ID Q2VKZ8_9NEOP Unreviewed; 357 AA. AC Q2VKZ8; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 09-DEC-2015, entry version 46. DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU004060}; DE Flags: Fragment; OS Velamysta pupilla. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Danainae; Ithomiini; Godyridina; OC Velamysta. OX NCBI_TaxID=304570 {ECO:0000313|EMBL:ABB90858.1}; RN [1] {ECO:0000313|EMBL:ABB90858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-43-3 {ECO:0000313|EMBL:ABB90858.1}; RX AGRICOLA=IND43764772; RX DOI=10.1603/0013-8746(2005)098[0873:PUOTAN]2.0.CO;2; RA Whinnett A., Brower A.V.Z., Lee M.-M., Willmott K.R., Mallet J.; RT "Phylogenetic utility of Tektin, a novel region for inferring RT systematic relationships among Lepidoptera."; RL Ann. Entomol. Soc. Am. 98:873-886(2005). RN [2] {ECO:0000313|EMBL:ABB90858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E-43-3 {ECO:0000313|EMBL:ABB90858.1}; 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. {ECO:0000256|RuleBase:RU000325}. 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|RuleBase:RU000325}. 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 GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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 Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Elongation factor {ECO:0000256|RuleBase:RU000325, KW ECO:0000313|EMBL:ABB90858.1}; KW GTP-binding {ECO:0000256|RuleBase:RU000323}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000323}; KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325, KW ECO:0000313|EMBL:ABB90858.1}. FT DOMAIN 1 171 Tr-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51722}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABB90858.1}. FT NON_TER 357 357 {ECO:0000313|EMBL:ABB90858.1}. 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 //