ID   EF1A2_DAUCA             Reviewed;         447 AA.
AC   P34823;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Daucus carota (Wild 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=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1396695; DOI=10.1111/j.1432-1033.1992.tb17272.x;
RA   Fukuda H., Kawahara R., Sunabori S., Komamine A.;
RT   "A gene expressed preferentially in the globular stage of somatic
RT   embryogenesis encodes elongation-factor 1 alpha in carrot.";
RL   Eur. J. Biochem. 209:157-162(1992).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D12709; BAA02205.1; -; mRNA.
DR   PIR; S29312; JS0719.
DR   AlphaFoldDB; P34823; -.
DR   SMR; P34823; -.
DR   PRIDE; P34823; -.
DR   EnsemblPlants; KZM95891; KZM95891; DCAR_019133.
DR   Gramene; KZM95891; KZM95891; DCAR_019133.
DR   OMA; PKEANTF; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
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; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..447
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090934"
FT   DOMAIN          5..230
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          153..156
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          194..196
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..156
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         55
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         79
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         187
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         261
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         289
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         306
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
FT   MOD_RES         362
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         396
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTY0"
SQ   SEQUENCE   447 AA;  49312 MW;  0A31635198A08A08 CRC64;
     MGKEKIHISI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
     DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
     GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKSRFEEI VKEVSSYLKK
     VGYNPDKIAF IPISGFEGDN MIDRSTNLDW YKGPTLLEAL DQISEPKRPS DKPLRLPLQD
     VYKIGGIGTV PVGRVETGVI KPGMVVTFGP SGLTTEVKSV EMHHEALQEA LPGDNVGFNV
     KNVAVKDLKR GYVASNSKDD PAKEAANFTA QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF
     AEIQTKIDRR SGKELEKEPK FLKNGDAGFV KMIPTKPMVV ETFMSYPPLG RFAVRDMRQT
     VAVGVIKSVE KKDPTGAKVT KAAIKKK