ID   A6YF18_9NEOP            Unreviewed;       408 AA.
AC   A6YF18;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-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=EF-1 alpha {ECO:0000313|EMBL:ABR92662.1};
OS   Parnassius cephalus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Parnassiinae; Parnassini; Parnassius; Tadumia.
OX   NCBI_TaxID=213927 {ECO:0000313|EMBL:ABR92662.1};
RN   [1] {ECO:0000313|EMBL:ABR92662.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Chichvarkhin A., Wahlberg N., Omoto K., Nylin S.;
RT   "Phylogeny of the genus Parnassius: evidence from five gene sequences.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; EF485070; ABR92662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6YF18; -.
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:ABR92662.1};
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:ABR92662.1}.
FT   DOMAIN          1..223
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABR92662.1"
FT   NON_TER         408
FT                   /evidence="ECO:0000313|EMBL:ABR92662.1"
SQ   SEQUENCE   408 AA;  44715 MW;  950565D897713C43 CRC64;
     QSTTTGHLIY KCGGINKRTI EKFEKEAQEM GKGSFKYAWV LDKLKAERER GITIDIALWK
     FETSKYYVTI IDAPGHRDFI KNMITGTSQA DCAVLIVAAG TGEFEAGISK NGQTREHALL
     AFTLGVKQLI VGVNKMDSTE PPYSEPRFEE IKKEVSSYIK KIGYNPAAVA FVPISGWHGD
     NMLEPSTKMP WFKGWQVERK EGKAEGKCLI EALDAILPPA RPTDKPLRLP LQDVYKIGGI
     GTVPVGRVET GVLKPGTIVV FAPANITTEV KSVEMHHEAL QEAVPGDNVG FNVKNVSVKE
     LRRGYVAGDS KNNPPKGAAD FTAQVIVLNH PGQISNGYTP VLDCHTAHIA CKFAEIKEKV
     DRRTGKSTEE NPKSIKSGDA AIVNLVPSKP LCVESFQEFP PLGRFAVR
//