The domain within your query sequence starts at position 41 and ends at position 413; the E-value for the Melibiase_2 domain shown below is 3.5e-190.

TPTMGWLHWERFMCNLDCQEEPDACISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAP
ERDSKGRLQADPQRFPSGIKHLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQT
FADWGVDLLKFDGCHCDSVVSLENGYKYMALALNRTGRSIVYSCEWPLYLRPFHKPNYTD
IQYYCNHWRNFDDVYDSWESIKNILSWTVVYQKEIVEVAGPGSWNDPDMLVIGNFGLSWD
QQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFRKENHIE
VWERPLSNLAWAVAVRNLQEIGGPCPYTIQISSLGRGLACNPGCIITQLLPEKVHLGFYE
WTLTLKTRVNPSG

Melibiase_2

Melibiase_2
PFAM accession number:PF16499
Interpro abstract (IPR002241):

O-Glycosyl hydrolases (EC 3.2.1.) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [(PUBMED:7624375), (PUBMED:8535779)]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

Glycoside hydrolase family 27 comprises enzymes with several known activities; alpha-galactosidase (EC 3.2.1.22); alpha-N-acetylgalactosaminidase (EC 3.2.1.49); isomalto-dextranase (EC 3.2.1.94).

Alpha-galactosidase (melibiase) catalyses the hydrolysis of melibiose into galactose and glucose [(PUBMED:7725791)]. In man, deficiency in the enzyme results in Fabry's disease (X-linked sphingolipidosis). Alpha-N-acetylgalactosaminidase catalyses the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides [(PUBMED:2174888)]. Two conserved Asp residues may be involved in the catalytic mechanism in these enzymes. Deficiency in this enzyme results in Schindler and Kanzaki diseases.

GO process:carbohydrate metabolic process (GO:0005975)
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 Melibiase_2