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EF2_IGNH4
ID   EF2_IGNH4               Reviewed;         740 AA.
AC   A8ACA7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Igni_1383;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82559.1; -; Genomic_DNA.
DR   RefSeq; WP_012123523.1; NC_009776.1.
DR   AlphaFoldDB; A8ACA7; -.
DR   SMR; A8ACA7; -.
DR   STRING; 453591.Igni_1383; -.
DR   EnsemblBacteria; ABU82559; ABU82559; Igni_1383.
DR   GeneID; 5562112; -.
DR   KEGG; iho:Igni_1383; -.
DR   eggNOG; arCOG01559; Archaea.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   OrthoDB; 1642at2157; -.
DR   PhylomeDB; A8ACA7; -.
DR   Proteomes; UP000000262; 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   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_1000008833"
FT   DOMAIN          18..263
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         606
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   740 AA;  82974 MW;  05A45D20903830EA CRC64;
     MPKYKHVEDI LKIMRNVEQV RNIGIIAHVD HGKTTTSDAL LAHAGILSPK LAGEARALDY
     LDVEQQRGIT VKAANVSLYH EYKGKPYVIN LIDTPGHVDF SGKVTRSLRV LDGAILVVDA
     VEGVMTQTET VLRQALEELV RPLLFINKVD RLIKELKLSP QEIQQRIVQI IKDVNERILT
     FAPDPEIAKK WLLDPAKGHV ALGSAKDKWG ITIPMAQEKG IKFSDIVEAY AKGSKDAIEE
     LFHKAPLHET LLDMVVRWVP NPREAQKYRV PRLWKGDINS ELGKAMLNCD PEGPLVVFIN
     DMRLDPHTKR LVATGRVWAG TATAGKEVWL VNAQKPGKIL QVSIYMGPDR EIVDYVTAGN
     IVAMLGLDDA RAGETLVDIN YKDQAAPFEQ LHYVSEPVVT VAIEPKNPRD LPKLIEALRT
     LSIEDPNLKV TINQETGEYL LSGMGMLHIE IALTQLKEVY GLEVKVSPPV ITYRETVRKP
     GEKVEGKSPN KHNKLYITVE PLEKEVIEMI QKGEITDDQD PRERAKVLRD KVNWDADTAR
     RIWAVDEENF NIFIDKTVGV QHLREVKDTI LAGWRLAMKE GPLAKEPVRG VKVILWDAVI
     HEDPAHRGPA QLYPAVRNAV YASMLTDSPT LLEPWQKLDI RVPNEYIGAV TGVITKHRGK
     ILEVIDMGGQ ARIVAAVPIA ESFELPMELR SVTAGRAFWG TEFYGWEPVP DQLLPELIRK
     IRERKGLPPE PPKAEDFLGP
 
 
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