The domain within your query sequence starts at position 179 and ends at position 363; the E-value for the Pribosyl_synth domain shown below is 1.6e-103.

DYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIH
PSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMAT
HGLLSSDAPRLIEESAIDEVVVTNTIPHEIQKLQCPKIKTVDISMILSEAIRRIHNGESM
SYLFR

Pribosyl_synth

Pribosyl_synth
PFAM accession number:PF14572
Interpro abstract (IPR005946):

Ribose-phosphate diphosphokinase, also known as ribose-phosphate pyrophosphokinase (RPPK), or phosphoribosyldiphosphate synthetase ( EC 2.7.6.1 ), catalyses the transfer of an intact diphosphate (PP) group from ATP to ribose-5-phosphate (R-5-P), which results in the formation of AMP and 5-phospho-D-ribosyl--1-diphosphate (PRPP).

PRPP is an essential precursor for purine and pyrimidine nucleotides, both in the de novo synthesis and in the salvage pathway, as well as in the synthesis of pyridine nucleotide coenzymes. The activity of PPPK is highly regulated. Besides competitive inhibition at the substrate binding sites, most RPPKs are regulated in an allosteric manner, in which ADP generally acts as the most potent inhibitor. In some systems, close homologues lacking enzymatic activity exist and perform regulatory functions.

GO process:nucleotide biosynthetic process (GO:0009165)
GO function:ribose phosphate diphosphokinase activity (GO:0004749), magnesium ion binding (GO:0000287)

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