ID I6LGF2_9NEOP Unreviewed; 350 AA.
AC I6LGF2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
OS Erysichton lineata lineata (hairy line-blue).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Lycaenidae; Polyommatinae; Erysichton.
OX NCBI_TaxID=379822 {ECO:0000313|EMBL:ABE60710.1};
RN [1] {ECO:0000313|EMBL:ABE60710.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MFB-99-T898 {ECO:0000313|EMBL:ABE60710.1}, and RG359-1
RC {ECO:0000313|EMBL:ABE60711.1};
RA Eastwood R.G., Hughes J.M., Pierce N.E., Grund R.;
RT "Phylogeny of the section Theclinesthes.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ456650; ABE60710.1; -; Genomic_DNA.
DR EMBL; DQ456651; ABE60711.1; -; Genomic_DNA.
DR AlphaFoldDB; I6LGF2; -.
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:ABE60710.1};
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:ABE60710.1}.
FT DOMAIN 1..165
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABE60710.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:ABE60710.1"
SQ SEQUENCE 350 AA; 38025 MW; F9EA909BEBEAC9CF CRC64;
WKFETAKYYV TIIDAPGHRD FIKNMITGTS QADCAVLIVA AGTGEFEAGI SKNGQTREHA
LLAFTLGVKQ LIVGVNKMDS TEPPYSESRF EEIKKEVSSY IKKIGYNPAA VAFVPISGWH
GDNMLEASTK MPWFKGWQVE RKEGKAEGKC LIEALDAILP PARPTDKALR LPLQDVYKIG
GIGTVPVGRV ETGVLKPGTI VVFAPANLTT EVKSVEMHHE ALQEAVPGDN VGFNVKNVSV
KELRRGYVAG DSKNNPPKGA ADFTAQVIVL NHPGQISNGY TPVLDCHTAH IACKFAEIKE
KVDRRSGKST EDNPKSIKSG DAAIVNLVPS KPLCVESFQE FPPLGRFAVR
//
