ID Q5EPR0_MELLT Unreviewed; 355 AA.
AC Q5EPR0;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1alpha {ECO:0000313|EMBL:AAW80198.1};
OS Melitaea latonigena (Brush-footed butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Nymphalinae; Melitaea.
OX NCBI_TaxID=113339 {ECO:0000313|EMBL:AAW80198.1};
RN [1] {ECO:0000313|EMBL:AAW80198.1}
RP NUCLEOTIDE SEQUENCE.
RA Wahlberg N., Brower A.V.Z., Nylin S.;
RT "Phylogenetic relationships of tribes and genera in the subfamily
RT Nymphalinae (Lepidoptera: Nymphalidae) based on three gene sequences.";
RL Submitted (OCT-2004) 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; AY788778; AAW80198.1; -; Genomic_DNA.
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:AAW80198.1};
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:AAW80198.1}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAW80198.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:AAW80198.1"
SQ SEQUENCE 355 AA; 38576 MW; 00E5ECB332552DE9 CRC64;
RGITIDIALW KFDTSKYYVT IIDAPGHRDF IKHMITGTSQ ADCAVLIVAA GTGEFEAGIS
KNGQTREHAL LAFTLGVKQL IVGVNKMDST EPPYSESRFE EIKKEVSSYI KKIGYNPAAV
AFVPISGWHG DNMLEPSTKM PWFKGWQVER KEGKAEGKCL IEALDAILPP ARPTDKALRL
PLQDVYKIGG IGTVPVGRVE TGVLKPGTIV VFAPANITTE VKSVEMHHEA LQEAVPGDXV
GFNVKXVSVK ELRRGYVAGD SKNNPPKGAA DFTAQVIVLN HPGQISNGYT PVLDCHTAHI
ACKFAEIKEK VDRRTGKSTE ENPKSXKSGD AAIVNLVPSK PLCVESFQEF PPLGR
//
