ID   EF1A_SPOFR              Reviewed;         413 AA.
AC   Q26487;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   Flags: Fragment;
OS   Spodoptera frugiperda (Fall armyworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7659020; DOI=10.1093/oxfordjournals.molbev.a040244;
RA   Cho S., Mitchell A., Regier J.C., Mitter C., Poole R.W., Friedlander T.P.,
RA   Zhao S.;
RT   "A highly conserved nuclear gene for low-level phylogenetics: elongation
RT   factor-1 alpha recovers morphology-based tree for heliothine moths.";
RL   Mol. Biol. Evol. 12:650-656(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 263-274.
RX   PubMed=12489131; DOI=10.1002/arch.10061;
RA   Stuart M.K., Chamberlain N.R.;
RT   "Monoclonal antibodies to elongation factor-1alpha inhibit in vitro
RT   translation in lysates of Sf21 cells.";
RL   Arch. Insect Biochem. Physiol. 52:17-34(2003).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; U20139; AAA93219.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q26487; -.
DR   SMR; Q26487; -.
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   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN           <1..>413
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090916"
FT   DOMAIN          <1..228
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         <1..7
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         287
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         360
FT                   /note="5-glutamyl glycerylphosphorylethanolamine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         413
SQ   SEQUENCE   413 AA;  45146 MW;  13C825B3D45FC018 CRC64;
     HVDSGKSTTT GHLIYKCGGI DKRTIEKFEK EAQEMGKGSF KYAWVLDKLK AERERGITID
     IALWKFETAK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE AGISKNGQTR
     EHALLAFTLG VKQLIVGVNK MDSTEPPYSE SRFEEIKKEV SSYIKKIGYN PAAVAFVPIS
     GWHGDNMLEA STKMPWFKGW NVERKEGKAE GKCLIEALDA ILPPARPTDK PLRLPLQDVY
     KIGGIGTVPV GRVETGILKP GTIVVFAPAN ITTEVKSVEM HHEALQEAVP GDNVGFNVKN
     VSVKELRRGY VAGDSKNNPP KGAADFTAQV IVLNHPGQIS NGYTPVLDCH TAHIACKFAE
     IKEKVDRRTG KSTEDNPKSI KSGDAAIVNL VPSKPLCVES FQEFPPLGRF AVR