ID   EF2_PICPA               Reviewed;         842 AA.
AC   Q874B9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=EFT1; Synonyms=PEF1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12880776; DOI=10.1016/s1046-5928(03)00129-3;
RA   Liu Y.Y., Woo J.H., Neville D.M. Jr.;
RT   "Targeted introduction of a diphtheria toxin resistant mutation into the
RT   chromosomal EF-2 locus of Pichia pastoris and expression of immunotoxin in
RT   the EF-2 mutants.";
RL   Protein Expr. Purif. 30:262-274(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY219033; AAO39212.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q874B9; -.
DR   SMR; Q874B9; -.
DR   PRIDE; Q874B9; -.
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_0000091020"
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;  93469 MW;  BED5CF616E47F1A6 CRC64;
     MVNFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
     KDEQERGITI KSTAISLYSE MGDDDVKEIK QKTEGNSFLI NLIDSPGHVD FSSEVTAALR
     VTDGALVVVD CVEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVT KEDLYQSFAR
     TVESVNVVIA TYTDKTIGDN QVYPEQGTVA FGSGLHGWAF TVRQFATRYS KKFGVDRIKM
     MERLWGDSYF NPKTKKWTNK DKDAAGKPLE RAFNMFVLDP IFRLFAAIMN FKKDEIPVLL
     EKLEINLKRE EKELEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA YRAETLYEGP
     SDDQFCIGIR ECDPKAELMV YISKMVPTSD KGRFYAFGRV FSGTVKSGQK VRIQGPNYVP
     GKKEDLFIKA VQRTVLMMGR TVEPIDDVPA GNILGIVGID QFLLKSGTLT TNEAAHNMKV
     MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YISESGEHIV AGTGELHLEI
     CLQDLQDDHA GVPLKISPPV VTYRETVTNE SSMTALSKSQ NKHNRIYLKA QPIDEELSLA
     IEEGKVHPRD DFKARARIMA DEYGWDVTDA RKIWCFGPDG TGANLVVDQS KAVQYLHEIK
     DSVVAGFQLA TKEGPILGEN MRSVRVNILD VTLHADAIHR GGGQVIPTMK RVTYAAFLLA
     EPAIQEPIFL VEIQCPENAI GGIYSVLNKK RGQVISEEQR PGTPLFTVKA YLPVNESFGF
     TGELRQATAG QAFPQMVFDH WANMNGNPLD PASKVGEIVL AARKRQGMKE NVPGYEEYYD
     KL