EF2_PYRHO
ID EF2_PYRHO Reviewed; 732 AA.
AC O59521;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=PH1899; ORFNames=PHBB002;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP MUTAGENESIS OF HIS-597, AND DIPHTHAMIDE AT HIS-597.
RX PubMed=20559380; DOI=10.1038/nature09138;
RA Zhang Y., Zhu X., Torelli A.T., Lee M., Dzikovski B., Koralewski R.M.,
RA Wang E., Freed J., Krebs C., Ealick S.E., Lin H.;
RT "Diphthamide biosynthesis requires an organic radical generated by an iron-
RT sulphur enzyme.";
RL Nature 465:891-896(2010).
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA31022.1; ALT_INIT; Genomic_DNA.
DR PIR; G71203; G71203.
DR RefSeq; WP_048053510.1; NC_000961.1.
DR PDB; 5H7J; X-ray; 2.30 A; A/B=1-732.
DR PDB; 5H7K; X-ray; 1.60 A; A=1-386.
DR PDB; 5H7L; X-ray; 3.10 A; A/B=1-732.
DR PDBsum; 5H7J; -.
DR PDBsum; 5H7K; -.
DR PDBsum; 5H7L; -.
DR AlphaFoldDB; O59521; -.
DR SMR; O59521; -.
DR STRING; 70601.3258339; -.
DR EnsemblBacteria; BAA31022; BAA31022; BAA31022.
DR GeneID; 1442743; -.
DR KEGG; pho:PH1899; -.
DR eggNOG; arCOG01559; Archaea.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000000752; 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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..732
FT /note="Elongation factor 2"
FT /id="PRO_0000091044"
FT DOMAIN 19..260
FT /note="tr-type G"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 597
FT /note="Diphthamide"
FT /evidence="ECO:0000269|PubMed:20559380"
FT MUTAGEN 597
FT /note="H->A: No histidine modification."
FT /evidence="ECO:0000269|PubMed:20559380"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5H7L"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 68..73
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 161..182
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:5H7K"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 306..319
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5H7K"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:5H7K"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:5H7L"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:5H7J"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 496..503
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 554..570
FT /evidence="ECO:0007829|PDB:5H7J"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 600..616
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 620..634
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 638..647
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 651..658
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 661..669
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 676..683
FT /evidence="ECO:0007829|PDB:5H7J"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:5H7J"
FT STRAND 689..699
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 702..715
FT /evidence="ECO:0007829|PDB:5H7J"
FT HELIX 725..728
FT /evidence="ECO:0007829|PDB:5H7J"
SQ SEQUENCE 732 AA; 82399 MW; 6914AFBAA6DEA09D CRC64;
MGRREEMIAK IKELMLQPER IRNIGIAAHI DHGKTTLSDN LLAGAGMISE ELAGKQLVLD
FDEQEQARGI TINAANVSMV HNYEGKDYLI NLIDTPGHVD FGGDVTRAMR AIDGVIIVVD
AVEGVMPQTE TVVRQALREY VKPVLFINKV DRLIRELKLT PQQMMERFSK IIMDVNRLIQ
RYAPEEYKKK WMVKVEDGSV AFGSAYYNWA LSVPFMKRTG VKFNEIIDLT LKGDNRTLRQ
KAPLHVVVLD MVVRHLPSPI EAQKYRIPHL WEGDISSDIG QAMLNCDPKG KMVMVVTKII
IDKHAGEVAT GRVWSGTVKS GQEVYLINTK RKARIQQVGI YMGPERINME AVPAGNIVAV
TGLRDAMAGE TVAEEQIEPF EALHYVSEPV VTVAIEAKNV KDLPRLIEAL RQLAKEDPTL
HVKIDEETGQ HLLSGMGELH LEVKLYKLKK DWGIDIEVSE PIVVYRESIT KSSPMVEGKS
PNRHNRFYIV VEPMPDEIYN AIKEGIIPEG RVKNPKEVAK KLAELGMDYE IARGIVDIYN
GNMFIDNTKG VQYLNEVMDL LIDGFHQAMD EGPLAREPVM KVIVRLLDAQ VHEDNVHRGP
AQIYPAIRTA IHCAMMKSNP VLYEPYQKVI INIPYEYMGA VSREITQRRG QLVDMKQEGE
VMTIIAEAPV AEMFGFAGSI RSATSGRALW STEHAGFKRV PNELAQQIIR QIRQRKGLDP
NPPTEKDVCP LF
