EF1A_PLAFK
ID EF1A_PLAFK Reviewed; 443 AA.
AC Q00080;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=MEF-1;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ross-Macdonald P.B., Williamson D.H.;
RT "Isolation of a gene coding ef1-alpha from the human malaria parasite,
RT P.falciparum.";
RL Submitted (AUG-1991) 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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; X60488; CAA43018.1; -; Genomic_DNA.
DR PIR; S21909; S21909.
DR AlphaFoldDB; Q00080; -.
DR SMR; Q00080; -.
DR DrugBank; DB11638; Artenimol.
DR PRIDE; Q00080; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..443
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090928"
FT DOMAIN 5..228
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 192..194
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 443 AA; 49041 MW; B1CDF718968F7ADD CRC64;
MGKEKTHINL VVIGHVDSGK STTTGHIIYK LGGIDRRTIE KFEKESAEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPRYFFTVI DAPGHKDFIK NMITGTSQAD VALLVVPADV
GGFDGAFSKE GQTKEHVLLA FTLGVKQIVV GVNKMDTVKY SEDRYEEIKK EVKDYLKKVG
YQADKVDFIP ISGFEGDNLI EKSDKTPWYK GRTLIEALDT MQPPKRPYDK PLRIPLQGVY
KIGGIGTVPV GRVETGILKA GMVLNFAPSA VVSECKSVEM HKEVLEEARP GDNIGFNVKN
VSVKEIKRGY VASDTKNEPA KGCSKFTAQV IILNHPGEIK NGYTPLLDCH TSHISCKFLN
IDSKIDKRSG KVVEENPKAI KSGDSALVSL EPKKPMVVET FTEYPPLGRF AIRDMRQTIA
VGIINQLKRK NLGAVTAKAP AKK
