ID Q4U1N8_9NEOP Unreviewed; 351 AA.
AC Q4U1N8;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:AAY44118.1};
OS Echinargus isola.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Lycaenidae; Polyommatinae; Echinargus.
OX NCBI_TaxID=328884 {ECO:0000313|EMBL:AAY44118.1};
RN [1] {ECO:0000313|EMBL:AAY44118.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16048773; DOI=10.1098/rspb.2005.3124;
RA Wahlberg N., Braby M.F., Brower A.V.Z., de Jong R., Lee M.-M., Nylin S.,
RA Pierce N.E., Sperling F.A.H., Vila R., Warren A.D., Zakharov E.;
RT "Synergistic effects of combining morphological and molecular data in
RT resolving the phylogeny of butterflies and skippers.";
RL Proc. R. Soc. B 272:1577-1586(2005).
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}.
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}.
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DR EMBL; DQ018914; AAY44118.1; -; Genomic_DNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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: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; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:AAY44118.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000313|EMBL:AAY44118.1}.
FT DOMAIN 1..166
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY44118.1"
FT NON_TER 351
FT /evidence="ECO:0000313|EMBL:AAY44118.1"
SQ SEQUENCE 351 AA; 38125 MW; 686FFEAADB2B9895 CRC64;
LWKFETAKYY VTIIDAPGHR DFIKNMITGT SQADCAVLIV AAGTGEFEAG ISKNGQTREH
ALLAFTLGVK QLIVGVNKMD STEPPYSESR FEEIKKEVSS YIKKIGYNPA AVAFVPISGW
HGDNMLEAST KMPWFKGWQV ERKEGKAEGK CLIEALDAIL PPARPTDKAL RLPLQDVYKI
GGIGTVPVGR VETGVLKPGT IVVFAPASIT TEVKSVEMHH EALQEAVPGD NVGFNVKNVS
VKELRRGYVA GDSKNNPPKG AADFTAQVIV LNHPGQISNG YTPVLDCHTA HIACKFAEIK
EKVDRRSGKS TEDNPKSIKS GDAAIVNLVP SKPLCVESFQ EFPXLGRFAV R
//
