(data stored in SCRATCH zone)

SWISSPROT: D6ZCI8_SEGRD

ID   D6ZCI8_SEGRD            Unreviewed;       702 AA.
AC   D6ZCI8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   10-APR-2019, entry version 54.
DE   RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN   OrderedLocusNames=Srot_0546 {ECO:0000313|EMBL:ADG97030.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97030.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97030.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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:0000256|HAMAP-Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00054}.
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DR   EMBL; CP001958; ADG97030.1; -; Genomic_DNA.
DR   RefSeq; WP_013137486.1; NC_014168.1.
DR   STRING; 640132.Srot_0546; -.
DR   EnsemblBacteria; ADG97030; ADG97030; Srot_0546.
DR   KEGG; srt:Srot_0546; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; ISRIYQM; -.
DR   OrthoDB; 88967at2; -.
DR   BioCyc; SROT640132:G1GLH-550-MONOMER; -.
DR   Proteomes; UP000002247; 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   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; IPR041095; EFG_II.
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_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_II; 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; 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; D6ZCI8.
DR   SWISS-2DPAGE; D6ZCI8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW   ECO:0000313|EMBL:ADG97030.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN       12    288       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      21     28       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
FT   NP_BIND      85     89       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
FT   NP_BIND     139    142       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
SQ   SEQUENCE   702 AA;  77235 MW;  ED131233B1639937 CRC64;
     MAGAQSVLTD LNRVRNFGIM AHIDAGKTTT TERILYYTGV NYKIGEVHEG AATMDWMEQE
     QERGITITSA ATTCYWNDHQ LNLIDTPGHV DFTVEVERNL RVLDGAVAVF DGKEGVEPQT
     EQVWRQADKY SVPRICFVNK MDKLGADFFY TIKTMVDRIG VKPLPIQLPI GAENDFEGVI
     DLVGNRALVW SADTKLGEKY DVVEIPAHLK EQAAEYRQQL LEAVAETDEV LLEKFFGGEE
     LTIEEIKGGL RKIVLTSERF LVLCGSAFKN KGVQPLLDAV IDFLPSPLDI PATLGHRPND
     EEAVVERHPD SNEPFAALAF KIAAHPFFGK LTYIRVYSGK IDGGSAVVNS TKGKKERIGK
     LFQMHANKEN PVESAQAGHI YAVMGLKDTT TGDTLSDVND QIVLESMTFP DPVISVAIEP
     KTKSDQEKMG IAINRLAEED PTFKVKLDHE TGQTVISGMG ELHLDILVDR MKREFKVEAN
     VGKPQVAYRE TIRRTVDKHE YTHKKQTGGR GQFARVIIKL EPSVAEDGSG YEFANAVTGG
     RIPTNFIPSV DAGVKDALQG GVLAGYPLTD VKVTLLDGAY HEVDSDELSF KTAGNQALRE
     AARKADPVIL EPIMKVEVIT PDDYVGDVIG DLNSRRGQIQ EMSQRGTSRV VSALVPLSEM
     FGYVGDLRSK TQGRANYSML FDSYAEVPGG VAKEIIAKAN GE
//

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