SCOPe 2.06: Domain d1fwcc2: 1fwc C:130-422,C:476-567

Lineage for d1fwcc2 (1fwc C:130-422,C:476-567)

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.1.9.2: alpha-subunit of urease, catalytic domain [51560] (1 protein)

6. Protein alpha-subunit of urease, catalytic domain [51561] (4 species)

7. Species Klebsiella aerogenes [TaxId:28451] [51562] (28 PDB entries)

8. Domain d1fwcc2: 1fwc C:130-422,C:476-567 [29032]
   Other proteins in same PDB: d1fwca_, d1fwcb_, d1fwcc1
   complexed with ni

Details for d1fwcc2

PDB Entry: 1fwc, 2 Å

PDB Description: klebsiella aerogenes urease, c319a variant at ph 8.5

PDB Compounds: (C:) urease

SCOPe Domain Sequences for d1fwcc2:

Sequence; same for both SEQRES and ATOM records:

>d1fwcc2 c.1.9.2 (C:130-422,C:476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes [TaxId: 28451]}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf

Timeline for d1fwcc2:

• d1fwcc2 first appeared (with stable ids) in SCOP 1.55
  
• d1fwcc2 appears in SCOPe 2.05
  
• d1fwcc2 appears in SCOPe 2.07
  
• d1fwcc2 appears in the current release, SCOPe 2.08