Fold: Single-stranded left-handed beta-helix

superhelix turns are made of parallel beta-strands and (short) turns

Lineage:

1. Root: scop
2. Class: All beta proteins [48724]
3. Fold: Single-stranded left-handed beta-helix [51160]
   superhelix turns are made of parallel beta-strands and (short) turns

Superfamilies:

1. Trimeric LpxA-like enzymes [51161] (8)
   superhelical turns are made of three short strands; duplication: the sequence hexapeptide repeats correspond to individual strands
   uperfamily
   1. UDP N-acetylglucosamine acyltransferase [51162] (2)
   2. Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD [51165] (1)
      contains extra N-terminal 3-helical domain
   3. Galactoside acetyltransferase-like [51168] (4)
   4. GlmU C-terminal domain-like [51171] (4)
   5. gamma-carbonic anhydrase-like [51174] (3)
      archaeal hexapeptide repeat proteins
   6. Serine acetyltransferase [110309] (2)
   7. YdcK-like [141583] (1)
      part of Pfam 00132
   8. PglD-like [159280] (1)
      contains extra N-terminal alpha/beta subdomain
2. An insect antifreeze protein [51177] (1)
   superhelical turns are made of three short strands
   uperfamily
   1. An insect antifreeze protein [51178] (2)
3. Adhesin YadA, collagen-binding domain [101967] (1)
   superhelical turns are made of two short strands
   uperfamily
   1. Adhesin YadA, collagen-binding domain [101968] (1)
4. Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain [159283] (1)
   probable rudiment form of the LpxA-like hexapeptide domain
   1. Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain [159284] (1)
      corresponds to the N-terminal part of Pfam 01050, but does not extend to the conserved functional motif; the predicted cupin fold may reside in the rest of the Pfam domain

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