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