ID S0AXA4_ENTHI Unreviewed; 442 AA.
AC S0AXA4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759 {ECO:0000313|EMBL:BAN38771.1};
RN [1] {ECO:0000313|EMBL:BAN38771.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HM-1:IMSS {ECO:0000313|EMBL:BAN38771.1};
RA Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J.,
RA Makioka A.;
RT "Short 5' UTR of Entamoeba genes.";
RL Submitted (JUN-2012) 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 {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; AK420147; BAN38771.1; -; mRNA.
DR AlphaFoldDB; S0AXA4; -.
DR VEuPathDB; AmoebaDB:EHI8A_141130; -.
DR VEuPathDB; AmoebaDB:KM1_115260; -.
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 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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:BAN38771.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:BAN38771.1}.
FT DOMAIN 5..228
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 442 AA; 48478 MW; D08AFCEBF0F309DF 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
KISGIGTVPC GRVETGVLRP GTIVQFAPSG VSSECKSVEM HHTALAQAIP GDNVGFNVRN
LTVKDIKRGN VASDVKNQPA VGCEDFTAQV IVMNHPGQIR KGYTPVFDCH TSPIACKFEE
FLSKIDRRTG KSMEGGEPEY IKNGDSALVK IVPTKPLCVE EFAKFPPLGR FAVRDMKQTV
AVGVVKAVTP RAANASAAGK KK
//
