ID Q006Q2_BOLEU Unreviewed; 413 AA.
AC Q006Q2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1alpha {ECO:0000313|EMBL:ABI98496.1};
OS Boloria eunomia (Bog fritillary butterfly) (Proclossiana eunomia).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Heliconiinae; Argynnini; Boloria.
OX NCBI_TaxID=405022 {ECO:0000313|EMBL:ABI98496.1};
RN [1] {ECO:0000313|EMBL:ABI98496.1}
RP NUCLEOTIDE SEQUENCE.
RA Simonsen T.J., Wahlberg N., Brower A.V.Z., de Jong R.;
RT "Morphology, molecules and Fritillaries: approaching a stable phylogeny for
RT Argynnini (Lepidoptera: Nymphalidae).";
RL Submitted (AUG-2006) 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, ECO:0000256|RuleBase:RU000325}.
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 ECO:0000256|RuleBase:RU000325}.
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DR EMBL; DQ922901; ABI98496.1; -; Genomic_DNA.
DR AlphaFoldDB; Q006Q2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ABI98496.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:ABI98496.1}.
FT DOMAIN 1..228
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI98496.1"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:ABI98496.1"
SQ SEQUENCE 413 AA; 45230 MW; 073AFF53AA16750D CRC64;
HVDSGKSTTT GHLIYKCGGI DKRTIEKFEK EAQEMGKGSF KYAWVLDKLK AERERGITID
IALWKFETSK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE AGISKNGQTR
EHALLAFTLG VKQLIVGVNK MDSTEPPYSE SRFEEIKKEV SSYIKKIGYN PAAVAFVPIS
GWHGDNMLEP STKMPWFKGW QVERKEGKAD GKCLIEALDA ILPPARPTDK PLRLPLQDVY
KIGGIGTVPV GRVETGVLKP GTIVVFAPAN ITTEVKSVEM HHEALQEAVP GDNVGFNVKN
VSVKELRRGY VAGDSKNNPP RGAADFTAQV IVLNHPGQIS NGYTPVLDCH TAHIACKFAE
IKEKVDRRTG KSTEDNPKSI KSGDAAIVIL QPSKPLCVES FQEFPPLGRF AVR
//