The domain within your query sequence starts at position 512 and ends at position 879; the E-value for the DUF608 domain shown below is 1.3e-153.

GRFGYLEGQEYRMYNTYDVHFYASFALVMLWPKLELSLQYDMALATLKEDLTRRRYLMSG
VVAPVKRRNVIPHDIGDPDDEPWLRVNAYLIHDTADWKDLNLKFVLQIYRDYYLTGDQGF
LEDMWPVCLAVMESEMKFDKDQDGLIENGGYADQTYDAWVTTGPSAYCGGLWLAAVAVMV
QMAVLCGAQDVQERFASILCRGREAYERLLWNGRYYNYDSSSHPQSRSIMSDQCAGQWFL
RACGLGEGDTEVFPTLHVVRALQTIFELNVQAFAGGAMGAVNGMHPHGVPDRSSVQSDEV
WVGVVYGLAATMIQEGLTWEGFRTAEGCYRTVWERLGLAFQTPEAYCQQQVFRSLAYMRP
LSIWAMQL

DUF608

 DUF608
PFAM accession number:PF04685
Interpro abstract (IPR006775):

This entry represents the catalytic region found in the CAZyme GH116 family members, which presently includes enzymes with beta-glucosidase ( EC 3.2.1.21 ), beta-xylosidase ( EC 3.2.1.37 ) and glucocerebrosidase ( EC 3.2.1.45 ) activity [ (PUBMED:20427274) ]. Proteins containing this domain include animal non-lysosomal glucosylceramidase GBA2, which catalyse the conversion of glucosylceramide to free glucose and ceramide [ (PUBMED:17105727) ]. GBA2 is involved in sphingomyelin generation and prevention of glycolipid accumulation and may also catalyse the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo [ (PUBMED:17080196) ]. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia [ (PUBMED:23332917) ]. The catalytic nucleophile, identified in Q97YG8 is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups [ (PUBMED:20427274) ].

GO function:hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF608