SCOP 1.69: Domain d1bpl.1: 1bpl A:,B:193-393

Lineage for d1bpl.1 (1bpl A:,B:193-393)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (11 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (24 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 d1bpl.1: 1bpl A:,B:193-393 [28703]
   Other proteins in same PDB: d1bplb1

Details for d1bpl.1

PDB Entry: 1bpl, 2.2 Å

PDB Description: glycosyltransferase

SCOP Domain Sequences for d1bpl.1:

Sequence; same for both SEQRES and ATOM records:

>g1bpl.1 c.1.8.1 (A:,B:193-393) Bacterial alpha-amylase {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgkaX
ydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflrdwvnhvrekt
gkemftvaeywqndlgalenylnktnfnhsvfdvplhyqfhaastqgggydmrkllnstv
vskhplkavtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvfygdmygtkgd
sqreipalkhkiepilkarkq

Timeline for d1bpl.1:

• d1bpl.1 first appeared (with stable ids) in SCOP 1.55
  
• d1bpl.1 appears in SCOP 1.67
  
• d1bpl.1 appears in SCOP 1.71
  
• d1bpl.1 appears in the current release, SCOPe 2.08