Structural Classification of Proteins
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Fold: Saposin-like

5 helices; folded leaf, closed

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: Saposin-like [47861]
    5 helices; folded leaf, closed

Superfamilies:

  1. Saposin [47862] (4)
    Lipid-binding can promote conformational changes and oligomerisation in some members
    link to SUPERFAMILY database - Superfamily
    1. Saposin B [81806] (1)
      the alternative subunit conformation is an open four-helical bundle; helices 3 and 4 form a contiguous helix
      1. Saposin B [81807]
        1. Human (Homo sapiens) [TaxId: 9606] [81808] (1) picpic
    2. NKL-like [47863] (3)
      1. NK-lysin, NKL [47864]
        1. Pig (Sus scrofa) [TaxId: 9823] [47865] (1) picpic
      2. Granulysin, NKG5 protein [81809]
        1. Human (Homo sapiens) [TaxId: 9606] [81810] (1) picpic
      3. Saposin C [89077]
        1. Human (Homo sapiens) [TaxId: 9606] [89078] (7) picpic
    3. Ameobapore A [101266] (1)
      1. Ameobapore A [101267]
        pore-forming toxin
        1. Entamoeba histolytica [TaxId: 5759] [101268] (1) picpic
    4. Swaposin [47866] (1)
      circularly permuted saposin domain inserted in plant acid proteases
      1. (Pro)phytepsin [47867]
        1. Barley (Hordeum vulgare) [TaxId: 4513] [47868] (1) picpic
  2. Bacteriocin AS-48 [47869] (1)
    link to SUPERFAMILY database - Superfamily
    1. Bacteriocin AS-48 [47870] (1)
      1. Bacteriocin AS-48 [47871]
        cyclic peptide
        1. Enterococcus faecalis [TaxId: 1351] [47872] (4) picpic
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MRC site 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