The domain within your query sequence starts at position 304 and ends at position 565; the E-value for the Asn_synthase domain shown below is 5.6e-56.

EENLASKEVLKTCSSKANIAILFSGGVDSMVIAALADRHIPLDEPIDLLNVAFVPKQKTG
LPIPNIERKQQNHHEIPSEESSQSPAADEGPGEAEVPDRVTGKAGLKELQSVNPSRTWNF
VEINVSLEELQKLRRARICHLVQPLDTVLDDSIGCAVWFASRGIGWLVTQDAVRSYKSSA
KVILTGIGADEQLAGYSRHRARFQSLGLEGLNEEIAMELGRISSRNLGRDDRVIGDHGKE
ARFAQHVPVPFATSLTMHMLSD

Asn_synthase

Asn_synthase
PFAM accession number:PF00733
Interpro abstract (IPR001962):

Family members that contain this domain catalyse the conversion of aspartate to asparagine. Asparagine synthetase B ( EC 6.3.5.4 ) catalyses the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase [ (PUBMED:10587437) ].

Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine [ (PUBMED:11551215) ]. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia [ (PUBMED:10587437) ].

GO process:asparagine biosynthetic process (GO:0006529)
GO function:asparagine synthase (glutamine-hydrolyzing) activity (GO:0004066)

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