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