ID E5BB68_LUCSE Unreviewed; 343 AA.
AC E5BB68;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Elongation factor 1 alpha protein {ECO:0000313|EMBL:CBX87344.1};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:CBX87344.1};
OS Lucilia sericata (Green bottle fly) (Phaenicia sericata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=13632 {ECO:0000313|EMBL:CBX87344.1};
RN [1] {ECO:0000313|EMBL:CBX87344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lu23 {ECO:0000313|EMBL:CBX87344.1};
RA McDonagh L.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBX87344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lu23 {ECO:0000313|EMBL:CBX87344.1};
RX PubMed=21867590; DOI=10.1017/S0031182011001089;
RA McDonagh L.M., Stevens J.R.;
RT "The molecular systematics of blowflies and screwworm flies (Diptera:
RT Calliphoridae) using 28S rRNA, COX1 and EF-1a: insights into the evolution
RT of dipteran parasitism.";
RL Parasitology 138:1760-1777(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR719254; CBX87344.1; -; Genomic_DNA.
DR AlphaFoldDB; E5BB68; -.
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; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:CBX87344.1};
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:CBX87344.1}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBX87344.1"
FT NON_TER 343
FT /evidence="ECO:0000313|EMBL:CBX87344.1"
SQ SEQUENCE 343 AA; 37184 MW; C2E5842B86982236 CRC64;
MDIALWKFET SKYYVTIIDA PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ
TREHALLAFT LGVKQLIVGV NKMDSSEPPY SEARYEEIKK EVSSYIKKIG YNPAAVAFVP
ISGWHGDNML EASTNMPWFK GWKIERKEGN ADGKTLIDAL DAILPPTRPT EKPLRLPLQD
VYKIGGIGTV PVGRVETGVL KPGTVVVFAP ANITTEVKSV EMHHEALVEA VPGDNVGFNV
KNVSVKELRR GYVAGDSKAN PPKGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF
AEIKEKVDRR SGKTTEDQPK FIKSGDAAIV NLVPSKPLCV EAF
//
