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Database: UniProt
Entry: D3UCH1_9NEOP
LinkDB: D3UCH1_9NEOP
Original site: D3UCH1_9NEOP 
ID   D3UCH1_9NEOP            Unreviewed;       366 AA.
AC   D3UCH1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE   Flags: Fragment;
GN   Name=EF1a {ECO:0000313|EMBL:CAX52979.1};
OS   Ecnomina legula.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Trichoptera; Annulipalpia; Psychomyioidea;
OC   Ecnomidae; Ecnomina.
OX   NCBI_TaxID=623202 {ECO:0000313|EMBL:CAX52979.1};
RN   [1] {ECO:0000313|EMBL:CAX52979.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Johanson K.A., Espeland M.;
RT   "Phylogeny of the Ecnomidae (Insecta: Trichoptera).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FN178904; CAX52979.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3UCH1; -.
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:CAX52979.1};
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:CAX52979.1}.
FT   DOMAIN          1..196
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAX52979.1"
FT   NON_TER         366
FT                   /evidence="ECO:0000313|EMBL:CAX52979.1"
SQ   SEQUENCE   366 AA;  39795 MW;  454D93D0F87B09E2 CRC64;
     QEMGKGSFKY AWVLDKLKAE RERGITIDIA LWKFETAKYY VTIIDAPGHR DFIKNMITGT
     SQADCAVLIV AAGTGEFEAG ISKNGQTREH ALLAFTLGVK QLVVGVNKMD STEPAYSEPR
     FEEIKKEVSS YIKKIGYNPA AVAFVPISGW HGDNMLEPSS KMPWFKGWNV ERKEGKAEGK
     CLIEALDAIL PPARPTDKAL RLPLQDVYKI GGIGTVPVGR VETGVLKPGT IVVFAPANIT
     TEVKSVEMHH EALQEAVPGD NVGFNVKNVS VKELRRGYVA GDSKNNPPKG AADFTAQVIV
     LNHPGQISNG YTPVLDCHTA HIACKFAEIQ QKVDRRTGKS TEDNPKAIKS GDAAIVNLVP
     SKPMCV
//
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