Structural Classification of Proteins
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Fold: Spectrin repeat-like

3 helices; bundle, closed, left-handed twist; up-and-down

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: Spectrin repeat-like [46965]
    3 helices; bundle, closed, left-handed twist; up-and-down

Superfamilies:

  1. Spectrin repeat [46966] (1) picpic
    link to SUPERFAMILY database - Superfamily
  2. Enzyme IIa from lactose specific PTS, IIa-lac [46973] (1) picpic
    link to SUPERFAMILY database - Superfamily
  3. Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain [46977] (1) picpic
    link to SUPERFAMILY database - Superfamily
  4. Smac/diablo [46984] (1) picpic
    link to SUPERFAMILY database - Superfamily
  5. BAG domain [63491] (1) picpic
    link to SUPERFAMILY database - Superfamily
  6. GAT-like domain [89009] (2) picpic
    link to SUPERFAMILY database - Superfamily
  7. Tubulin chaperone cofactor A [46988] (1) picpic
    link to SUPERFAMILY database - Superfamily
  8. Ribosomal protein S20 [46992] (1) picpic
    link to SUPERFAMILY database - Superfamily
  9. Glycogen synthesis protein GlgS [109747] (1) picpic
    link to SUPERFAMILY database - Superfamily
  10. Alpha-hemoglobin stabilizing protein AHSP [109751] (1) picpic
    the bundle twist angle is close to zero (small positive value); similar to the RRF alpha-helical bundle, scop_sf 55194
    link to SUPERFAMILY database - Superfamily
  11. PhoU-like [109755] (1) picpic
    duplication: consists of two sequence each repeats adopting this fold
    link to SUPERFAMILY database - Superfamily
  12. XseB-like [116842] (1) picpic
    helix-swapped homodimer
    link to SUPERFAMILY database - Superfamily
  13. MIT domain [116846] (1) picpic
    link to SUPERFAMILY database - Superfamily
  14. PPK N-terminal domain-like [140356] (1) picpic
    link to SUPERFAMILY database - Superfamily
  15. MIT domain-like [140361] (1) picpic
    link to SUPERFAMILY database - Superfamily
  16. Efb C-domain-like [158366] (1) 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