ID J9PSL0_9HYME Unreviewed; 365 AA.
AC J9PSL0;
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 altichum.
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=1039017 {ECO:0000313|EMBL:AEX27990.1};
RN [1] {ECO:0000313|EMBL:AEX27990.1}
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; JQ266524; AEX27990.1; -; Genomic_DNA.
DR AlphaFoldDB; J9PSL0; -.
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:AEX27990.1};
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:AEX27990.1}.
FT DOMAIN 1..184
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEX27990.1"
FT NON_TER 365
FT /evidence="ECO:0000313|EMBL:AEX27990.1"
SQ SEQUENCE 365 AA; 39652 MW; F495412FBD937927 CRC64;
VLDKLKAERE RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ ADCAVLIVAA
GTGEFEAGIS KNGQTREHAL LAFTLGVKQL IVGVNKMDST EPPYSEARFE EIKKEVSSYI
KKIGYNPAAV AFVPISGWHG DNMLEASSKM PWFKGWAVER KEGKADGKCL IEALDAILPP
SRPTDKALRL PLQDVYKIGG IGTVPVGRVE TGLLKPGMVV TFAPAGITTE VKSVEMHHEA
LTEAVPGDNV GFNVKNVSVK ELRRGYVAGD SKNNPPKGAA DFTAQVIVLN HPGQISNGYT
PVLDCHTAHI ACKFHKIIEK CDRRTGKTTE MEPKAIKSGD AAIVTLVPSK PMCVEAFQEF
PPLGR
//
