The domain within your query sequence starts at position 115 and ends at position 273; the E-value for the EF_TS domain shown below is 9.6e-23.

AVLVEVNCETDFVSRNLKFQQLVQQVALGTMAHCQNLTDRLSTYSKGFLNSSELSELAAG
PDREGSLKDQLALAIGKLGENMILKRAAWVKVPSGFYVGSYVHGVTQSPSLQNLVLGKYG
ALVICETPEQIANLEEVGRRLGQHVVGMAPLSVGSLDDE

EF_TS

• PFAM accession number: PF00889
• Interpro abstract (IPR014039):

  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.

  Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta) [ (PUBMED:12762045) ].

  This entry represents the C-terminal dimerisation domain found primarily in EF-Tu (EF1A) proteins from bacteria, mitochondria and chloroplasts.

• GO process: translational elongation (GO:0006414)
• GO function: translation elongation factor activity (GO:0003746)

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