ID Q6PTM0_LESCO Unreviewed; 411 AA.
AC Q6PTM0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Lestes congener (Spotted Spreadwing damselfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Palaeoptera; Odonata; Zygoptera; Lestidae; Lestes.
OX NCBI_TaxID=273679 {ECO:0000313|EMBL:AAT06182.1};
RN [1] {ECO:0000313|EMBL:AAT06182.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15084738; DOI=10.1073/pnas.0401670101;
RA Peterson K.J., Lyons J.B., Nowak K.S., Takacs C.M., Wargo M.J.,
RA McPeek M.A.;
RT "Estimating metazoan divergence times with a molecular clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6536-6541(2004).
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; AY580225; AAT06182.1; -; mRNA.
DR AlphaFoldDB; Q6PTM0; -.
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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAT06182.1};
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:AAT06182.1}.
FT DOMAIN 1..226
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAT06182.1"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:AAT06182.1"
SQ SEQUENCE 411 AA; 45092 MW; 32821059257D885C CRC64;
DSGKSTTTGH LIYKCGGIDK RTIEKFEKEA QEMGKGSFKY AWVLDKLKAE RERGITIDIA
LWKFETAKYY ITIIDAPGHR DFIKNMITGT SQADCAVLIV AAGTGEFEAG ISKNGQTREH
ALLAFTLGVK QLIVGVNKMD STEPPYSEAR FEEIKKEVGN YIKKIGYNPA AVAFVPISGW
HGDNMLESSD KMPWFKGWKV ERKDGNADGK CLIEALDAIL PPSRPTEKPL RLPLQDVYKI
GGIGTVPVGR VETGVMKPGM LVTFAPANIT TEVKSVEMHH EALQEAYPGD NVGFNVKNVS
VKELRRGYVC GDSKSNPPKA ASDFTAQVIV LNHPGQIANG YTPVLDCHTA HIACKFADIK
EKCDRRTGKT TEENPKSIKS GDAAIVNLVP SKPMCVESFQ EFPPLGRFAV R
//
