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Database: UniProt
Entry: E5CWQ0_9NEOP
LinkDB: E5CWQ0_9NEOP
Original site: E5CWQ0_9NEOP 
ID   E5CWQ0_9NEOP            Unreviewed;       355 AA.
AC   E5CWQ0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE   Flags: Fragment;
GN   Name=Ef-1a {ECO:0000313|EMBL:ACY78199.1};
OS   Jamides alecto.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Lycaenidae; Polyommatinae; Jamides.
OX   NCBI_TaxID=124405 {ECO:0000313|EMBL:ACY78199.1};
RN   [1] {ECO:0000313|EMBL:ACY78199.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21270033; DOI=10.1098/rspb.2010.2213;
RA   Vila R., Bell C.D., Macniven R., Goldman-Huertas B., Ree R.H.,
RA   Marshall C.R., Balint Z., Johnson K., Benyamini D., Pierce N.E.;
RT   "Phylogeny and palaeoecology of Polyommatus blue butterflies show Beringia
RT   was a climate-regulated gateway to the New World.";
RL   Proc. R. Soc. B 278:2737-2744(2011).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; GQ128711; ACY78199.1; -; Genomic_DNA.
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   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
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   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF236; ELONGATION FACTOR 1-ALPHA 1; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:ACY78199.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000313|EMBL:ACY78199.1}.
FT   DOMAIN          1..170
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACY78199.1"
FT   NON_TER         355
FT                   /evidence="ECO:0000313|EMBL:ACY78199.1"
SQ   SEQUENCE   355 AA;  38541 MW;  FE363A2C5675D52F CRC64;
     IDIALWKFET AKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ
     TREHALLAFT LGVKQLIVGV NKMDSTEPPY NEGRFEEIKK EVSSYIKKIG YNPAAVAFVP
     ISGWHGDNML EVSTKMPWFK GWQVERKEGK ADGKCLIEAL DAILPPARPT DKALRLPLQD
     VYKIGGIGTV PVGRVETGVL KPGTIVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV
     KNVSVKELRR GYVAGDSKNN PPKGASDFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF
     AEIKEKVDRR SGKSTEDNPK SIKSGDAAIV NLVPSKPLCV ESFQEFPPLG RXAVR
//
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