ID   EF1A_APIME              Reviewed;         461 AA.
AC   P19039;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2116322; DOI=10.1016/0014-5793(90)80936-d;
RA   Walldorf U., Hovemann B.T.;
RT   "Apis mellifera cytoplasmic elongation factor 1 alpha (EF-1 alpha) is
RT   closely related to Drosophila melanogaster EF-1 alpha.";
RL   FEBS Lett. 267:245-249(1990).
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; X52884; CAA37066.1; -; Genomic_DNA.
DR   EMBL; X52885; CAA37066.1; JOINED; Genomic_DNA.
DR   PIR; S10738; EFHB1.
DR   RefSeq; NP_001011628.1; NM_001011628.2.
DR   RefSeq; XP_006566906.1; XM_006566843.2.
DR   RefSeq; XP_006566907.1; XM_006566844.2.
DR   RefSeq; XP_006566908.1; XM_006566845.2.
DR   AlphaFoldDB; P19039; -.
DR   SMR; P19039; -.
DR   STRING; 7460.GB52028-PA; -.
DR   PaxDb; P19039; -.
DR   PRIDE; P19039; -.
DR   EnsemblMetazoa; NM_001011628; NP_001011628; GeneID_408385.
DR   EnsemblMetazoa; XM_006566843; XP_006566906; GeneID_408385.
DR   EnsemblMetazoa; XM_006566844; XP_006566907; GeneID_408385.
DR   GeneID; 408385; -.
DR   KEGG; ame:408385; -.
DR   CTD; 408385; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   InParanoid; P19039; -.
DR   OMA; DIMVRKL; -.
DR   OrthoDB; 1150082at2759; -.
DR   PhylomeDB; P19039; -.
DR   Proteomes; UP000005203; Unplaced.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..461
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090904"
FT   DOMAIN          5..242
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         301
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         374
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  50521 MW;  038B34364D2826AA CRC64;
     MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGI
     GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDMTDP PYSEARFEEI KKEVSSYIKK
     IGYNTASVAF VPISGWHGDN MLEPSPKTPW YKGWKVERKD GNADGKTLIE ALDAILPPSR
     PTDKALRLPL QDVYKIGGIG TVPVGRVETG ILKPGMLVTF APAALTTEVK SVEMHHEALT
     EALPGDNVGF NVKNISVKEL RRGYVAGDSK NQPPRGAADF TAQVIVLNHP GQISNGYTPV
     LDCHTAHIAC KFAEIKEKCD RRTGKTTEEN PKSIKSGDAA IVMLQPTKPM CVEAFQEFPP
     LGRFAVRDMR QTVAVGVIKS VTFKDTQGKV TKAAEKAQKK K