EF2_PYRIL
ID EF2_PYRIL Reviewed; 740 AA.
AC A1RVX2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Pisl_1957;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL89104.1; -; Genomic_DNA.
DR RefSeq; WP_011763679.1; NC_008701.1.
DR AlphaFoldDB; A1RVX2; -.
DR SMR; A1RVX2; -.
DR STRING; 384616.Pisl_1957; -.
DR EnsemblBacteria; ABL89104; ABL89104; Pisl_1957.
DR GeneID; 4616286; -.
DR KEGG; pis:Pisl_1957; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000002595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..740
FT /note="Elongation factor 2"
FT /id="PRO_0000335861"
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; 83051 MW; 542E1809533F0EEA CRC64;
MSSAVRIVEK QLDEILAIAR NPAQIRNAGT LAHVDHGKTT TTDSLLMGAG LLSPKVAGKA
LAMDYVPIEQ LRQMTVKAAN ISLYFEYGGK PYLINFVDTP GHVDFTGHVT RSLRVMDGGL
VVVDAVEGVM TQTETVVRQA LEEYVRPVLF INKIDRLIKE LRLSPQEIQQ RILTIVKDFN
ALIEMFAPPE FKDKWKIDPG KGQMAMGSAL HKWGITIPMA QKAGIKFSNI IDAYEKGYVD
QLAQEFPLYK TLLSMIIEHV PPPNVAQKYR IPRLWRGDLN SEVGKALLEA DPNGPTVIAV
SKVNKDPHAG LIVTGRVFSG TIREGDEIYI IGRKMKKKVL QTYIYMGPSR IIVPYMPAGN
IVALMGVDEA RAGDTLVDPR ISDIPPFEKM RYIAEPVVTV AIEPKNPAEL AKLVEALKDL
VIEDPTLDLK IDQETGQILL SGVGTLHLEI ATWLLKERSK TEFTVSPPLI RFRETVRERS
QVWEGKSPNK HNRLYFYVEP LDETTIELIA TKEITEDQDP RERAKILREK AGWDTDEARG
IWAIDDRYFN VIVDKTSGIQ YLREIRDYIV QGFRWATEAG PLAQEPIRGV KVVLVDAVVH
EDPAHRGPAQ IMPATKNAIF AAMLSAKPTV LEPLLRLDIK VAPDYIGAVT SVLNKHRGKI
LDMTQQEYMA YLRAELPVLE SFTISDELRA AAAGKIFWSM QFSRWAPVPE SMLLDLVKQL
RKKKGLKEEI PKPTDFVEVY
