SCOPe 2.08: Domain d2ftwa2: 2ftw A:60-393

Lineage for d2ftwa2 (2ftw A:60-393)

1. Root: SCOPe 2.08

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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.1.9: Metallo-dependent hydrolases [51556] (19 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 proteins)
   automatically mapped to Pfam PF13147

6. Protein Dihydropyrimidine amidohydrolase Pyd2 [141805] (2 species)

7. Species Slime mold (Dictyostelium discoideum) [TaxId:44689] [141807] (1 PDB entry)
   Uniprot Q86LT2 60-393

8. Domain d2ftwa2: 2ftw A:60-393 [134084]
   Other proteins in same PDB: d2ftwa1
   complexed with mli, zn

Details for d2ftwa2

PDB Entry: 2ftw, 2.05 Å

PDB Description: Crystal structure of dihydropyrimidinase from dictyostelium discoideum

PDB Compounds: (A:) dihydropyrimidine amidohydrolase

SCOPe Domain Sequences for d2ftwa2:

Sequence; same for both SEQRES and ATOM records:

>d2ftwa2 c.1.9.6 (A:60-393) Dihydropyrimidine amidohydrolase Pyd2 {Slime mold (Dictyostelium discoideum) [TaxId: 44689]}
pggidththfqlpfmgtvsvddfdigtqaavaggttfiidfviptrgqslleaydqwkkw
adekvncdyslhvaitwwseqvsremeilvkergvnsfkcfmayknsfmvtdqemyhifk
rckelgaiaqvhaengdmvfegqkkmlemgitgpeghelsrpealeaeatnraiviadsv
ctpvyivhvqsigaadvickhrkegvrvygepiaaglgvdgshmwnhdwrhaaafvmgpp
irpdprtkgvlmdylargdldcvgtdnctfcadqkamgkddftkipngvngvedrmsivw
engvntgkltwcqfvratsserarifniyprkgr

Timeline for d2ftwa2:

• d2ftwa2 first appeared in SCOP 1.73
  
• d2ftwa2 appears in SCOPe 2.07