ID   EF1A_ENTHI              Reviewed;         430 AA.
AC   P31018;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2011152; DOI=10.1016/0166-6851(91)90217-t;
RA   de Meester F., Bracha R., Huber M., Keren Z., Rozenblatt S., Mirelman D.;
RT   "Cloning and characterization of an unusual elongation factor-1 alpha cDNA
RT   from Entamoeba histolytica.";
RL   Mol. Biochem. Parasitol. 44:23-32(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-143.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RA   Bhattacharya A.;
RL   Submitted (JAN-1995) 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; M92073; AAA29096.1; -; mRNA.
DR   EMBL; X83684; CAA58654.1; -; mRNA.
DR   AlphaFoldDB; P31018; -.
DR   SMR; P31018; -.
DR   STRING; 5759.rna_EHI_011210-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_195540; -.
DR   VEuPathDB; AmoebaDB:EHI7A_030290; -.
DR   VEuPathDB; AmoebaDB:EHI8A_035930; -.
DR   VEuPathDB; AmoebaDB:EHI_011210; -.
DR   VEuPathDB; AmoebaDB:KM1_038160; -.
DR   eggNOG; KOG0052; Eukaryota.
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   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..430
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090922"
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"
FT   CONFLICT        62
FT                   /note="N -> I (in Ref. 2; CAA58654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109..142
FT                   /note="ADVAILIVAAGTGEFEAGISKNGQTREHILLSYT -> LMLLFL (in
FT                   Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   430 AA;  47264 MW;  26F23FDDF3741108 CRC64;
     MPKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDQRTIE KFEKESAEMG KGSFKYAWVL
     DNLKAERERG ITIDISLWKF ETSKYYFTII DAPGHRDFIK NMITGTSQAD VAILIVAAGT
     GEFEAGISKN GQTREHILLS YTLGVKQMIV GVNKMDAIQY KQERYEEIKK EISAFLKKTG
     YNPDKIPFVP ISGFQGDNMI EPSTNMPWYK GPTLIGALDS VTPPERPVDK PLRLPLQDVY
     KISGIGTVPV GRVETGILKP GTIVQFAPSG VSSECKSIEM HHTALAQAIP GDNVGFNVRN
     LTVKDIKRGN VASDAKNQPA VGCEDFTAQV IVMNHPGQIR KGYTPVLDCH TSHIACKFEE
     LLSKIDRRTG KSMEGGEPEY IKNGDSALVK IVPTKPLCVE EFAKFPPLGR FAVRDMKQTV
     AVGVVKAVTP