SCOPe 2.07: Domain d2aaaa2: 2aaa A:1-381

Lineage for d2aaaa2 (2aaa A:1-381)

1. Root: SCOPe 2.07

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.8: (Trans)glycosidases [51445] (15 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (26 proteins)
   members of the family may contain various insert subdomains
   in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain

6. Protein Fungal alpha-amylases [51462] (2 species)

7. Species Aspergillus niger, acid amylase [TaxId:5061] [51463] (1 PDB entry)

8. Domain d2aaaa2: 2aaa A:1-381 [28764]
   Other proteins in same PDB: d2aaaa1
   complexed with ca

Details for d2aaaa2

PDB Entry: 2aaa, 2.12 Å

PDB Description: calcium binding in alpha-amylases: an x-ray diffraction study at 2.1 angstroms resolution of two enzymes from aspergillus

PDB Compounds: (A:) alpha-amylase

SCOPe Domain Sequences for d2aaaa2:

Sequence; same for both SEQRES and ATOM records:

>d2aaaa2 c.1.8.1 (A:1-381) Fungal alpha-amylases {Aspergillus niger, acid amylase [TaxId: 5061]}
lsaaswrtqsiyflltdrfgrtdnsttatcntgneiycggswqgiidhldyiegmgftai
wispiteqlpqdtadgeayhgywqqkiydvnsnfgtadnlkslsdalhargmylmvdvvp
dhmgyagngndvdysvfdpfdsssyfhpyclitdwdnltmvedcwegdtivslpdldtte
tavrtiwydwvadlvsnysvdglridsvlevqpdffpgynkasgvycvgeidngnpasdc
pyqkvldgvlnypiywqllyafesssgsisnlynmiksvasdcsdptllgnfienhdnpr
fakytsdysqaknvlsyiflsdgipivyageeqhyaggkvpynreatwlsgydtsaelyt
wiattnairklaiaadsayit

Timeline for d2aaaa2:

• d2aaaa2 first appeared (with stable ids) in SCOP 1.55, called d2aaa_2
  
• d2aaaa2 appears in SCOPe 2.06
  
• d2aaaa2 appears in the current release, SCOPe 2.08