SCOPe 2.03: Domain d1vfma3: 1vfm A:121-502

Lineage for d1vfma3 (1vfm A:121-502)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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 Maltogenic amylase, central domain [51465] (4 species)
   contains an additional N-terminal domain

7. Species Thermoactinomyces vulgaris, TVAII [TaxId:2026] [51467] (16 PDB entries)

8. Domain d1vfma3: 1vfm A:121-502 [120044]
   Other proteins in same PDB: d1vfma1, d1vfma2, d1vfmb1, d1vfmb2
   automatically matched to d1bvza3
   complexed with ca

Details for d1vfma3

PDB Entry: 1vfm, 2.9 Å

PDB Description: crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 2/alpha-cyclodextrin complex

PDB Compounds: (A:) Neopullulanase 2

SCOPe Domain Sequences for d1vfma3:

Sequence; same for both SEQRES and ATOM records:

>d1vfma3 c.1.8.1 (A:121-502) Maltogenic amylase, central domain {Thermoactinomyces vulgaris, TVAII [TaxId: 2026]}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrlnvanevdhafwrefrrlvkslnpdalivgeiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
nterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr

Timeline for d1vfma3:

• d1vfma3 first appeared in SCOP 1.73
  
• d1vfma3 appears in SCOPe 2.02
  
• d1vfma3 appears in SCOPe 2.04
  
• d1vfma3 appears in the current release, SCOPe 2.08