ID Q2VKZ8_9NEOP PRELIMINARY; PRT; 357 AA. AC Q2VKZ8; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 05-SEP-2006, entry version 8. DE Elongation factor 1-alpha (Fragment). OS Velamysta pupilla. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Danainae; Ithomiini; Dircennina; OC Velamysta. OX NCBI_TaxID=304570; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-43-3; RA Whinnett A., Brower A.V.Z., Lee M.-M., Willmott K.R., Mallet J.; RT "The Phylogenetic Utility of Tektin, a Novel Region for Inferring RT Systematic Relationships Amongst Lepidoptera."; RL Ann. Entomol. Soc. Am. 98:873-886(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-43-3; RA Brower A.V.Z., Freitas A.V.L., Lee M.-M., Silva-Brandao K.L., RA Whinnett A., Willmott K.R.; RT "Phylogenetic relationships among the Ithomiini (Lepidoptera: RT Nymphalidae) inferred from one mitochondrial and two nuclear gene RT regions."; RL Syst. Entomol. 31:288-301(2006). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis (By similarity). CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. CC EF-Tu/EF-1A subfamily. 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; DQ073021; ABB90858.1; -; Genomic_DNA. DR SMR; Q2VKZ8; 1-357. DR GO; GO:0005737; C:cytoplasm; IEA. DR GO; GO:0005525; F:GTP binding; IEA. DR GO; GO:0000166; F:nucleotide binding; IEA. DR GO; GO:0003746; F:translation elongation factor activity; IEA. DR GO; GO:0006412; P:protein biosynthesis; IEA. DR GO; GO:0006414; P:translational elongation; IEA. DR InterPro; IPR004539; EF1_alpha. DR InterPro; IPR004160; EFTU_C. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR000795; ProtSyn_GTP_bd. DR InterPro; IPR009000; Translat_factor. 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 TIGRFAMs; TIGR00483; EF-1_alpha; 1. KW Elongation factor; GTP-binding; Nucleotide-binding; KW Protein biosynthesis. FT NON_TER 1 1 FT NON_TER 357 357 SQ SEQUENCE 357 AA; 38744 MW; B6ECCACFD91BAE24 CRC64; TIDIALWKFE TAKFYVTIID APGHRDFIKN MITGTSQADC AVLIVAAGTG EFEAGISKNG QTREHALLAF TLGVKQLIVG VNKMDSTEPP YSEPRFEEIK KEVSSYIKKI GYNPAAVAFV PISGWHGDNM LEPSTKMPWF KGWQVERKEG KAEGKCLIEA LDAILPPARP TDKALRLPLQ DVYKIGGIGT VPVGRVETGV LKPGTIVVFA PANITTEVKS VEMHHEALQE AVPGDNVGFN VKNVSVKELR RGYVAGDSKN SPPKGAADFT AQVIVLNHPG QISNGYTPVL DCHTAHIACK FAEIKEKVDR RSGKSTEDNP KSIKSGDAAI VNLVPSKPLC VEAFQEFPPL GRFAVRD //