ID   EF2_LACK1               Reviewed;         842 AA.
AC   Q875S0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=EFT2;
OS   Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS   JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=226302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC   / NRRL Y-12651;
RX   PubMed=12594514; DOI=10.1038/nature01419;
RA   Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT   "Yeast genome duplication was followed by asynchronous differentiation of
RT   duplicated genes.";
RL   Nature 421:848-852(2003).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AY144999; AAO32562.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q875S0; -.
DR   SMR; Q875S0; -.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..842
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091022"
FT   DOMAIN          17..253
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         699
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   842 AA;  93362 MW;  3EC66C0511A19CDB CRC64;
     MVAFTVDQIR SLMDKVTNIR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
     KDEQERGITI KSTAISLFSE MSDDDVKDIK QKTEGNSFLI NLIDSPGHVD FSSEVTAALR
     VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVCVNKV DRALLELQVS KEDLYQSFAR
     TVESVNVIIS TYADEVLGDV QVYPSKGTIA FGSGLHGWAF TIRQFANRYS KKFGVDREKM
     MERLWGDSYF NPKTKKWTNK ETDTDGKPLE RAFNMFVLDP IFRLFSAIMN FKKDEIPVLL
     EKLEINLKGE EKELEGKALL KIVMRKFLPA ADALLEMIIM HLPSPVTAQN YRAEQLYEGP
     SDDPACIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYIP
     GKKDDLFIKA VQRAVLMMGR FVEPIDDCPA GNIVGLVGVD QFLLKTGTLT TFEGAHNMKV
     MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
     CLQDLENDHA GIPLKISPPV VAYRETVEGE SSQVALSKSP NKHNRIYLKA EPIDEEVSLA
     IEAGKINPRD DFKARARVMA DDFGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
     DSVVAAFQWA SKEGPIFGEQ MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA
     EPKIQEPVFL VEIQCPEQAV GGIYSVLNRK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
     TGELRQATGG QAFPQMVFDH WATLGTDPLD PTTKAGEIVT AARKRHGMKE EVPGWQEYYD
     KL