ID Q4U1N3_9NEOP Unreviewed; 351 AA.
AC Q4U1N3;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:AAY44123.1};
OS Riodina lysippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Riodinidae; Riodininae; Riodinini; Riodina.
OX NCBI_TaxID=124365 {ECO:0000313|EMBL:AAY44123.1};
RN [1] {ECO:0000313|EMBL:AAY44123.1}
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; DQ018919; AAY44123.1; -; 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:AAY44123.1};
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:AAY44123.1}.
FT DOMAIN 1..166
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT UNSURE 5
FT /note="E or Q"
FT /evidence="ECO:0000313|EMBL:AAY44123.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY44123.1"
FT NON_TER 351
FT /evidence="ECO:0000313|EMBL:AAY44123.1"
SQ SEQUENCE 351 AA; 38116 MW; 3CF18A6DCF60FBB1 CRC64;
LWKFETAKYY VTIIDAPGXR DFIKNMITGT SQADCAVLXX AAGTGEFEAG ISKNGQTREH
ALLAFTLGVK QLIVGVNKMD STEPPYSEPR FEEIKKEVSS YIKKIGYNPA AVAFVPISGW
HGDNMLEPST KMPWFKGWQV ERKEGKAEGK CLIEALDAIL PPARPTDKPL RLPLQDVYKI
GGIGTVPVGR VETGVLKPGT IVVFAPANIT TEVKSVXMHH EALQEAVPGD NVGFNVKNVS
VKELRRGYVA GDSKNNPPKG AADFTAQVIV LNHPGQISNG YTPVLDCHTA HIACKFAEIK
EKVDRRSGKS TEENPKSIKS GDAAIVNLVP SKPLCVXSFQ EFPPXGXFAV R
//