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Database: UniProt
Entry: H9CVC1_9NEOP
LinkDB: H9CVC1_9NEOP
Original site: H9CVC1_9NEOP 
ID   H9CVC1_9NEOP            Unreviewed;       413 AA.
AC   H9CVC1;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE   Flags: Fragment;
GN   Name=EF-1alpha {ECO:0000313|EMBL:AFC61454.1};
OS   Taygetis leuctra.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Satyrinae; Satyrini; Euptychiina; Taygetis.
OX   NCBI_TaxID=1141073 {ECO:0000313|EMBL:AFC61454.1};
RN   [1] {ECO:0000313|EMBL:AFC61454.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Matos Maravi P.F., Pena C., Willmott K.R., Freitas A.V., Wahlberg N.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFC61454.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23000820; DOI=10.1016/j.ympev.2012.09.005;
RA   Matos-Maravi P.F., Pena C., Willmott K.R., Freitas A.V., Wahlberg N.;
RT   "Systematics and evolutionary history of butterflies in the "Taygetis
RT   clade" (Nymphalidae: Satyrinae: Euptychiina): Towards a better
RT   understanding of Neotropical biogeography.";
RL   Mol. Phylogenet. Evol. 66:54-68(2013).
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; JQ392785; AFC61454.1; -; Genomic_DNA.
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:AFC61454.1};
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:AFC61454.1}.
FT   DOMAIN          1..228
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFC61454.1"
FT   NON_TER         413
FT                   /evidence="ECO:0000313|EMBL:AFC61454.1"
SQ   SEQUENCE   413 AA;  45023 MW;  C2BD95B115FC4D6B CRC64;
     HVDSGKSTTT GXLIYKCGGI DKRTIEKFEK EAQEMGKGSF KYAWVLDKLK AERERGITID
     IALWKFETAK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE AGISKNGQTR
     EHALLAFTLG VKQLIVGVNK MDSTEPPYSE SRFEEIKKEV SSYIKKIGYN PAAVAFVPIS
     GWHGDNMLEA STKMPWFKGW QVERKEGKGE GKCLIEALDA ILPPARPTDK ALRLPLQDVY
     KIGGIGTVPV GRVETGILKP GTIVVFAPAN ITTEVKSVEM HHEALSEAVP GDNVGFNVKN
     VSVKELRRGY VAGDSKNNPP KGAADFTAQV IVLNHPGQIS NGYTPVLDCH TAHIACKFAE
     IKEKVDRRSG KSTEDNPKSI KSGDAAIVNL VPSKPLCVEA FQEFPPLGRF AVR
//
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