The domain within your query sequence starts at position 42 and ends at position 348; the E-value for the Asparaginase_2 domain shown below is 1.3e-62.

GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNA
GIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIP
PCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLELAERVETDFIQLKRRRQ
SSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ
NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSPFLACEDGVLG
GVIVLRS

Asparaginase_2

 Asparaginase_2
PFAM accession number:PF01112
Interpro abstract (IPR000246):

Threonine peptidases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. The threonine peptidases belong to clan PB or are unassigned, clan T-. The type example for this clan is the archaean proteasome beta component of Thermoplasma acidophilum.

This group of sequences have a signature that places them in MEROPS peptidase family T2 (clan PB(T)). The glycosylasparaginases ( EC 3.5.1.26 ) are threonine peptidases. Also in this family is L-asparaginase ( EC 3.5.1.1 ), which catalyses the following reaction: L-asparagine + H 2 O = L-aspartate + NH 3

Glycosylasparaginase catalyses: N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartate cleaving the GlcNAc-Asn bond that links oligosaccharides to asparagine in N-linked glycoproteins. The enzyme is composed of two non-identical alpha/beta subunits joined by strong non-covalent forces and has one glycosylation site located in the alpha subunit [ (PUBMED:8877373) ] and plays a major role in the degradation of glycoproteins.

GO function:hydrolase activity (GO:0016787)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Asparaginase_2