SCOPe 2.06: Domain d1raka2: 1rak A:56-375

Lineage for d1raka2 (1rak A:56-375)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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.1.9: 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.1.9.5: Cytosine deaminase catalytic domain [69390] (1 protein)
   automatically mapped to Pfam PF13147
   automatically mapped to Pfam PF07969

6. Protein Cytosine deaminase catalytic domain [69391] (1 species)

7. Species Escherichia coli [TaxId:562] [69392] (8 PDB entries)
   Uniprot P25524

8. Domain d1raka2: 1rak A:56-375 [111762]
   Other proteins in same PDB: d1raka1
   complexed with fe, fpy, gol; mutant

Details for d1raka2

PDB Entry: 1rak, 1.32 Å

PDB Description: bacterial cytosine deaminase d314s mutant bound to 5-fluoro-4-(s)- hydroxyl-3,4-dihydropyrimidine.

PDB Compounds: (A:) Cytosine deaminase

SCOPe Domain Sequences for d1raka2:

Sequence; same for both SEQRES and ATOM records:

>d1raka2 c.1.9.5 (A:56-375) Cytosine deaminase catalytic domain {Escherichia coli [TaxId: 562]}
pfvephihldttqtagqpnwnqsgtlfegierwaerkallthddvkqrawqtlkwqiang
iqhvrthvdvsdatltalkamlevkqevapwidlqivafpqegilsypngealleealrl
gadvvgaiphfeftreygveslhktfalaqkydrlidvhcdeiddeqsrfvetvaalahh
egmgarvtashttamhsyngaytsrlfrllkmsginfvanplvnihlqgrfdtypkrrgi
trvkemlesginvcfghdsvfdpwyplgtanmlqvlhmglhvcqlmgygqindglnlith
hsartlnlqdygiaagnsan

Timeline for d1raka2:

• d1raka2 first appeared in SCOP 1.71
  
• d1raka2 appears in SCOPe 2.05
  
• d1raka2 appears in SCOPe 2.07
  
• d1raka2 appears in the current release, SCOPe 2.08