SCOP 1.69: Domain d1p1ma2: 1p1m A:50-330

Lineage for d1p1ma2 (1p1m A:50-330)

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.1.9: Metallo-dependent hydrolases [51556] (13 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.1.9.9: Hypothetical protein TM0936, probable catalytic domain [82258] (1 protein)

6. Protein Hypothetical protein TM0936, probable catalytic domain [82259] (1 species)

7. Species Thermotoga maritima [TaxId:243274] [82260] (2 PDB entries)

8. Domain d1p1ma2: 1p1m A:50-330 [87697]
   Other proteins in same PDB: d1p1ma1
   structural genomics

Details for d1p1ma2

PDB Entry: 1p1m, 1.5 Å

PDB Description: structure of thermotoga maritima amidohydrolase tm0936 bound to ni and methionine

SCOP Domain Sequences for d1p1ma2:

Sequence; same for both SEQRES and ATOM records:

>d1p1ma2 c.1.9.9 (A:50-330) Hypothetical protein TM0936, probable catalytic domain {Thermotoga maritima}
alfnththapmtllrgvaedlsfeewlfskvlpiedrltekmayygtilaqmemarhgia
gfvdmyfheewiakavrdfgmralltrglvdsngddggrleenlklynewngfegrifvg
fgphspylcseeylkrvfdtakslnapvtihlyetskeeydledilniglkevktiaahc
vhlperyfgvlkdipffvshnpasnlklgngiapvqrmiehgmkvtlgtdgaasnnslnl
ffemrlasllqkaqnprnldvntclkmvtydgaqamgfksg

Timeline for d1p1ma2:

• d1p1ma2 first appeared in SCOP 1.65
  
• d1p1ma2 appears in SCOP 1.67
  
• d1p1ma2 appears in SCOP 1.71
  
• d1p1ma2 appears in the current release, SCOPe 2.08