ID Q590U9_9HYME Unreviewed; 375 AA.
AC Q590U9;
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 Callohesma calliopsella.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Colletidae; Euryglossinae; Callohesma.
OX NCBI_TaxID=288349 {ECO:0000313|EMBL:AAU15080.1};
RN [1] {ECO:0000313|EMBL:AAU15080.1}
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; AY585126; AAU15080.1; -; Genomic_DNA.
DR AlphaFoldDB; Q590U9; -.
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:AAU15080.1};
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:AAU15080.1}.
FT DOMAIN 1..194
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAU15080.1"
FT NON_TER 375
FT /evidence="ECO:0000313|EMBL:AAU15080.1"
SQ SEQUENCE 375 AA; 40870 MW; 71D33A5FABC21E6B CRC64;
MGKGSFKYAW VLDKLKAERE RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ
ADCAVLIVAA GTGEFEAGIS KNGQTREHAL LAFTLGVKQL IVGVNKMDST EPPYSEARFE
EIKKEVSSYI KKIGYNPAAV AFVPISGWHG DNMLEVSSKM AWFKGWTVER KEGKVEGKCL
IEALDAILPP TRPTDKALRL PLQDVYKIGG IGTVPVGRVE TGVLKPGMIV TFAPTALTTE
VKSVEMHHEA LQEAVPGDNV GFNVKNVSVK DLRRGYVAGD SKNNPPKGAA DFTAQVIVLN
HPGQISNGYT PVLDCHTAHI ACKFAEIKEK CDRRTGKTSE ENPKAIKSGD AAIVVLVPSK
PMCVEAFQEF PPLGR
//
