ID Q30CI5_GREPL Unreviewed; 413 AA.
AC Q30CI5;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Greta polissena (Polissena clearwing butterfly) (Hypomenitis polissena).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Ithomiini; Godyridina; Hypomenitis.
OX NCBI_TaxID=1908658 {ECO:0000313|EMBL:ABA10510.1};
RN [1] {ECO:0000313|EMBL:ABA10510.1}
RP NUCLEOTIDE SEQUENCE.
RA Brower A.V.Z., Freitas A.V.L., Lee M.-M., Silva-Brandao K.L., Whinnett A.,
RA Willmott K.R.;
RT "Phylogenetic relationships among the Ithomiini (Lepidoptera: Nymphalidae)
RT inferred from one mitochondrial and two nuclear gene regions.";
RL Syst. Entomol. 31:288-301(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; DQ177944; ABA10510.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30CI5; -.
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:ABA10510.1};
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:ABA10510.1}.
FT DOMAIN 1..232
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABA10510.1"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:ABA10510.1"
SQ SEQUENCE 413 AA; 44952 MW; C949988ABF1A2E62 CRC64;
VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL DKLKAERERG
ITIDIALWKF ETAKFYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGT GEFEAGISKN
GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSEPRFEEI KKEVSSYIKK IGYNPAAVAF
VPISGWHGDN MLEASTKMPW FKGWQVERKE GKAEGKCLIE ALDAILPPAR PTDKALRLPL
QDVYKIGGIG TVPVGRVETG VLKPGTIVVF APANITTEVK SVEMHHEALQ EAVPGDNVGF
NVKNVSVKEL RRGYVAGDSK NSPPKGAADF TAQVIVLNHP GQISNGYTPV LDCHTAHIAC
KFAEIKEKVD RRSGKSTEDN PKSIKSGDAA IVNLVPSKPL CVEAFQEFPP LGR
//