ID A5YUR8_LORPI Unreviewed; 371 AA.
AC A5YUR8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Elongation factor 1 alpha {ECO:0000313|EMBL:ABQ82258.1};
DE Flags: Fragment;
OS Loricera pilicornis (Ground beetle) (Carabus pilicornis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Adephaga; Caraboidea; Carabidae;
OC Loricerinae; Loricerini; Loricera.
OX NCBI_TaxID=60819 {ECO:0000313|EMBL:ABQ82258.1};
RN [1] {ECO:0000313|EMBL:ABQ82258.1}
RP NUCLEOTIDE SEQUENCE.
RA McMahon D.P., Kathirithamby J.;
RT "EF-1alpha intron structure further corroborates the invalidity of Halteria
RT (Strepsiptera + Diptera).";
RL Submitted (MAY-2007) 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}.
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; EF588668; ABQ82258.1; -; Genomic_DNA.
DR AlphaFoldDB; A5YUR8; -.
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; 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; 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:SF170; ELONGATION FACTOR 1-ALPHA 2; 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:ABQ82258.1};
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:ABQ82258.1}.
FT DOMAIN 1..178
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ82258.1"
FT NON_TER 371
FT /evidence="ECO:0000313|EMBL:ABQ82258.1"
SQ SEQUENCE 371 AA; 40463 MW; E0E1B3C30C0066DF CRC64;
AERERGITID IALWKFETAK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE
AGISKNGQTR EHALLAFTLG VKQLIVGVNK MDSTEPPYSE PRFEEIKKEV SSYIKKIGYN
PAAVAFVPIS GWHGDNMLEP SDKMPWFKGW AIERKEGKAD GKCLIEALDA ILPPSRPTEK
PLRLPLQDVY KIGGIGTVPV GRVETGVLKP GMVVVFAPAG LTTEVKSVEM HHEALQEAVP
GDNVGFNVKN VSVKELRRGY VAGDSKSNPP RGAADFTAQV IVLNHPGQIS NGYTPVLDCH
TAHIACKFAE IKEKCDRRTD KTTEENPKAI KSGDAAIVIL VPSKPMCVEA FQEFPPLGRF
AVRDMRQTVA V
//
