ID   Q2VKZ8_9NEOP            Unreviewed;       357 AA.
AC   Q2VKZ8;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE   Flags: Fragment;
OS   Velamysta pupilla.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Ithomiini; Godyridina; 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; 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 systematic
RT   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., 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}.
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}.
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DR   EMBL; DQ073021; ABB90858.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   InterPro; IPR004161; EFTu-like_2.
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   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; 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:0000313|EMBL:ABB90858.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..171
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABB90858.1"
FT   NON_TER         357
FT                   /evidence="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
//