ID E0X138_9NEOP Unreviewed; 355 AA.
AC E0X138;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
OS Eois sp. 820.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Larentiinae; Eois.
OX NCBI_TaxID=873410 {ECO:0000313|EMBL:ADL67294.1};
RN [1] {ECO:0000313|EMBL:ADL67294.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ433398; ADL67294.1; -; Genomic_DNA.
DR AlphaFoldDB; E0X138; -.
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:ADL67294.1};
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:ADL67294.1}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADL67294.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:ADL67294.1"
SQ SEQUENCE 355 AA; 38508 MW; 891C38B01C05DE81 CRC64;
IDIALWKFET AKFYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ
TREHALLAFT LGVKQLIVGV NKMDSTEPPY SESRFEEIKK EVSSYIKKIG YNPATVAFVP
ISGWHGDNML EPSTKMPWFK GWAVERKEGK ADGKCLIEAL DAILPPARPT DKALRLPLQD
VYKIGGIGTV PVGRVETGVL KPGTVVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV
KNVSVKELRR GYVAGDSKSN PPKGASDFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF
AEIKEKVDRR TGKSTEDNPK SIKSGDAAIV NLVPSKPLCV ESFQEFPPLG RFAVR
//
