ID F2XHR6_9NEOP Unreviewed; 395 AA.
AC F2XHR6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-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-1alpha {ECO:0000313|EMBL:AEA34845.1};
OS Tebenna gnaphaliella.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Sesioidea;
OC Choreutidae; Choreutinae; Tebenna.
OX NCBI_TaxID=691997 {ECO:0000313|EMBL:AEA34845.1};
RN [1] {ECO:0000313|EMBL:AEA34845.1}
RP NUCLEOTIDE SEQUENCE.
RA Rota J.;
RT "Data partitioning in Bayesian analysis: molecular phylogenetics of
RT metalmark moths (Lepidoptera: Choreutidae).";
RL Syst. Entomol. 36:317-329(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, 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; HQ541522; AEA34845.1; -; Genomic_DNA.
DR AlphaFoldDB; F2XHR6; -.
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; 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; 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:AEA34845.1};
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:AEA34845.1}.
FT DOMAIN 1..220
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEA34845.1"
FT NON_TER 395
FT /evidence="ECO:0000313|EMBL:AEA34845.1"
SQ SEQUENCE 395 AA; 43121 MW; 61E6C7DBA51B4E04 CRC64;
TTGHLIYKCG GIDKRTIEKF EKEAQEMGKG SFKYAWVLDK LKAERERGIT IDIALWKFET
AKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ TREHALLAFT
LGVKQLIVGV NKMDSTEPPY SESRFEEIKK EVSSYIKKIG YNPAAVAFVP ISGWHGDNML
EPSTKMPWFK GWAVERKEGK ADGKCLIEAL DAILPPARPT DKALRLPLQD VYKIGGIGTV
PVGRVETGVL KPGTIVVFAP ANLTTEVKSV EMHHEALQEA VPGDNVGFNV KNVSVKELRR
GYVAGDSKNN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF AEIKEKVDRR
TGKSTEDNPK SIKSGDAAIV ILVPSKPLCV ESFQE
//
