ID E0X137_9NEOP Unreviewed; 355 AA.
AC E0X137;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
OS Eois muscosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Larentiinae; Eois.
OX NCBI_TaxID=873486 {ECO:0000313|EMBL:ADL67293.1};
RN [1] {ECO:0000313|EMBL:ADL67293.1}
RP NUCLEOTIDE SEQUENCE.
RA Strutzenberger P., Brehm G., Bodner F., Fiedler K.;
RT "Molecular phylogeny of Eois (Lepidoptera, Geometridae): evolution of wing
RT patterns and host plant use in a species-rich group of Neotropical moths.";
RL Zool. Scr. 39:603-620(2010).
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; GQ433397; ADL67293.1; -; Genomic_DNA.
DR AlphaFoldDB; E0X137; -.
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:ADL67293.1};
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:ADL67293.1}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADL67293.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:ADL67293.1"
SQ SEQUENCE 355 AA; 38482 MW; 4D8128CC122ABE54 CRC64;
IDIALWKFET AKFYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ
TREHALLAFT LGVKQLIVGV NKMDSTEPPY SESRFEEIKK EVSSYIKKIG YNPATVAFVP
ISGWHGDNML EVSTKMPWFK GWAVERKEGK SNGTCLIEAL DAILPPARPT DKALRLPLQD
VYKIGGIGTV PVGRVETGVL KPGTVVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV
KNVSVKELRR GYVAGDSKSN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF
AEIKEKVDRR TGKSTEDNPK SIKSGDAAIV NLVPSKPLCV ESFQEFPPLG RFAVR
//
