ID Q25110_9NEOP Unreviewed; 413 AA.
AC Q25110;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Heliolonche pictipennis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliolonche.
OX NCBI_TaxID=38056 {ECO:0000313|EMBL:AAA93213.1};
RN [1] {ECO:0000313|EMBL:AAA93213.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7659020;
RA Cho S., Mitchell A., Regier J.C., Mitter C., Poole R.W., Friedlander T.P.,
RA Zhao S.;
RT "A highly conserved nuclear gene for low-level phylogenetics: elongation
RT factor-1 alpha recovers morphology-based tree for heliothine moths.";
RL Mol. Biol. Evol. 12:650-656(1995).
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; U20133; AAA93213.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25110; -.
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:AAA93213.1};
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:AAA93213.1}.
FT DOMAIN 1..228
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAA93213.1"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:AAA93213.1"
SQ SEQUENCE 413 AA; 45079 MW; 9E829E105CC4CE3B CRC64;
HVDSGKSTTT GHLIYKCGGI DKRTIEKFEK EAQEMGKGSF KYAWVLDKLK AERERGITID
IALWKFETAK YYVTIIDAPG HRDFIKNMIT GTSQADCAVL IVAAGTGEFE AGISKNGQTR
EHALLAFTLG VKQLIVGVNK MDSTEPPYSE SRFEEIKKEV SSYIKKIGYN PAAVAFVPIS
GWHGDNMLEA STKMPWFKGW NVERKEGKAE GKCLIEALDA ILPPARPTDK ALRLPLQDVY
KIGGIGTVPV GRVETGILKP GTIVVFAPAN ITTEVKSVEM HHEALQEAVP GDNVGFNVKN
VSVKELRRGY VAGDSKNNPP KGAADFTAQV IVLNHPGSIS NGYTPVLDCH TAHIACKFAE
IKEKVDRRTG KSTEDNPKSI KSGDAAIVNL VPSKPLCVES FQEFPPLGRF AVR
//
