ID D3UCD7_9NEOP Unreviewed; 366 AA.
AC D3UCD7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:CAX52944.1};
OS Ecnomus sp. EJ4.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Trichoptera; Annulipalpia; Psychomyioidea;
OC Ecnomidae; Ecnomus.
OX NCBI_TaxID=623156 {ECO:0000313|EMBL:CAX52944.1};
RN [1] {ECO:0000313|EMBL:CAX52944.1}
RP NUCLEOTIDE SEQUENCE.
RA Johanson K.A., Espeland M.;
RT "Phylogeny of the Ecnomidae (Insecta: Trichoptera).";
RL Biol. J. Linn. Soc. Lond. 26:36-48(2010).
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; FN178869; CAX52944.1; -; Genomic_DNA.
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:CAX52944.1};
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:CAX52944.1}.
FT DOMAIN 1..196
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAX52944.1"
FT NON_TER 366
FT /evidence="ECO:0000313|EMBL:CAX52944.1"
SQ SEQUENCE 366 AA; 39764 MW; 9F1729B49925FB58 CRC64;
QEMGKGSFKY AWVLDKLKAE RERGITIDIA LWKFETAKYY VTIIDAPGHR DFIKNMITGT
SXADCAVLIV AAGTGEFEAG ISKNGQTREH ALLAFTLGVK QLIVGVNKMD STEPPYSEAR
FEEIKKEVSS YIKKIGYNPA AVAFVPISGW HGDNMLEPSS KMPWFKGWKV ERKEGNGDGK
CLIEALDAIL PPARPTDKAL RLPLQDVYKI GGIGTVPVGR VETGVLKPGT IVVFAPANIT
TEVKSVEMHH EALQEAVPGD NVGFNVKNVS VKELRRGYVA GDSKNNPPKG AADFTAQVIV
LNHPGQISNG YTPVLDCHTA HIACKFAEIQ QKVDRRTGKS TEDNPKAIKS GDAAIVNLVP
SKPMCV
//
