ID Q2LB25_9NEOP Unreviewed; 408 AA.
AC Q2LB25;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1-alpha {ECO:0000313|EMBL:ABC68676.1};
OS Ethope noirei.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Zetherini; Ethope.
OX NCBI_TaxID=366066 {ECO:0000313|EMBL:ABC68676.1};
RN [1] {ECO:0000313|EMBL:ABC68676.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16563805; DOI=10.1016/j.ympev.2006.02.007;
RA Pena C., Wahlberg N., Weingartner E., Kodandaramaiah U., Nylin S.,
RA Freitas A.V., Brower A.V.;
RT "Higher level phylogeny of Satyrinae butterflies (Lepidoptera: Nymphalidae)
RT based on DNA sequence data.";
RL Mol. Phylogenet. Evol. 40:29-49(2006).
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; DQ338915; ABC68676.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LB25; -.
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:ABC68676.1};
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:ABC68676.1}.
FT DOMAIN 1..223
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC68676.1"
FT NON_TER 408
FT /evidence="ECO:0000313|EMBL:ABC68676.1"
SQ SEQUENCE 408 AA; 44619 MW; 4982F95B03DD2E6D CRC64;
KSTTTGHLIY KCGGIDKRTI EKFEKEAQEM GKGSFKYAWV LDKLKAERER GITIDIALWK
FETAKYYVTI IDAPGHRDFI KNMITGTSQA DCAVLIVAAG TGEFEAGISK NGQTREHALL
AFTLGVKQLI VGVNKMDSTE PPYSEPRFEE IKKEVSSYIK KIGYNPAAVA FVPISGWHGD
NMLEPSTKMP WFKGWQVERK EGKGEGKCLI EALDAILPPA RPTDKPLRLP LQDVYKIGGI
GTVPVGRVET GILKTGTIVV FAPANITTEV KSVEMHHEAL SEAVPGDNVG FNVKNVSVKE
LRRGYVAGDS KNNPPKGAAD FTAQVIVLNH PGQISNGYTP VLDCHTAHIA CKFAEIKEKV
DRRSGKSTED NPKSIKSGDA AIVNLVPSKP LCVEAFQEFP PLGRFAVR
//
