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Database: UniProt/TrEMBL
Entry: E4QDG9_CALH1
LinkDB: E4QDG9_CALH1
Original site: E4QDG9_CALH1 
ID   E4QDG9_CALH1            Unreviewed;       400 AA.
AC   E4QDG9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   22-NOV-2017, entry version 49.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:ADQ07587.1};
GN   OrderedLocusNames=Calhy_1877 {ECO:0000313|EMBL:ADQ07587.1};
OS   Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 /
OS   108).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ07587.1, ECO:0000313|Proteomes:UP000006890};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=108;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ07587.1, ECO:0000313|Proteomes:UP000006890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18901 / VKM B-2411 / 108
RC   {ECO:0000313|Proteomes:UP000006890};
RX   PubMed=21216991; DOI=10.1128/JB.01515-10;
RA   Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA   Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J.,
RA   Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N.,
RA   Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT   "Complete genome sequences for the anaerobic, extremely thermophilic
RT   plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT   Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor
RT   kronotskyensis, Caldicellulosiruptor owensenis, and
RT   Caldicellulosiruptor lactoaceticus.";
RL   J. Bacteriol. 193:1483-1484(2011).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP002219; ADQ07587.1; -; Genomic_DNA.
DR   RefSeq; WP_013403741.1; NC_014652.1.
DR   ProteinModelPortal; E4QDG9; -.
DR   SMR; E4QDG9; -.
DR   STRING; 632292.Calhy_1877; -.
DR   EnsemblBacteria; ADQ07587; ADQ07587; Calhy_1877.
DR   GeneID; 31772165; -.
DR   KEGG; chd:Calhy_1877; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; AIRDMGM; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000006890; 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; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 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   Complete proteome {ECO:0000313|Proteomes:UP000006890};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ADQ07587.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    209       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   400 AA;  44008 MW;  2F1372E372AA7632 CRC64;
     MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITKVLALKG KAQFMAYDQI DKAPEERERG
     ITINTAHVEY ETDARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVNVPY IVVFLNKVDM VDDPELIELV EMEVRELLSK YGYPGDEVPI VKGSALKALE
     STSQDPNAPE YQCILELMDA VDKYIPTPQR DIDKPFLMPI EDVFSITGRG TVVTGRVERG
     TLKTGEEVEI VGFAPEPRKT VVTGIEMFRK VLDEAVAGDN VGCLLRGIQK NEVERGQVLA
     KPGTIKPHTK FKAQVYVLTK EEGGRHTPFF NGYRPQFYFR TTDVTGTITL PEGVEMCMPG
     DNVEMTVELI SPIAIESGLR FAIREGGRTV GAGSVTTIIE
//
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