The domain within your query sequence starts at position 473 and ends at position 593; the E-value for the AIRS domain shown below is 1.2e-17.

FAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDSIGQDLVAMCVNDILAQGAEPL
FFLDYFSCGKLDLSTTEAVIAGIAAACQQAGCALLGGETAEMPNMYPPGEYDLAGFAVGA
M

AIRS

AIRS
PFAM accession number:PF00586
Interpro abstract (IPR016188):

This entry represents a structural domain with a core structure consisting of beta-alpha-beta-alpha-beta(2), which is found in two enzymes of the purine biosynthetic pathway: at the N-terminal of aminoimidazole ribonucleotide (AIR) synthetase (PurM) [(PUBMED:10508786)], as well as the N1 and N2 domains of formylglycinamide ribonucleotide (FGAR) amidotransferase (PurL) (PurM-like module) [(PUBMED:15301531)]. PurM and PurL utilise ATP to activate the oxygen of an amide within their substrate toward nucleophilic attack by a nitrogen. PurM uses the product of PurL, formylglycinamidine ribonucleotide (FGAM) and ATP to make AIR, ADP and P(i). It is also found as domains 1 and 3 in phosphoribosylformylglycinamidine synthase II (smPurL) (EC 6.3.5.3) (carries a duplication: tandem repeats of two PurM-like units arranged like the PurM subunits in the dimer) [(PUBMED:16544324)].

This domain is also found at the N-terminal of thiamine monophosphate kinase (EC 2.7.4.16) (ThiL) [(PUBMED:9188462)]. ThiL phosphorylates thiamin monophosphate to form thiamin pyrophosphate, an essential cofactor that is synthsised de novo by Salmonella typhimurium.

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