EF2_ENTHI
ID EF2_ENTHI Reviewed; 840 AA.
AC Q06193;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EF-2;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SFL-3;
RX PubMed=8422275; DOI=10.1089/dna.1993.12.89;
RA Plaimauer B., Ortner S., Wiedermann G., Scheiner O., Duchene M.;
RT "Molecular characterization of the cDNA coding for translation elongation
RT factor-2 of pathogenic Entamoeba histolytica.";
RL DNA Cell Biol. 12:89-96(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-790.
RC STRAIN=HK-9;
RX PubMed=8074887; DOI=10.1266/jjg.69.119;
RA Shirakura T., Hashimoto T., Nakamura Y., Kamaishi T., Cao Y., Adachi J.,
RA Hasegawa M., Yamamoto A., Goto N.;
RT "Phylogenetic place of a mitochondria-lacking protozoan, Entamoeba
RT histolytica, inferred from amino acid sequences of elongation factor 2'.";
RL Jpn. J. Genet. 69:119-135(1994).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; L02417; AAA29097.1; -; mRNA.
DR EMBL; D21259; BAA04800.1; -; Genomic_DNA.
DR AlphaFoldDB; Q06193; -.
DR SMR; Q06193; -.
DR STRING; 5759.rna_EHI_189490-1; -.
DR PRIDE; Q06193; -.
DR VEuPathDB; AmoebaDB:EHI5A_197280; -.
DR VEuPathDB; AmoebaDB:EHI7A_139120; -.
DR VEuPathDB; AmoebaDB:EHI8A_150970; -.
DR VEuPathDB; AmoebaDB:EHI_189490; -.
DR VEuPathDB; AmoebaDB:KM1_077970; -.
DR eggNOG; KOG0469; 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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 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 Phosphoprotein; Protein biosynthesis.
FT CHAIN 1..840
FT /note="Elongation factor 2"
FT /id="PRO_0000091013"
FT DOMAIN 17..251
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 102..106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 697
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 471
FT /note="V -> DT (in Ref. 2; BAA04800)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="E -> D (in Ref. 2; BAA04800)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="P -> A (in Ref. 2; BAA04800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 840 AA; 93324 MW; 2E705327E3B52210 CRC64;
MSSTGVKTMK DFMLNKSNIR NMCVIAHVDH GKSTLTDSLV TLAGIISNEK AGVARYTDTR
PDEQERCITI KSTSISMYYE IEDKEDIPAD ANGNGFLINL IDSPGHVDFS SEVTAALRVT
DGALVVVDCV EGVCVQTETV LRQALTERVK PIVIINKVDR VILELKEEPE EAYQSFCRSI
ENVNVLISTY KDELLGDVQV SPGEGTVAFG SGLHGWAFTL EKFAKMWSAK FGIDRKRMLE
KLWGDNYWDA KAKKWKKNGK GDHGEVLQRG FVQFCFDPIT KLFNAIMEGR KADYEKMLTN
LQIKLSADDK EKEGKELLKT VMKLWLPAGV TLLEMIVLHL PSPVVAQKYR TSNLYTGPMD
DEAAKAMANC DEKGPLMMYV SKMIPTNDKG RFYAFGRVFS GTIRTGGKAR ICGPNYVPGK
KDDCVIKNIQ RTMLMMGRYT DPIDECPCGN VIGLVGVDQY LLKSGTITDS VAHIIKDMKF
SVSPVVRVAV ETKNPSDLPK LVEGMKRLSR SDPLCLCYTE ESGEHIVAGA GELHLEVCLK
ELQEDYCSGV PLIVTEPVVS FRETITEPSR IQCLSKSANN QNRLFMRAFP FPEGLAEDIE
AGEIKPDTDF KERAKFLSEK YGWDVDEARK IWCFGPDNCG PNLFVDVTKG IQYLNEVKDS
IVNGFNNAMH DGVVCNEQIR GVRINLEDVK LHADAIHRGG AQMIPCARRC CFACVLTGAP
SLLEPMYLAE IQCPESAIGG IYTVMSRRRG KIISEEQRPG TPLFNVRAYL PVCESFGFTA
DLRSHTSGQA FPQCVFDHWQ LLNGDVTDAT SKVGSIVAAI RKRKGLPEGV PGLDKFYDKL
