL; LNRQ01000007; KZM89102.1; -; Genomic_DNA.
DR   RefSeq; XP_017219133.1; XM_017363644.1.
DR   AlphaFoldDB; A0A161ZNR2; -.
DR   STRING; 79200.A0A161ZNR2; -.
DR   EnsemblPlants; KZM89102; KZM89102; DCAR_026177.
DR   GeneID; 108196381; -.
DR   Gramene; KZM89102; KZM89102; DCAR_026177.
DR   KEGG; dcr:108196381; -.
DR   OrthoDB; 167272at2759; -.
DR   Proteomes; UP000077755; Chromosome 7.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF5; ELONGATION FACTOR TU, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325}; Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT   DOMAIN          77..281
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   476 AA;  51862 MW;  ACF054D7747834CF CRC64;
     MAISALSSSS INLINPANPN PNSAFSPTSS RKFILTSSFL ANPSTLSSQF QTPTSPFRSR
     ATRLTVRAAR GKFERKKPHI NIGTIGHVDH GKTTLTAALT MALAAMGGSA PKKYDEIDAA
     PEERARGITI NTATVEYETE SRHYAHVDCP GHADYVKNMI TGAAQMDGAI LVVSGADGPM
     PQTKEHILLA KQVGVPNMVV FLNKEDQVDD AELLELVELE VREELNKYEF PGDDIPIVSG
     SALLALEALM ENPAIKRGDN EWVDKIYALM DNVDSYIPIP QRQTELPFLM AIEDVFSITG
     RGTVATGRVE RGTIKVGETV DIVGLKDTRG TTVTGVEMFQ KFLDEALAGD NVGLLLRGIQ
     KIDIQRGMVL AKPGSITPHT KFEAIVYILK KDEGGRHSPF FTGYRPQFYM RTTDVTGKVT
     TIKNEKDEES KMVMPGDRVK MVVELIVPIA CEQGMRFAIR EGGKTVGAGV INAIIE
//
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