ID F6JRG6_9HYME Unreviewed; 363 AA.
AC F6JRG6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:ADN31973.1};
DE Flags: Fragment;
OS Heteroperreyia hubrichi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Tenthredinoidea; Pergidae;
OC Perreyiinae; Heteroperreyia.
OX NCBI_TaxID=860944 {ECO:0000313|EMBL:ADN31973.1};
RN [1] {ECO:0000313|EMBL:ADN31973.1}
RP NUCLEOTIDE SEQUENCE.
RA Heraty J.M.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADN31973.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21540117; DOI=10.1016/j.ympev.2011.04.003;
RA Heraty J., Ronquist F., Carpenter J.M., Hawks D., Schulmeister S.,
RA Dowling A.P., Murray D., Munro J., Wheeler W.C., Schiff N., Sharkey M.;
RT "Evolution of the hymenopteran megaradiation.";
RL Mol. Phylogenet. Evol. 60:73-88(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; GQ410690; ADN31973.1; -; Genomic_DNA.
DR AlphaFoldDB; F6JRG6; -.
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; 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; 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:SF170; ELONGATION FACTOR 1-ALPHA 2; 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:ADN31973.1};
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:ADN31973.1}.
FT DOMAIN 1..178
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN31973.1"
FT NON_TER 363
FT /evidence="ECO:0000313|EMBL:ADN31973.1"
SQ SEQUENCE 363 AA; 39367 MW; 40E92C83B65F5BC3 CRC64;
AERERGITID ITLWKFETSK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE
AGISKNGQTR EHALLAFTLG VKQLIVGVNK MDSAEPPYSE ARFEEIKKEV TSYIKKIGYN
PAAVPFVPIS GWHGDNMLEP SSNMPWFKGW NVERKEGKAD GKCLIEALDA ILPPSRPTDK
ALRLPLQDIY KIGGIGTVPV GRVETGVLKP GMVVVFAPAG LTTEVKSVEM HHEALAEAVP
GDNVGFNVKN VSVKELRRGY VAGDSKANPP KGAADFTAQV IVLNHPGQIS NGYTPVLDCH
TAHIACKFAE IKEKCDRRTG KTTEENPKAI KSGDAAIVNL VPTKPMCVEA FQEFPPLGRF
AVD
//
