ID B3FUY4_9MUSC Unreviewed; 347 AA.
AC B3FUY4;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Elongation factor-1 alpha {ECO:0000313|EMBL:ACC37941.1};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:ACC37941.1};
OS Dicranosepsis emiliae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Sciomyzoidea;
OC Sepsidae; Dicranosepsis.
OX NCBI_TaxID=517509 {ECO:0000313|EMBL:ACC37941.1};
RN [1] {ECO:0000313|EMBL:ACC37941.1}
RP NUCLEOTIDE SEQUENCE.
RA Meier R., Su K.F.Y., Kutty S.;
RT "Morphology versus molecules: The phylogenetic relationships of Sepsidae
RT (Diptera: Cyclorrhapha) based on morphological and DNA sequence data from
RT ten genes.";
RL Submitted (JAN-2008) 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}.
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; EU435985; ACC37941.1; -; Genomic_DNA.
DR AlphaFoldDB; B3FUY4; -.
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:ACC37941.1};
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:ACC37941.1}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACC37941.1"
FT NON_TER 347
FT /evidence="ECO:0000313|EMBL:ACC37941.1"
SQ SEQUENCE 347 AA; 37655 MW; 57EC58E223336863 CRC64;
DIALWKFETS KYYVTIIDAP GHRDFIKNMI TGTSQADCAV LIVAAGTGEF EAGISKNGQT
REHALLAFTL GVKQLIVGVN KMDSSEPPYS EARYEEIKKE VSSYIKKIGY NPAAVAFVPI
SGWHGDNMLE PSTNMPWFKG WKVERKEGNA EGKTLIEALD AILPPTRPTD KALRLPLQDV
YKIGGIGTVP VGRVETGVLK PGCVVVFAPA NITTEVKSVE MHHEALTEAV PGDNVGFNVK
NVSVKELRRG YVAGDSKANP PKGAADFTAQ VIVLNHPGQI ANGYTPVLDC HTAHIACKFA
EIKEKVDRRS GKTTEENPKF IKSGDAAIVN LVPSKPLCVE SFQEFPP
//
