(data stored in ACNUC7421 zone)

SWISSPROT: EFG1_PSEHT

ID   EFG1_PSEHT              Reviewed;         704 AA.
AC   Q3ILP5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 87.
DE   RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   OrderedLocusNames=PSHAa0226;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome
CC       changes from the pre-translocational (PRE) to the post-
CC       translocational (POST) state as the newly formed A-site-bound
CC       peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC       sites, respectively. Catalyzes the coordinated movement of the two
CC       tRNA molecules, the mRNA and conformational changes in the
CC       ribosome. {ECO:0000255|HAMAP-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}.
DR   EMBL; CR954246; CAI85329.1; -; Genomic_DNA.
DR   RefSeq; WP_011326943.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILP5; -.
DR   SMR; Q3ILP5; -.
DR   STRING; 326442.PSHAa0226; -.
DR   PRIDE; Q3ILP5; -.
DR   EnsemblBacteria; CAI85329; CAI85329; PSHAa0226.
DR   KEGG; pha:PSHAa0226; -.
DR   PATRIC; fig|326442.8.peg.217; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; ISRIYQM; -.
DR   OrthoDB; POG091H02CO; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_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; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 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; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 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;
DR   PRODOM; Q3ILP5.
DR   SWISS-2DPAGE; Q3ILP5.
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    704       Elongation factor G 1.
FT                                /FTId=PRO_0000225227.
FT   DOMAIN        8    290       tr-type G.
FT   NP_BIND      17     24       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND      88     92       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND     142    145       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
SQ   SEQUENCE   704 AA;  77485 MW;  0114DB8520747784 CRC64;
     MARTTPLERY RNIGICAHVD AGKTTTTERI LFYTGLSHKI GETHDGAATM DWMEQEQERG
     ITITSAATTC FWKGMDAQFD AHRINIIDTP GHVDFTIEVE RSLRVLDGAV VVLCASSGVQ
     PQTETVWRQA NKYEVPRMIF VNKMDRTGAD FFAVVDQVKS RLGATPVPIQ LPIGAEDGFK
     GVIDLIKMKA INWNEADQGM TFTYEAIPAE LQELADEWRS HLVESAAEAT EELMDKYLEG
     EELSEAEIKE ALRQRTLAND IVPMTCGSAF KNKGVQAVLD CVVEYMPAPT QVKQIQGILE
     DGTEEERPAD DKAPFAALAF KIATDPFVGT LTFFRVYSGT VKQGDAVYNP VKSKRERLGR
     IVQMHSNSRE EIKEVFAGDI AAAIGLKDVT TGETLCDPKS IITLERMEFP EPVISVAVEP
     RTIADQDKMG IALGKLAAED PSFRVQTDEE SGQIIISGMG ELHLDILVER MKREFSVECN
     VGKPQVAYRE AIRSTVKVEG KFIRQSGGRG QYGHVWLKLE PMDITDDEAP IYEFVNETVG
     GSIPKEYVPA VDKGIQEQMS QGVLAGYPLL GVKATLYDGS FHDVDSNEMA FKIAGSLAMK
     QGALQASPVL LEPVMKVEVL TPEANMGDVV GDLNRRRGMI EGMEDALGGL KQINAQVPLS
     EMFGYATDLR SATQGRASYS MEFLKYAEAS KHVAETIISA RAVI
//

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