The domain within your query sequence starts at position 204 and ends at position 302; the E-value for the GSH_synthase domain shown below is 2.5e-36.

AVVLLIAQEKERNIFDQRAVENELLDRKIHVIRGRFEDVSERGSLDQNRRLFMDDQEVAV
VYFRDGYMPSQYNSQNWEARLMLERSRAAKCPDIAIQLA

GSH_synthase

GSH_synthase
PFAM accession number:PF03199
Interpro abstract (IPR004887):

This entry represents the substrate-binding domain of glutathione synthetase (EC 6.3.2.3) (GSS), a homodimeric enzyme that catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to phosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis, the first step being catalysed by gamma-glutamylcysteine synthetase [(PUBMED:15981742)]. In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, and increased rate of haemolysis and defective function of the central nervous system. The substrate-binding domain has a 3-layer alpha/beta/alpha structure [(PUBMED:10369661)].

GO process:glutathione biosynthetic process (GO:0006750)
GO function:ATP binding (GO:0005524), glutathione synthase activity (GO:0004363)

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