ID E9LZG2_9NEOP Unreviewed; 335 AA.
AC E9LZG2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE Flags: Fragment;
GN Name=EF-1a {ECO:0000313|EMBL:ADW53986.1};
OS Boloria improba.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Heliconiinae; Argynnini; Boloria; Clossiana.
OX NCBI_TaxID=977890 {ECO:0000313|EMBL:ADW53986.1};
RN [1] {ECO:0000313|EMBL:ADW53986.1}
RP NUCLEOTIDE SEQUENCE.
RA Simonsen T.J., Wahlberg N., Warren A.D., Sperling F.A.H.;
RT "The evolutionary history of Boloria (Lepidoptera: Nymphalidae): phylogeny,
RT zoogeography and larval foodplant relationships.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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; HQ161323; ADW53986.1; -; Genomic_DNA.
DR AlphaFoldDB; E9LZG2; -.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
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:ADW53986.1};
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:ADW53986.1}.
FT DOMAIN 1..150
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADW53986.1"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:ADW53986.1"
SQ SEQUENCE 335 AA; 36313 MW; BAAFC8AAF9867D91 CRC64;
PGHRDFIKNM ITGTSQADCA VLIVAAGTGE FEAGISKNGQ TREHALLAFT LGVKQLIVGV
NKMDSTEPPY SEPRFEEIKK EVSSYIKKIG YNPAAVAFVP ISGWHGDNML EPSTKMPWFK
GWQVERKEGK ADGKCLIEAL DAILPPARPT DKPLRLPLQD VYKIGGIGTV PVGRVETGVL
KPGTIVVFAP ANITTEVKSV EMHHEALQEA VPGDNVGFNV KNVSVKELRR GYVAGDSKNN
PPRGAADFTA QVIVLNHPGQ ISNGYTPVLD CHTAHIACKF AEIKEKVDRR TGKSTEDNPK
SIKSGDAAIV ILQPSKPLCV ESFQEFPPLG RFAVR
//
