The domain within your query sequence starts at position 19 and ends at position 335; the E-value for the Dak1 domain shown below is 1.9e-112.

AGLVASNPDLQLLQGHRVALRSDLDTLKGRVALLSGGGSGHEPAHAGFIGKGMLTGVIAG
SVFASPPVGSILAAIRAVAQAGTVGTLLIVKNYTGDRLNFGLAMEQAKAEGISVEMVIVE
DDSAFTVLKKAGRRGLCGTVLIHKVAGALAEEGMGLEEITKRVSVIAKTMGTLGVSLSSC
SVPGATHTFELAADEIELGLGIHGEAGVRRIKIAPVDQIVTLMLDHMTNTSNIFHVPVRS
GSSVVLIVNNLGGLSFLELGIIADAAIRLLEGRGVKVARALVGTFMSALEMPGVSLTLML
VDEPVLKLIDAETTAKA

Dak1

Dak1
PFAM accession number:PF02733
Interpro abstract (IPR004006):

Dihydroxyacetone (Dha) kinases are a family of sequence-conserved enzymes that phosphorylate dihydroxyacetone, glyceraldehyde and other short-chain ketoses and aldoses. They can be divided into two groups according to the source of high-energy phosphate that they utilise, either ATP or phosphoenolpyruvate (PEP). The ATP-dependent forms are the two-domain Dha kinases (DAK), which occur in animals, plants and eubacteria. They consist of a Dha binding (K) and an ATP binding (L) domain. The PEP-dependent forms occur only in eubacteria and a few archaebacteria and consist of three subunits. Two subunits, DhaK and DhaL, are homologous to the K and L domains. Intriguingly, the ADP moiety is not exchanged for ATP but remains permanently bound to the DhaL subunit where it is rephosphorylated in situ by the third subunit, DhaM, which is homologous to the IIA domain of the mannose transporter of the bacterial PEP:sugar phosphotransferase system (PTS) [(PUBMED:16647083), (PUBMED:18957416)].

The DhaK domain consists of two alpha/beta-folds, each containing a six- stranded mixed beta-sheet surrounded by six and three helices, respectively. Dha is bound in hemiaminal linkage to the imidazole nitrogen of an invariant histidine [(PUBMED:12966101), (PUBMED:12813127)].

GO process:glycerol metabolic process (GO:0006071)
GO function:glycerone kinase activity (GO:0004371)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Dak1