Structural Classification of Proteins
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Superfamily: dUTPase-like

forms tight trimer through an additional beta-sheet in each subunit
subunit beta-sheets are orthogonally packed around the three-fold axis
link to SUPERFAMILY database - Superfamily

Lineage:

  1. Root: scop
  2. Class: All beta proteins [48724]
  3. Fold: beta-clip [51268]
    double-stranded ribbon sharply bent in two places; the ribbon ends form incomplete barrel; jelly-roll
  4. Superfamily: dUTPase-like [51283]
    forms tight trimer through an additional beta-sheet in each subunit
    subunit beta-sheets are orthogonally packed around the three-fold axis
    link to SUPERFAMILY database - Superfamily

Families:

  1. dUTPase-like [51284] (9)
    1. Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) [51285]
      1. Escherichia coli [TaxId: 562] [51286] (10) picpic
        SQ P06968
      2. Mycobacterium tuberculosis, rv2697c [TaxId: 1773] [82213] (8) picpic
      3. Human (Homo sapiens) [TaxId: 9606] [102010] (11) picpic
      4. Feline immunodeficiency virus [TaxId: 11673] [51287] (8) picpic
      5. Equine infectious anemia virus [TaxId: 11665] [51288] (2) picpic
      6. Plasmodium falciparum [TaxId: 5833] [141654] (3) picpic
        SQ Q8II92 1-159
    2. Bifunctional dCTP deaminase/dUTPase [89425]
      elaborated fold with additional structures
      1. Archaeon Methanococcus jannaschii [TaxId: 2190] [89426] (5) picpic
        synonym: Methanocaldococcus jannaschii
    3. Deoxycytidine triphosphate deaminase (dCTP deaminase) [117335]
      1. Escherichia coli [TaxId: 562] [117336] (3) picpic
        SQ P28248
    4. Monomeric viral dUTPase [141655]
      related to the trimeric dUTPase domain by domain duplication, fusion and partial deletion; retains only one of the three ancestral active sites
      1. Epstein-barr virus [TaxId: 10376] [141656] (4) picpic
        SQ P03195 121-256! SQ P03195 4-116
        Human herpesvirus 4

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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