ID   EF2_PARKE               Reviewed;         845 AA.
AC   P28996;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
OS   Parachlorella kessleri (Green alga) (Chlorella kessleri).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Parachlorella.
OX   NCBI_TaxID=3074;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668412; DOI=10.1104/pp.97.1.469;
RA   Schnelboegl G., Tanner W.;
RT   "Amino acid sequence of an algal peptide elongation factor EF-2 deduced
RT   from the complementary DNA sequence.";
RL   Plant Physiol. 97:469-471(1991).
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; M68064; AAA33028.1; -; mRNA.
DR   PIR; S32819; S32819.
DR   AlphaFoldDB; P28996; -.
DR   SMR; P28996; -.
DR   PRIDE; P28996; -.
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..845
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091009"
FT   DOMAIN          17..346
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         104..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..161
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         702
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   845 AA;  94115 MW;  872E4F3925B1AB20 CRC64;
     MVKFTIDQIR GLMEYQNNIR NMSVIAHVDH GKSTLTDSLV AAAGIIAFEQ AGDQRLTDTR
     ADEQERGITI KSTGISLYYQ MTDEQLKGFT GERQGNDFLI NLIDSPGHVD FSSEVTAALR
     ITDGALVVVD CIEGVCVQTE TVLRQALGER IRPVLTINKI DRCFLELMLD PEEAYLAYRR
     VIENANVIMA TYADEHLGDT QTHPEAGTVS FSAGLHGWAF TLTVFANMYA AKFGTDTKRM
     MEKLWGDNFF DATTRKWTKK HTGADTCKRG FCQFIYEPIK TVIEAAMNDN KDKLFDLLKK
     LNVYSKLKPE DRELMGKPLM KRVMQTWLPA HEALLEMMIW HLPSPAKAQK YRVDVLYEGP
     LDDTYATAVR NCDADGPLMM YVSKMIPAAD KGRFYAFGRV FSGRIATGRK VRIMGPNYVP
     GQKKDLYVKT VQRTVLCMGR RQEAVEDVPC GNTVALVGLD QFITKNATLT DEKCEDAHTI
     KAMKFSVSPV VRVAVEPKVA SDLPKLVEGL KRLAKSDPMV QCTIEETGEH IIAGAGELHL
     EICLKDLQDD FMGGAEIRVS EPVVSFRETV IGTSDHVVMS KSPNKHNRLY MQARPMEDGL
     AEAIDEGKIG PRDDPKVRSK ILSEEFGWDK ELAKKILAFG PDTTGPNMVT DITKGVQYLN
     EIKDSVVAAF QWASKEGVLA EENMRGIVFE VCDVVLHADA IHRGGGQIIP TARRSMYAAQ
     LTAQPRLLEP VYLVEIQCPE QAMGGVYSVL NQKRGMVFEE LQRPGTPIFN LKAYLPVIES
     FGFTSTLRAA TAGQAFPQCV FDHWEAMGSD PTQVGSQANT LVMDIRKRKG LKPEPAALSE
     YEDKL