ID J9PST0_9HYME Unreviewed; 363 AA.
AC J9PST0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Lasioglossum baudini.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Halictinae; Halictini; Lasioglossum;
OC Lasioglossum incertae sedis.
OX NCBI_TaxID=1039129 {ECO:0000313|EMBL:AEX27963.1};
RN [1] {ECO:0000313|EMBL:AEX27963.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22982437; DOI=10.1016/j.ympev.2012.08.013;
RA Gibbs J., Brady S.G., Kanda K., Danforth B.N.;
RT "Phylogeny of halictine bees supports a shared origin of eusociality for
RT Halictus and Lasioglossum (Apoidea: Anthophila: Halictidae).";
RL Mol. Phylogenet. Evol. 65:926-939(2012).
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; JQ266497; AEX27963.1; -; Genomic_DNA.
DR AlphaFoldDB; J9PST0; -.
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: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; 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:AEX27963.1};
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:AEX27963.1}.
FT DOMAIN 1..182
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEX27963.1"
FT NON_TER 363
FT /evidence="ECO:0000313|EMBL:AEX27963.1"
SQ SEQUENCE 363 AA; 39509 MW; C7E9E3ED63FC836C CRC64;
DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGT
GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSEARFEEI KKEVSSYIKK
IGYNPAAVAF VPISGWHGDN MLEVSSKMPW FKGWNVERKD GKAEGKCLIE ALDAILPPSR
PTDKALRLPL QDVYKIGGIG TVPVGRVETG LLKPGMVVTF APAGITTEVK SVEMHHEALT
EAVPGDNVGF NVKNVSVKEL RRGYVAGDSK NNPPKGAADF TAQVIVLNHP GQISNGYTPV
LDCHTAHIAC KFHKIIEKCD RRTGKTTEME PKAIKSGDAA IVTLVPTKPM CVEAFQEFPP
LGR
//
