SCOP 1.65: Domain d1bli_2: 1bli 3-393

Lineage for d1bli_2 (1bli 3-393)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 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] (9 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (22 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 Bacterial alpha-amylase [51447] (7 species)

7. Species Bacillus licheniformis [TaxId:1402] [51448] (4 PDB entries)

8. Domain d1bli_2: 1bli 3-393 [28702]
   Other proteins in same PDB: d1bli_1
   complexed with ca, na; mutant

Details for d1bli_2

PDB Entry: 1bli, 1.9 Å

PDB Description: bacillus licheniformis alpha-amylase

SCOP Domain Sequences for d1bli_2:

Sequence; same for both SEQRES and ATOM records:

>d1bli_2 c.1.8.1 (3-393) Bacterial alpha-amylase {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgkaw
dwevsnefgnydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflr
dwvnhvrektgkemftvaeywsydlgalenylnktnfnhsvfdvplhyqfhaastqgggy
dmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvf
ygdmygtkgdsqreipalkhkiepilkarkq

Timeline for d1bli_2:

• d1bli_2 first appeared (with stable ids) in SCOP 1.55
  
• d1bli_2 appears in SCOP 1.63
  
• d1bli_2 appears in SCOP 1.67
  
• d1bli_2 appears in the current release, SCOPe 2.08, called d1blia2