ID Q590W3_9HYME Unreviewed; 375 AA.
AC Q590W3;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Holcopasites ruthae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Ammobatoidini; Holcopasites.
OX NCBI_TaxID=156329 {ECO:0000313|EMBL:AAU15066.1};
RN [1] {ECO:0000313|EMBL:AAU15066.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17015826; DOI=10.1073/pnas.0604033103;
RA Danforth B.N., Sipes S., Fang J., Brady S.G.;
RT "The history of early bee diversification based on five genes plus
RT morphology.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15118-15123(2006).
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; AY585112; AAU15066.1; -; Genomic_DNA.
DR AlphaFoldDB; Q590W3; -.
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:AAU15066.1};
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:AAU15066.1}.
FT DOMAIN 1..194
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAU15066.1"
FT NON_TER 375
FT /evidence="ECO:0000313|EMBL:AAU15066.1"
SQ SEQUENCE 375 AA; 40884 MW; F3BB5ABED1F667F6 CRC64;
MGKGSFKYAW VLDKLKAERE RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ
ADCAVLIVAA GTGEFEAGIS KNGQTREHAL LAFTLGVKQL IVGVNKMDST EPPYSEARFE
EIKKEVSSYI KKIGYNPAAV AFVPISGWNG DNMLEVSSKM PWFKGWTVER KEGKVEGKCL
IEALDAILPP TRPTDKALRL PLQDVYKIGG IGTVPVGRVE TGLLKPGMVV TFAPAGLTTE
VKSVEMHHEA LQEAVPGDNV GFNVKNVSVK ELRRGYVAGD SKNNPPKGAA DFTAQVIVLN
HPGQISNGYT PVLDCHTAHI ACKFAEIKEK CDRRNGKTTE ENPKAIKSGD AAIVVLVPTK
PMCVEAFQEF PPLGR
//
