SCOPe 2.06: Domain d1t3m.2: 1t3m C:,D:

Lineage for d1t3m.2 (1t3m C:,D:)

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 folds)

3. Fold d.153: Ntn hydrolase-like [56234] (2 superfamilies)
   4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing

4. Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families)
   N-terminal residue provides two catalytic groups, nucleophile and proton donor

5. Family d.153.1.5: (Glycosyl)asparaginase [56261] (2 proteins)
   automatically mapped to Pfam PF01112

6. Protein Glycosylasparaginase (aspartylglucosaminidase, AGA) [56262] (5 species)
   the precursor chain is cleaved onto 2 fragments by autoproteolysis

7. Species Escherichia coli [TaxId:562] [103315] (3 PDB entries)
   Uniprot P37595
   isoaspartyl peptidase with L-asparaginase activity
   putative L-asparaginase YbiK

8. Domain d1t3m.2: 1t3m C:,D: [106362]
   complexed with na, no3

Details for d1t3m.2

PDB Entry: 1t3m, 1.65 Å

PDB Description: Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli

PDB Compounds: (C:) Putative L-asparaginase, (D:) Putative L-asparaginase

SCOPe Domain Sequences for d1t3m.2:

Sequence; same for both SEQRES and ATOM records:

>g1t3m.2 d.153.1.5 (C:,D:) Glycosylasparaginase (aspartylglucosaminidase, AGA) {Escherichia coli [TaxId: 562]}
kaviaihggagaisraqmslqqelryiealsaivetgqkmleagesaldvvteavrllee
cplfnagigavftrdetheldacvmdgntlkagavagvshlrnpvlaarlvmeqsphvmm
igegaenfafargmervspeifstslryeqllaarkXtvgavaldldgnlaaatstggmt
nklpgrvgdsplvgagcyannasvavsctgtgevfiralaaydiaalmdygglslaeace
rvvmeklpalggsggliaidhegnvalpfntegmyrawgyagdtpttgiyr

Timeline for d1t3m.2:

• d1t3m.2 first appeared in SCOP 1.69
  
• d1t3m.2 appears in SCOPe 2.05
  
• d1t3m.2 appears in SCOPe 2.07
  
• d1t3m.2 appears in the current release, SCOPe 2.08