The domain within your query sequence starts at position 94 and ends at position 356; the E-value for the Carb_kinase domain shown below is 6.2e-63.

IGIVGGCQEYTGAPYFAGISALKVGADLTHVFCAREAAPVIKSYSPELIVHPVLDSSNAV
EEVEKWLPRLHALVVGPGLGRDDLLLNNVRGILESTKARDIPVVIDADGLWLVAQQPALI
HSYHKAILTPNHVEFSRLWEAVLSSPMDSNDLKGSTLKLSQALGNITVVQKGEQDLISNG
QQVLVCNQEGSSRRCGGQGDLLSGSLGVMVHWALRAGPEKTNGSSPLLVAAWGACTLTRE
CNRQAFQKYGRSTTTTDMITEVG

Carb_kinase

Carb_kinase
PFAM accession number:PF01256
Interpro abstract (IPR000631):

Hydration of NAD(P)H to NAD(P)HX, which inhibits several dehydrogenases, is corrected by an ATP-dependent dehydratase and an epimerase. The ATP-dependent dehydratase has been identified as the product of the vertebrate Carkd (carbohydrate kinase domain) gene [ (PUBMED:24611804) ]. In E. coli, it is found as the C-terminal domain of a bifunctional enzyme (YjeF) that also includes the epimerase and uses ADP instead of ATP [ (PUBMED:21994945) ]. These enzymes are widespread in eukaryotes, prokaryotes, and archaea.

GO function:ADP-dependent NAD(P)H-hydrate dehydratase activity (GO:0052855)

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