ID   C8C2M5_CYLPE            Unreviewed;       400 AA.
AC   C8C2M5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:ACV43830.1};
OS   Cyllopsis pertepida (Canyonland satyr butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Satyrinae; Satyrini; Euptychiina; Cyllopsis.
OX   NCBI_TaxID=366046 {ECO:0000313|EMBL:ACV43830.1};
RN   [1] {ECO:0000313|EMBL:ACV43830.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pena C., Nylin S., Wahlberg N.;
RT   "The radiation of Satyrini butterflies (Nymphalidae: Satyrinae): a
RT   challenge for phylogenetic methods.";
RL   Zool. J. Linn. Soc. 161:64-87(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GQ357274; ACV43830.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8C2M5; -.
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:ACV43830.1};
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:ACV43830.1}.
FT   DOMAIN          1..215
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACV43830.1"
FT   NON_TER         400
FT                   /evidence="ECO:0000313|EMBL:ACV43830.1"
SQ   SEQUENCE   400 AA;  43766 MW;  43B71B864C364A83 CRC64;
     IYKCGGIDKR TIEKFEKEAQ EMGKGSFKYA WVLDKLKAER ERGITIDIAL WKFETAKYYV
     TIIDAPGHRD FIKNMITGTS QADCAVLIVA AGTGEFEAGI SKNGQTREHA LLAFTLGVKQ
     LIVGVNKMDS TEPPYNESRF EEIKKEVSSY IKKIGYNPAA VAFVPISGWH GDNMLEASTK
     MPWFKGWQVE RKEGKAEGKC LIEALDAILP PARPTDKALR LPLQDVYKIG GIGTVPVGRV
     ETGIIKPGTI VVFAPANIVT EVKSVEMHHE ALSEAVPGDN VGFNVKNVSV KELRRGYVAG
     DSKNNPPKGA ADFTAQVIVL NHPGQISNGY TPVLDCHTAH IACKFAEIKE KVDRRSGKST
     EDNPKSIKSG DAAIVNLVPS KPLCVEAFQE FPPLGRFAVR
//