The domain within your query sequence starts at position 231 and ends at position 315; the E-value for the Asn_synthase domain shown below is 3.9e-6.

KEKVGTSKVLVLLSGGVDSTVCTALLNRALNQDQVIAVHIDNGFMRKRESQSVEEALKKL
GIQVKVINAAHSFYNGTTTLPISDE

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