ID   EF2_BLAHO               Reviewed;         867 AA.
AC   Q17152;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
OS   Blastocystis hominis.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC   Blastocystis.
OX   NCBI_TaxID=12968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=HE87-1;
RA   Nakamura Y., Hashimoto T., Yoshikawa H., Kamaishi T., Nakamura F.,
RA   Okamoto K.I., Hasegawa M.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000250}.
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; D79219; BAA11469.1; -; mRNA.
DR   AlphaFoldDB; Q17152; -.
DR   SMR; Q17152; -.
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..867
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091007"
FT   DOMAIN          17..368
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         120..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..179
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         723
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   867 AA;  96349 MW;  EE4B8E57DEC61A0F CRC64;
     MVNFTIDQIR HMMNMTHNIR NLSVVAHVDH GKSTLTDALV SKAGIISKKA AGDARFTDTR
     ADEQERCITI KSTGISLYFE YDPETIDKQA AAPLNPTEEG DPTEEDIEIK QNSYLINLID
     SPGHVDFSSE VTASLRVTDG ALVVVDSVGG VCVQTETVLR QALAERIRPV LSCMCNKLDR
     VIAELQLDPE EAYHKLMKSV ESVNVIIATY PDEAVGDIQV YPNQGTVAFG SGLQQWGFTR
     KFARLYAKKF GIDETKMMER LWGDYFFDAE NKKWAKTDKK DERKAQGKKP LKRAFVQFVL
     DPVYGLYRAL NEGRTEKYMK MLDTLGVTLT SEEKDLRDKA LVKRVMSKWL PAADALLEMI
     VLHLPSPVDA QKYRAPLLYD GPEDDEACTA MKKCDPNGCL MMYVSKMVPT ADQSRFYAFG
     RVFSGIIRSG QKVRILGPKY SATNKSDLLI KSVQRTVIMM GRYVEQVADI PCGNTCGLVG
     VDQYILKQAT LTDCESAMTI KMMKFSVSPV VRVAVEPKNP GDLPRLVEGL KRLSKSDPMV
     VVITNTEAGE HIIAGAGELH LEICLKDLQD DFMKGTPIKI SPPVVEFRES VNQATTEPGL
     AKSPNKHNRL YVNVEPMPDG LAQEIEDQKV TPEQEFKERA RYMSTTYGMD VELMRKIWAF
     GPNGNGPNIF CEATHGVQYL NEIKESVVAG FGAACAAGPI VDEPCRNVLC KLMDVTLHAD
     SIHRGMGQIM PPARRVVLGT MLKAEPILVE PVFLCEIQVP RAVSGGIYGV LTRRRGHVFE
     EIDEVGTPMM NIKSYLPVAE SFGFTQDLRG ATAGQAFPQC VFSHWQAYNG GDPLTEGTKT
     NEMVKSIRNR KGLAPEVPTP ERYLDKL