ID   EF1A1_HORVU             Reviewed;         447 AA.
AC   P34824;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8159799; DOI=10.1104/pp.104.2.807;
RA   Sutton F., Kenefick D.G.;
RT   "Nucleotide sequence of a cDNA encoding an elongation factor (EF-1 alpha)
RT   from barley primary leaf.";
RL   Plant Physiol. 104:807-807(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 155-161; 201-205 AND 335-341.
RC   STRAIN=cv. Bomi; TISSUE=Starchy endosperm;
RX   PubMed=11271488;
RX   DOI=10.1002/1522-2683(200011)21:17<3693::aid-elps3693>3.0.co;2-i;
RA   Kristoffersen H.E., Flengsrud R.;
RT   "Separation and characterization of basic barley seed proteins.";
RL   Electrophoresis 21:3693-3700(2000).
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; L11740; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P34824; -.
DR   SMR; P34824; -.
DR   ExpressionAtlas; P34824; 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; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..447
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090936"
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;  49178 MW;  B82A5C98A841ED7C CRC64;
     MGKEKIHISI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL
     DKLKAERERG ITIDIALWKF ETTKYSCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT
     GVFQAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKSRYDEI VKEVSSYLKK
     VGYNPDKVPF VPISGFEGDN MIERSSNLDW YKGPTLLEAL DQINEPKRPS DKPLHLPLQD
     VYKIGGIGTV PVGRVETGVI KPGMVVTFGP TGLTTEVKSV EVHHESLLEA LPGDNVGFNV
     KNVAVKDLKR GYVASNSKDD PAKEAANFTA QVIIMNHPGQ ISNGYAPVLD CHTSHIAVKF
     AEIQTKIDRR SGKELEAAPK FLKNGDAGFV KMIPTKPMVV ETFAQYPPLG RFAVRDMRQT
     VAVGVIKSVE KKEPTGAKVT KAAIKKK