Structural Classification of Proteins
home mail help root up expand collapse

Family: Excisionase-like

kinked C-terminal helix

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: Putative DNA-binding domain [46954]
    core: 3 helices; architecture is similar to that of the "winged helix" fold but topology is different
  4. Superfamily: Putative DNA-binding domain [46955]
    link to SUPERFAMILY database - Superfamily
  5. Family: Excisionase-like [46891]
    kinked C-terminal helix

Protein Domains:

  1. mu transposase, DNA-binding domain [46892]
    1. Bacteriophage mu [TaxId: 10677] [46893] (4)
      1. 1qpm picpic
        1. chain a [16230] picpiclink
      2. 1g4d picpic
        protein/DNA complex
        1. chain a [16227] picpiclink
      3. 1tns picpic
        1. chain a [16228] picpiclink
      4. 1tnt picpic
        1. chain a [16229] picpiclink
  2. Excisionase Xis [89004]
    1. Bacteriophage lambda [TaxId: 10710] [89005] (8)
      SQ P03699 1-55
      1. 1rh6 picpic
        mutant
        1. chain a [104935] picpiclink
        2. chain b [104936] picpiclink
      2. 2og0 picpic
        automatically matched to d1lx8a_
        mutant
        1. region a:1-51 [139059] picpiclink
      3. 2og0 picpic
        automatically matched to d1lx8a_
        mutant
        1. region b:1-52 [139060] picpiclink
      4. 2ief picpic
        automatically matched to d1lx8a_
        mutant
        1. region a:1-55 [137304] picpiclink
      5. 2ief picpic
        automatically matched to d1lx8a_
        mutant
        1. region b:1-54 [137305] picpiclink
      6. 2ief picpic
        automatically matched to d1lx8a_
        mutant
        1. region c:1-53 [137306] picpiclink
      7. 1pm6 picpic
        mutant
        1. chain a [94894] picpiclink
      8. 1lx8 picpic
        C-terminally truncated variant
        mutant
        1. chain a [84734] picpiclink

Enter search key:

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