ID   EF2_CRYPV               Reviewed;         832 AA.
AC   Q23716;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
OS   Cryptosporidium parvum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=5807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AuCP-1;
RX   PubMed=7630379; DOI=10.1016/0166-6851(95)00051-2;
RA   Jones D.E., Tu T.D., Mathur S., Sweeney R.W., Clark D.P.;
RT   "Molecular cloning and characterization of a Cryptosporidium parvum
RT   elongation factor-2 gene.";
RL   Mol. Biochem. Parasitol. 71:143-147(1995).
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; U21667; AAC46607.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q23716; -.
DR   SMR; Q23716; -.
DR   PRIDE; Q23716; -.
DR   VEuPathDB; CryptoDB:cgd8_2930; -.
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   Phosphoprotein; Protein biosynthesis.
FT   CHAIN           1..832
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091010"
FT   DOMAIN          17..336
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          580..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..155
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         689
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   832 AA;  92761 MW;  577D2DE23D77E3FA CRC64;
     MVNFTVEQIR EIMGKPHNIR NMSVIAHVDH GKSTLTDSLV CKAGIIASKA AGDARFTDTR
     ADEQERCITI KSTGISLFFE HDLEDGKGRQ PFLINLIDSP GHVDFSSEVT AALRVTDGAL
     VVVDAVDGVC IQTETVLRQA LNERIRPVLH VNKVDRALLE LQWEAEDIYQ NFTRVIENVN
     VIISTYSDEL MGDVQVFPEK GTVSFGSGLH GWAFTIEKFA RIYAKKFGVE KSKMMQRLWG
     DNFFNPETKK FTKTQEPGSK RAFCQFIMEP ICQLFSSIMN GDKAKYEKML VNLGVELKGD
     DKALVDKPLL KKVMQLWLSA GDTLLEMIVT HLPSPAAAQK YRVENLYEGP QDDETAKGIR
     NCDPDAPLCM FVSKMVPTSD KGRFYAFGRV FSGTVATGQK VRIQGPRYVP GGKEDLNIKN
     IQRTVLMMGR YVEQIPDVPA GNTVGLVGID QYLLKSGTIT TSETAHNIAS MKYSVSPVVR
     VAVRPKDNKE LPKLVEGLKK LSKSDPLVVC SKEETGEHII AGCGELHVEI CLQDLQQEYA
     QIEIVASDPI VSYRETVVNL SNQTCLSKSP NKHNRLYMTA EPLPDGLTDD IEEGKVSPRD
     DPKERSNLLH DKYGFDKNAA MKIWCFGPET TGPNIMVDVT TGIQYLTEIK DHCNSAFQWA
     TKEGILCEED MRGIRFNLLD VTLHADAIHR GAGQITPTCR RVMYAAALTA SPRLLEPMFL
     VEISAPQEVV GGIYATLNQR RGHVFHEEPK SGTPQVEIKA YLPVADSFKF TTVLRAATSG
     KAFPQCVFDH WELINGDPLE KGSKTEELVK AIRRRKNIKE EIPALDNYLD KL