The domain within your query sequence starts at position 523 and ends at position 631; the E-value for the GTP_EFTU_D3 domain shown below is 2.2e-23.

CHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRF
VKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLV

GTP_EFTU_D3

GTP_EFTU_D3
PFAM accession number:PF03143
Interpro abstract (IPR004160):

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [(PUBMED:12762045), (PUBMED:15922593), (PUBMED:12932732)]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.

EF1A (also known as EF-1alpha or EF-Tu) is a G-protein. It forms a ternary complex of EF1A-GTP-aminoacyltRNA. The binding of aminoacyl-tRNA stimulates GTP hydrolysis by EF1A, causing a conformational change in EF1A that causes EF1A-GDP to detach from the ribosome, leaving the aminoacyl-tRNA attached at the A-site. Only the cognate aminoacyl-tRNA can induce the required conformational change in EF1A through its tight anticodon-codon binding [(PUBMED:15680978), (PUBMED:12102560)]. EF1A-GDP is returned to its active state, EF1A-GTP, through the action of another elongation factor, EF1B (also known as EF-Ts or EF-1beta/gamma/delta).

EF1A consists of three structural domains. This entry represents the C-terminal domain, which adopts a beta-barrel structure, and is involved in binding to both charged tRNA and to EF1B (or EF-Ts, IPR001816) [(PUBMED:9253415)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GTP_EFTU_D3