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EF2_PYRAE
ID   EF2_PYRAE               Reviewed;         740 AA.
AC   Q8ZZC1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=PAE0332;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
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|HAMAP-Rule:MF_00054}.
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DR   EMBL; AE009441; AAL62720.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZZC1; -.
DR   SMR; Q8ZZC1; -.
DR   STRING; 178306.PAE0332; -.
DR   EnsemblBacteria; AAL62720; AAL62720; PAE0332.
DR   KEGG; pai:PAE0332; -.
DR   PATRIC; fig|178306.9.peg.253; -.
DR   eggNOG; arCOG01559; Archaea.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   InParanoid; Q8ZZC1; -.
DR   OMA; GVMTQTE; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_A; EF_G_EF_2_A; 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; 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; IPR004543; Transl_elong_EFG/EF2_arc.
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; TIGR00490; aEF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..740
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091042"
FT   DOMAIN          23..264
FT                   /note="tr-type G"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         98..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         152..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         605
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   740 AA;  83150 MW;  262E97F71A39CEFF CRC64;
     MSSAVRIVEK QLDEILAIAK NPAQIRNAGT LAHVDHGKTT TSDSLLMGAG LLSPKVAGKA
     LAMDYVPIEQ LRQMTVKAAN ISLYFEYGGK PYLINFVDTP GHVDFTGHVT RSLRVMDGGL
     VVVDAVEGVM TQTETVVRQA LEEYVRPVLF INKIDRLIKE LRLSPQEIQQ RILTIVKDFN
     ALIDMFAPPE FKDKWKIDPG KGQMALGSAL HKWGITIPMA QKAGIKFSNI VDAYEKGYVD
     QLAQEFPLYK TILSMIIEHI PPPNVAQKYR IPRLWRGELN SEVGKALLEA DPNGPTVIAV
     SKVNKDPHAG LIATGRVFSG TIREGDEVYI IGRRLKKKVL QTYIYMGPSR IIVPYMPAGN
     IVALMGVDEA RAGDTLVDPK FSEIPPFEKM RYISEPVVTV AIEPKNPAEL ARLVEALKDL
     VVEDPTLDLK IDQETGQILL SGVGTLHLEI ATWLLKERTK TEFTVSPPLI RFRETVRERS
     QVWEGKSPNK HNRLYFYVEP LDETTIELIA SREITEDQEP RERAKILREK AGWDTDEARG
     IWAIDDRYFN VIVDKTSGIQ YLREIRDYIV QGFRWSMEAG PLAQEPMRGV KVVLVDAVVH
     EDPAHRGPAQ IMPATKNAIF AAVLSARPTL LEPLMRLDIK VAPDYIGAVT SVLNKHRGKI
     LDMTQQEYMA FLRAELPVLE SFNISDELRA AAAGKIFWSM QFARWAPFPE SMLGDFVKQL
     RKKKGLKEEI PKPTDFVEVY
 
 
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