The domain within your query sequence starts at position 100 and ends at position 288; the E-value for the PRK domain shown below is 3.4e-60.

AIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDHPDA
FDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLEL
LDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVV
PRGSGNTVA

PRK

PRK
PFAM accession number:PF00485
Interpro abstract (IPR006083):

Phosphoribulokinase (PRK) EC 2.7.1.19 catalyses the ATP-dependent phosphorylation of ribulose-5-phosphate to ribulose-1,5-phosphate, a key step in the pentose phosphate pathway where carbon dioxide is assimilated by autotrophic organisms [ (PUBMED:2175647) ]. In general, plant enzymes are light-activated by the thioredoxin/ferredoxin system, while those from photosynthetic bacteria are regulated by a system that has an absolute requirement for NADH. Thioredoxin/ferredoxin regulation is mediated by the reversible oxidation/reduction of sulphydryl and disulphide groups.

Uridine kinase (pyrimidine ribonucleoside kinase) is the rate-limiting enzyme in the pyrimidine salvage pathway. It catalyzes the following reaction: ATP + Uridine = ADP + UMP

Pantothenate kinase ( EC 2.7.1.33 ) catalyzes the rate-limiting step in the biosynthesis of coenzyme A, the conversion of pantothenate to D-4'-phosphopantothenate in the presence of ATP.

GO function:ATP binding (GO:0005524), kinase activity (GO:0016301)

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