SCOPe 2.05: Domain d1ef2a2: 1ef2 A:1130-1422,A:1476-1567

Lineage for d1ef2a2 (1ef2 A:1130-1422,A:1476-1567)

1. Root: SCOPe 2.05

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] (27 PDB entries)

8. Domain d1ef2a2: 1ef2 A:1130-1422,A:1476-1567 [29051]
   Other proteins in same PDB: d1ef2a1, d1ef2b_, d1ef2c_
   complexed with mn

Details for d1ef2a2

PDB Entry: 1ef2, 2.5 Å

PDB Description: crystal structure of manganese-substituted klebsiella aerogenes urease

PDB Compounds: (A:) urease alpha subunit

SCOPe Domain Sequences for d1ef2a2:

Sequence; same for both SEQRES and ATOM records:

>d1ef2a2 c.1.9.2 (A:1130-1422,A:1476-1567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes [TaxId: 28451]}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglkihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf

Timeline for d1ef2a2:

• d1ef2a2 first appeared (with stable ids) in SCOP 1.55
  
• d1ef2a2 appears in SCOPe 2.04
  
• d1ef2a2 appears in SCOPe 2.06
  
• d1ef2a2 appears in the current release, SCOPe 2.08