ID E5CWI4_9NEOP Unreviewed; 390 AA.
AC E5CWI4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=Ef-1a {ECO:0000313|EMBL:ACY78133.1};
OS Chilades putli.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Lycaenidae; Polyommatinae; Chilades.
OX NCBI_TaxID=689491 {ECO:0000313|EMBL:ACY78133.1};
RN [1] {ECO:0000313|EMBL:ACY78133.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21270033; DOI=10.1098/rspb.2010.2213;
RA Vila R., Bell C.D., Macniven R., Goldman-Huertas B., Ree R.H.,
RA Marshall C.R., Balint Z., Johnson K., Benyamini D., Pierce N.E.;
RT "Phylogeny and palaeoecology of Polyommatus blue butterflies show Beringia
RT was a climate-regulated gateway to the New World.";
RL Proc. R. Soc. B 278:2737-2744(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; GQ128645; ACY78133.1; -; 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:ACY78133.1};
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:ACY78133.1}.
FT DOMAIN 1..205
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACY78133.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:ACY78133.1"
SQ SEQUENCE 390 AA; 42729 MW; 35C4A7C5E9EC299B CRC64;
TIEKFEKEAQ EMGKGSFKYA WVLDKLKAER ERGITIDIAL WKFETSKYYV TIIDAPGHRD
FIKNMITGTS QADCAVLIVA AGTGEFEAGI SKNGQTREHA LLAFTLGVKQ LIVGVNKMDS
TEPPYSESRF EEIKKEVSSY IKKIGYNPAA VAFVPISGWH GDNMLEVSTK MPWFKGWQVE
RKEGKAEXKX LIEALDAILP PARPTDXXLR LPLQDVYKIG GXGTVPVGRV ETGVLKPGTI
VVFAPASITT EVKSVEMHHE ALQEAVPGDN VGFXVKNVSV KELRRGYVAG DSKNNPPKGA
ADFTAQVIVL NHPGQISNGY TPVLDCHTAH IACKFAEIKE KVDRRSGKST EDNPKSIKSG
DAAIVNLVPS KPXCVESFQX FPPLGRFAVR
//
