ID Q30CH0_9NEOP Unreviewed; 415 AA.
AC Q30CH0;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Mechanitis polymnia.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Ithomiini; Mechanitina; Mechanitis.
OX NCBI_TaxID=127245 {ECO:0000313|EMBL:ABA10525.1};
RN [1] {ECO:0000313|EMBL:ABA10525.1}
RP NUCLEOTIDE SEQUENCE.
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, 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; DQ177959; ABA10525.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30CH0; -.
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:ABA10525.1};
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:ABA10525.1}.
FT DOMAIN 1..234
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABA10525.1"
FT NON_TER 415
FT /evidence="ECO:0000313|EMBL:ABA10525.1"
SQ SEQUENCE 415 AA; 45242 MW; 443AC12892A874E6 CRC64;
YIVVIGHVDS GKSTTTGHLI YKCGGIDKRT IEKFEKEAQE MGKGSFKYAW VLDKLKAERE
RGITIDIALW KFETAKFYVT IIDAPGHRDF IKNMITGTSQ ADCAVLIVAA GTGEFEAGIS
KNGQTREHAL LAFTLGVKQL IVGVNKMDST EPPYSESRFE EIKKEVSSYI KKIGYNPAAV
AFVPISGWHG DNMLEQSTKM PWFKGWQVER KEGKAEGKCL IEALDAILPP ARPTDKALRL
PLQDVYKIGG IGTVPVGRVE TGVLKPGTIV VFAPANITTE VKSVEMHHEA LQEAVPGDNV
GFNVKNVSVK ELRRGYVAGD SKNSPPKGAA DNTAQVIVLN HPGQISNGYT PVLDCHTAHI
ACKFAEIKEK VDRRSGKSTE DNPKSIKSGD AAIVNLVPSK PLCVEAFQEF PPLGR
//