ID E9LZF4_9NEOP Unreviewed; 405 AA.
AC E9LZF4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:ADW53978.1};
OS Boloria alberta.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Heliconiinae; Argynnini; Boloria; Clossiana.
OX NCBI_TaxID=977885 {ECO:0000313|EMBL:ADW53978.1};
RN [1] {ECO:0000313|EMBL:ADW53978.1}
RP NUCLEOTIDE SEQUENCE.
RA Simonsen T.J., Wahlberg N., Warren A.D., Sperling F.A.H.;
RT "The evolutionary history of Boloria (Lepidoptera: Nymphalidae): phylogeny,
RT zoogeography and larval foodplant relationships.";
RL Submitted (AUG-2010) 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, ECO:0000256|RuleBase:RU000325}.
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 ECO:0000256|RuleBase:RU000325}.
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DR EMBL; HQ161315; ADW53978.1; -; Genomic_DNA.
DR AlphaFoldDB; E9LZF4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ADW53978.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ADW53978.1}.
FT DOMAIN 1..220
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADW53978.1"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:ADW53978.1"
SQ SEQUENCE 405 AA; 44402 MW; E11098F33489E595 CRC64;
TTGHLIYKCG GIDKRTIEKF EKEAQEMGKG SFKYAWVLDK LKAERERGIT IDIALWKFET
SKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ TREHALLAFT
LGVKQLIVGV NKMDSTEPPY SESRFEEIKK EVSSYIKKIG YNPAAVAFVP ISGWHGDNML
EPSTKMPWFK GWQVERKEGK ADGKCLIEAL DAILPPARPT DKPLRLPLQD VYKIGGIGTV
PVGRVETGVL KPGTIVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV KNVSVKELRR
GYVAGDSKNN PPRGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF AEIKEKVDRR
TGKSTEDNPK SIKSGDAAIV ILQPSKPLCV EAFQEFPPLG RFAVR
//