EF1A_SOYBN
ID EF1A_SOYBN Reviewed; 447 AA.
AC P25698;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEFS1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1715783; DOI=10.1007/bf00040630;
RA Aguilar F., Montandon P.E., Stutz E.;
RT "Two genes encoding the soybean translation elongation factor eEF-1 alpha
RT are transcribed in seedling leaves.";
RL Plant Mol. Biol. 17:351-360(1991).
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; X56856; CAA40182.1; -; Genomic_DNA.
DR PIR; S17434; S17434.
DR AlphaFoldDB; P25698; -.
DR SMR; P25698; -.
DR STRING; 3847.GLYMA17G23900.1; -.
DR ProMEX; P25698; -.
DR eggNOG; KOG0052; Eukaryota.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P25698; -.
DR Proteomes; UP000008827; Unplaced.
DR Genevisible; P25698; GM.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..447
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090945"
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; 49378 MW; D08354B5D566F268 CRC64;
MGKEKVHISI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
GGFEAGISKD GQTREHALLS FTLGVKQMIC CCNKMDATTP KYSKARYDEI VKEVSSYLKK
VGYNPDKIPF VPISGFEGDN MIERSTNLDW YKGPTLLDAL DQISEPKRPS DKPLRLPLQD
VYKIGGIGTV PVGRVETGVL KPGMVVTFAP TGLTTEVKSV EMHHESLTEA HPGDNVGFNV
KNVAVKDLKR GYVASNSKDD PAKEAANFTA QVIIINHPGQ IGNGYAPVLD CHTSHIAVKF
AELMTKIDRR SGKELEKEPK FLKNGDAGFV KMIPTKPMVV ETFSEYPPLG RFAVRDMRQT
VAVGVIKNVE KKDPTGAKVT KAAQKKK
