The domain within your query sequence starts at position 179 and ends at position 344; the E-value for the GTP_EFTU domain shown below is 8.9e-34.



PFAM accession number:PF00009
Interpro abstract (IPR000795):

The translational GTPases are the Bacteria elongation factors, EFTu, EFG, and the initiation factor, IF2, and their archaeal homologues, the EF1, EF2, aeIF5b and aeIF2. They all contain two homologous N-terminal domains: a GTPase or G-domain, followed by an OB-domain. These translational proteins' G-domains are both structurally and functionally related to a larger family of GTPase G proteins [ (PUBMED:11916378) ].

In both prokaryotes and eukaryotes, there are three distinct types of elongation factors, EF-1alpha (EF-Tu), which binds GTP and an aminoacyl-tRNAand delivers the latter to the A site of ribosomes; EF-1beta (EF-Ts), which interacts with EF-1a/EF-Tu to displace GDP and thus allows the regeneration of GTP-EF-1a; and EF-2 (EF-G), which binds GTP and peptidyl-tRNA and translocates the latter from the A site to the P site. In EF-1-alpha, a specific region has been shown [ (PUBMED:3126836) ] to be involved in a conformational change mediated by the hydrolysis of GTP to GDP. This region is conserved in both EF-1alpha/EF-Tu as well as EF-2/EF-G and thus seems typical for GTP-dependent proteins which bind non-initiator tRNAs to the ribosome. The GTP-binding protein synthesis factor family also includes the eukaryotic peptide chain release factor GTP-binding subunits [ (PUBMED:7556078) ] and prokaryotic peptide chain release factor 3 (RF-3) [ (PUBMED:7737996) ]; the prokaryotic GTP-binding protein lepA and its homologue in yeast (GUF1) and Caenorhabditis elegans (ZK1236.1); yeast HBS1 [ (PUBMED:1394434) ]; rat statin S1 [ (PUBMED:1709933) ]; and the prokaryotic selenocysteine-specific elongation factor selB [ (PUBMED:2531290) ].

GO function:GTPase activity (GO:0003924), GTP binding (GO:0005525)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GTP_EFTU