EF2_DESA1
ID EF2_DESA1 Reviewed; 736 AA.
AC B8D6B2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=DKAM_1317;
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX PubMed=19114480; DOI=10.1128/jb.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
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; CP001140; ACL11643.1; -; Genomic_DNA.
DR RefSeq; WP_012608984.1; NC_011766.1.
DR AlphaFoldDB; B8D6B2; -.
DR SMR; B8D6B2; -.
DR STRING; 490899.DKAM_1317; -.
DR PRIDE; B8D6B2; -.
DR EnsemblBacteria; ACL11643; ACL11643; DKAM_1317.
DR GeneID; 7171371; -.
DR KEGG; dka:DKAM_1317; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000006903; 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; Reference proteome.
FT CHAIN 1..736
FT /note="Elongation factor 2"
FT /id="PRO_1000201497"
FT DOMAIN 18..261
FT /note="tr-type G"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT MOD_RES 602
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 736 AA; 82748 MW; 1C94C3C7123CF31C CRC64;
MVKFKQTSEV LKIMGNIEQI RNIGITAHVD HGKTTLSDTL LSAAGLISEK IAGQALALDY
LDVEQKRQMT VKAANASLYH EYKGKPYLIN LIDTPGHVDF QSKTIRALRV IDGAIVVVDA
VEGVMTQTEM YLRVALEERV RPVLFINKID RLIKELRLSP TEIQQRLVQI VRDVNTLIAT
YADKEFQKAW LLDPMKGQVA FGSARDRWGL TIPLVQQKGI KFSDIVDVYT RGKEAVAELQ
KTAPLHEAIL DMVVKHIPNP REAQRYRIPK IWHGDPNHEI VKYLMEADPN GPLVMLINDI
RVDPHAGLVA TGRIYSGTLR PGEEVWLVNA RVPQRVLQVS LYMGPYRELA DEITAGNIAA
ALGLEKARSG ETVVSMKYKD TMTPFEKLKM ITESVVTVAI EPKNPQQTTK LIDALYKLHL
EDPSLIVKIN EETGEYLLSG VGTLHIEIAL TLLKDLYGLE VVTSPPVIVY RETIRDRSQV
FEGKSPNKHN KFYISVTPLN EETLRLLSEG IIMEDMDARE RAKILREQAG WDADEARRIM
AIDENLNILI DMTTGVQYLR EVKDTIIQGF RLAMREGPLA MEPVRGVKVV LHDAVIHEDP
AHRGPAQIFP AVRNAIFAGF LTARPTILEP ILKLDIRSPM EYIGNISSVI TKKRGKLIEV
QQMETTARVI AEIPVSESFD IADMLRNVTA GKAIWGQEFS RWAPVPENML MDLIAKIRTR
KGLKPEPPKP EDFLSP
