ID A8HHW5_9NEOP Unreviewed; 396 AA.
AC A8HHW5;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1alpha {ECO:0000313|EMBL:ABV83827.1};
OS Methona curvifascia.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Ithomiini; Mechanitina; Methona.
OX NCBI_TaxID=471070 {ECO:0000313|EMBL:ABV83827.1};
RN [1] {ECO:0000313|EMBL:ABV83827.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LS02-162 {ECO:0000313|EMBL:ABV83827.1};
RX PubMed=17785265; DOI=10.1098/rspb.2007.1035;
RA Elias M., Hill R.I., Willmott K.R., Dasmahapatra K.K., Brower A.V.,
RA Mallet J., Jiggins C.D.;
RT "Limited performance of DNA barcoding in a diverse community of tropical
RT butterflies.";
RL Proc. R. Soc. B 274:2881-2889(2007).
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; EU069211; ABV83827.1; -; Genomic_DNA.
DR AlphaFoldDB; A8HHW5; -.
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; 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; 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:ABV83827.1};
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:ABV83827.1}.
FT DOMAIN 1..219
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV83827.1"
FT NON_TER 396
FT /evidence="ECO:0000313|EMBL:ABV83827.1"
SQ SEQUENCE 396 AA; 43265 MW; 1B45BC47594FE8D6 CRC64;
TGHLIYKCGG IDKRTIEKFE KEAQEMGKGS FKYAWVLDKL KAERERGITI DIALWKFETA
KFYVTIIDAP GHRDFIKNMI TGTSQADCAV LIVAAGTGEF EAGISKNGQT REHALLAFTL
GVKQLIVGVN KMDSTEPPYS ESRFEEIKKE VSSYIKKIGY NPAAVAFVPI SGWHGDNMLE
VSTKMPWFKG WQVERKEGKA EGKCLIEALD AILPPARPTD KALRLPLQDV YKIGGIGTVP
VGRVETGVLK PGTIVVFAPA NITTEVKSVE MHHEALQEAV PGDNVGFNVK NVSVKELRRG
YVAGDSKNSP PKGAADFTAQ VIVLNHPGQI SNGYTPVLDC HTAHIACKFA EIKEKVDRRS
GKSTEDNPKS IKSGDAAIVN LVPSKPLCVE AFQEFP
//
