ID C8C2Q5_9NEOP Unreviewed; 400 AA.
AC C8C2Q5;
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:ACV43860.1};
OS Pedaliodes phrasiclea.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Satyrini; Pronophilina; Pedaliodes.
OX NCBI_TaxID=669562 {ECO:0000313|EMBL:ACV43860.1};
RN [1] {ECO:0000313|EMBL:ACV43860.1}
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}.
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DR EMBL; GQ357304; ACV43860.1; -; Genomic_DNA.
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:ACV43860.1};
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:ACV43860.1}.
FT DOMAIN 1..215
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV43860.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:ACV43860.1"
SQ SEQUENCE 400 AA; 43598 MW; F8E24CB3417094A0 CRC64;
IXQCGGIDKR TIEKFEKEAQ EMGKGSFKYA WVLDKLKAER ERGITIDIAL WKFETAKFYV
TIIDAPGHRD FIKNMITGTS QADCAVLIVA AGTGEFEAGI SKNGQTREHA LLAFTLGVKQ
LIVGVNKMDS TEPPYSEPRF EEIKKEVSSY IKKIGYNPAA VAFVPISGWH GDNMLEASTK
MPWFKGWAVE RKEGKADGKC LIEALDAILP PARPTDKALR LPLQDVYKIG GIGTVPVGRV
ETGVLKPGTI VVFAPANITT EVKSVEMHHE ALSEAVPGDN VGFNVKNVSV KELRRGYVAG
DSKNNPPKGA ADFTAQVIVL NHPGQISNGY TPVLDCHTAH IACKFAEIKE KVDRRSGKST
EDNPKSIKSG DAAIVNLVPS KPLCVEAFQE FPPLGRFAVR
//