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Database: UniProt/TrEMBL
Entry: E8N3M2_ANATU
LinkDB: E8N3M2_ANATU
Original site: E8N3M2_ANATU 
ID   E8N3M2_ANATU            Unreviewed;       400 AA.
AC   E8N3M2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   28-MAR-2018, entry version 50.
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=tufA {ECO:0000313|EMBL:BAJ63036.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=ANT_10020 {ECO:0000313|EMBL:BAJ63036.1}, ANT_19020
GN   {ECO:0000313|EMBL:BAJ63928.1};
OS   Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS   UNI-1).
OC   Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63036.1, ECO:0000313|Proteomes:UP000008922};
RN   [1] {ECO:0000313|EMBL:BAJ63036.1, ECO:0000313|Proteomes:UP000008922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC   {ECO:0000313|Proteomes:UP000008922}, and UNI-1
RC   {ECO:0000313|EMBL:BAJ63036.1};
RA   Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A.,
RA   Oguchi A., Fukui S., Takahashi M., Yashiro I., Hosoyama A.,
RA   Sekiguchi Y., Hanada S., Fujita N.;
RT   "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; AP012029; BAJ63036.1; -; Genomic_DNA.
DR   EMBL; AP012029; BAJ63928.1; -; Genomic_DNA.
DR   RefSeq; WP_013559427.1; NC_014960.1.
DR   STRING; 926569.ANT_19020; -.
DR   EnsemblBacteria; BAJ63036; BAJ63036; ANT_10020.
DR   EnsemblBacteria; BAJ63928; BAJ63928; ANT_19020.
DR   KEGG; atm:ANT_10020; -.
DR   KEGG; atm:ANT_19020; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; ATHE926569:G1GVU-1069-MONOMER; -.
DR   BioCyc; ATHE926569:G1GVU-2050-MONOMER; -.
DR   Proteomes; UP000008922; 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:UP000008922};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:BAJ63036.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008922}.
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;  44255 MW;  9560A944C68F7B23 CRC64;
     MAKQKFERTK PHLNVGTMGH IDHGKTTLTA AITKYCNLLG KAEFKAYDQI DNAPEEKARG
     ITINIAHVEY ETEKRHYAHV DMPGHRDYIK NMITGAAQVD GAILVVAAPD GPMPQTREHV
     LLARQVEVPS IVVFLNKVDM MDDPELLELV EMELREMLNG YGFPGDTTPI VRGSALKALE
     CPSKDPNAPE YACIKELLRV VDEYIPEPPR PVDQPFMMPV EDVFSIKGRG TVVTGRIERG
     RIKVGEPVEI VGLREKSMSS VVTGVEMFHK TLDEGIAGDN VGLLLRGVER TDVERGMVIA
     KPGSITPHTR FMSEVYVLKK EEGGRHKAFF NGYRPQFYIR TMDVTGTIKL PEGVEMVMPG
     DNVNLEVELI VPVALEQGSK FAIREGGLTV GAGVITKILE
//
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