EF1A_SOLLC
ID EF1A_SOLLC Reviewed; 448 AA.
AC P17786;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. VFNT Cherry;
RX PubMed=2377481; DOI=10.1093/nar/18.14.4276;
RA Shewmaker C.K., Ridge N.P., Pokalsky A.R., Rose R.E., Hiatt W.R.;
RT "Nucleotide sequence of an EF-1 alpha genomic clone from tomato.";
RL Nucleic Acids Res. 18:4276-4276(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Caligrande;
RX PubMed=2748335; DOI=10.1093/nar/17.12.4661;
RA Pokalsky A.R., Haitt W.R., Ridge N., Rasmussen R., Houck C.M.,
RA Shewmaker C.K.;
RT "Structure and expression of elongation factor 1 alpha in tomato.";
RL Nucleic Acids Res. 17:4661-4673(1989).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53043; CAA37212.1; -; Genomic_DNA.
DR EMBL; X14449; CAA32618.1; -; mRNA.
DR PIR; S10507; S10507.
DR RefSeq; NP_001234035.1; NM_001247106.2.
DR RefSeq; XP_004240579.1; XM_004240531.3.
DR AlphaFoldDB; P17786; -.
DR SMR; P17786; -.
DR STRING; 4081.Solyc06g005060.2.1; -.
DR PaxDb; P17786; -.
DR PRIDE; P17786; -.
DR EnsemblPlants; Solyc06g005060.3.1; Solyc06g005060.3.1; Solyc06g005060.3.
DR EnsemblPlants; Solyc06g009970.3.1; Solyc06g009970.3.1; Solyc06g009970.3.
DR GeneID; 101244084; -.
DR GeneID; 544055; -.
DR Gramene; Solyc06g005060.3.1; Solyc06g005060.3.1; Solyc06g005060.3.
DR Gramene; Solyc06g009970.3.1; Solyc06g009970.3.1; Solyc06g009970.3.
DR KEGG; sly:101244084; -.
DR KEGG; sly:544055; -.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P17786; -.
DR OMA; SEKMAWF; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P17786; -.
DR Proteomes; UP000004994; Chromosome 6.
DR ExpressionAtlas; P17786; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..448
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090938"
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 448 AA; 49288 MW; C8E8BF6C1C0A7F56 CRC64;
MGKEKIHISI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKARYDEI VKEVSSYLKK
VGYNPDKIPF VPISGFEGDN MIERSTNLDW YKGPTLLEAL DQINEPKRPS DKPLRLPLQD
VYKIGGIGTV PVGRVETGVI KPGMVVTFGP TGLTTEVKSV EMHHEALQEA LPGDNVGFNV
KNVAVKDLKR GYVASNSKDD PAKGAASFTA QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF
AEILTKIDRR SGKELEKEPK FLKNGDAGMV KMIPTKPMVV ETFAEYPPLG RFAVRDMRQT
VAVGVVKNVD KKDPTGAKVT KAAQKKGK
