The domain within your query sequence starts at position 32 and ends at position 333; the E-value for the Asparaginase_2 domain shown below is 2.5e-86.
NTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMI MDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTS RDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKPSGFLKQSISPHKEEVDIHSHDTIGMVV IHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQ AVEYMRGGDDPAIACQKVILRIQKYYPNFFGAVICASVNGSYGAACNKLPTFTQFSFMVS NS
Asparaginase_2 |
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PFAM accession number: | PF01112 |
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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: Glycosylasparaginase catalyses: |
GO function: | hydrolase activity (GO:0016787) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Asparaginase_2