Fold: Lipocalins

barrel, closed or opened; n=8, S=12; meander

Lineage:

1. Root: scop
2. Class: All beta proteins [48724]
3. Fold: Lipocalins [50813]
   barrel, closed or opened; n=8, S=12; meander

Superfamilies:

1. Lipocalins [50814] (9)
   bind hydrophobic ligands in their interior
   uperfamily
   1. Retinol binding protein-like [50815] (30)
      barrel, closed; n=8, S=12, meander
   2. Fatty acid binding protein-like [50847] (28)
      ten-stranded meander beta-sheet folded upon itself
      relates to the common fold by opening the barrel and insertion of beta-hairpin
   3. Thrombin inhibitor [50872] (1)
      topology permutation: strands 2 and 3 swapped their positions in the barrel
   4. Hypothetical protein YodA [101863] (1)
      bacterial metal-binding, lipocalin-like protein
   5. Hypothetical protein YwiB [101866] (1)
      bacterial proteins with a fatty acid binding protein-like fold
   6. Phenolic acid decarboxylase (PAD) [141469] (1)
      Pfam 05870; dimeric enzyme made of lipocalin-like subunits
   7. Dinoflagellate luciferase repeat [141472] (1)
      PfamB 017809; comprises a fatty acid binding protein-like fold, wrapped into the extra N- and C-terminal 'tails'
   8. Rv2717c-like [141475] (2)
      bacterial and plant proteins with a fatty acid binding protein-like fold
   9. All1756-like [159230] (1)
      cyanobacterial proteins with duplicated fatty acid binding protein-like domains; N-terminal and C-terminal domains correspond to PfamB 40396 and PfamB 60468, respectively

Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009 Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk