ID F8TJD2_9NEOP Unreviewed; 355 AA.
AC F8TJD2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:AEI17381.1};
OS Phengaris arion (large blue).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Lycaenidae; Polyommatinae; Phengaris.
OX NCBI_TaxID=203779 {ECO:0000313|EMBL:AEI17381.1};
RN [1] {ECO:0000313|EMBL:AEI17381.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21669295; DOI=10.1016/j.ympev.2011.05.016;
RA Ugelvig L.V., Vila R., Pierce N.E., Nash D.R.;
RT "A phylogenetic revision of the Glaucopsyche section (Lepidoptera:
RT Lycaenidae), with special focus on the Phengaris-Maculinea clade.";
RL Mol. Phylogenet. Evol. 61:237-243(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}.
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; HQ918098; AEI17381.1; -; Genomic_DNA.
DR AlphaFoldDB; F8TJD2; -.
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:AEI17381.1};
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:AEI17381.1}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEI17381.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:AEI17381.1"
SQ SEQUENCE 355 AA; 38549 MW; A8C42FE79E61E747 CRC64;
IDIALWKFET AKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ
TREHALLAFT LGVKQLIVGV NKMDSTEPPY SESRFEEIKK EVSSYIKKIG YNPAAVAFVP
ISGWHGDNML EASTKMPWFK GWQVERKEGK AEGKCLIEAL DAILPPARPT DKALRLPLQD
VYKIGGIGTV PVGRVETGVL KPGTIVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV
KNVSVKELRR GYVAGDTKNN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF
AEIKEKVDRR SGKSTEVDPK SIKSGDAAIV NLVPSKPLCV ESFQEFPPLG RFAVR
//