ID E3TNT3_9NEOP Unreviewed; 366 AA.
AC E3TNT3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:ADO86578.1};
OS Agmina joycei.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Trichoptera; Annulipalpia; Psychomyioidea;
OC Ecnomidae; Agmina.
OX NCBI_TaxID=909967 {ECO:0000313|EMBL:ADO86578.1};
RN [1] {ECO:0000313|EMBL:ADO86578.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20722893; DOI=10.1111/j.1420-9101.2010.02072.x;
RA Espeland M., Johanson K.A.;
RT "The diversity and radiation of the largest monophyletic animal group on
RT New Caledonia (Trichoptera: Ecnomidae: Agmina).";
RL J. Evol. Biol. 23:2112-2122(2010).
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; GU967018; ADO86578.1; -; Genomic_DNA.
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; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF236; ELONGATION FACTOR 1-ALPHA 1; 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; 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:ADO86578.1};
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:ADO86578.1}.
FT DOMAIN 1..196
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADO86578.1"
FT NON_TER 366
FT /evidence="ECO:0000313|EMBL:ADO86578.1"
SQ SEQUENCE 366 AA; 39809 MW; D81329DB281108E0 CRC64;
QEMGKGSFKY AWVLDKLKAE RERGITIDIA LWKFETAKYY VTIIDAPGHR DFIKNMITGT
SQADCAVLIV AAGTGEFEAG ISKNGQTREH ALLAFTLGVK QLIVGVNKMD STEPPYSEPR
FEEIKKEVSS YIKKIGYNPA AVAFVPISGW XGDNMLEPSS KMPWFKGWNV ERKEGKAEGK
CLIEALDAIL PPARPTDKAL RLPLQDVYKI GGIGTVPVGR VETGVLKPGT IVVFAPANIT
TEVKSVEMHH EALQEAVPGD NVGFNVKNVS VKELRRGYVA GDSKNNPPKG AADFTAQVIV
LNHPGQISNG YTPVLDCHTA HIACKFAEIQ QKVDRRTGKS TEDNPKAIKS GDAAIVNLVP
SKPMCV
//
