Structural Classification of Proteins
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Fold: DinB/YfiT-like putative metalloenzymes

core: 4 helices; bundle, closed, left-handed twist; an unusual topology with a higher contact order

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: DinB/YfiT-like putative metalloenzymes [109853]
    core: 4 helices; bundle, closed, left-handed twist; an unusual topology with a higher contact order

Superfamilies:

  1. DinB/YfiT-like putative metalloenzymes [109854] (4)
    contains metal-binding site on the bundle surface surrounded by loops
    link to SUPERFAMILY database - Superfamily
    1. YfiT-like putative metal-dependent hydrolases [109855] (1)
      probably distantly related to the DinB family (Pfam 05163)
      1. YfiT [109856]
        1. Bacillus subtilis [TaxId: 1423] [109857] (1) picpic
          SQ O31562
    2. DinB-like [140603] (4)
      Pfam 05163
      1. Hypothetical protein BH3987 [140604]
        family assignment by RPS BLAST hit; similar to YfiT subunit fold and metal-binding site, but different dimerisation mode
        1. Bacillus halodurans [TaxId: 86665] [140605] (2) picpic
          SQ Q9RC77 1-141
      2. Hypothetical protein BCE2162 [158513]
        1. Bacillus cereus [TaxId: 1396] [158514] (2) picpic
          SQ Q739H9 1-142
      3. Hypothetical protein DR1065 [158515]
        1. Deinococcus radiodurans [TaxId: 1299] [158516] (1) picpic
          SQ Q9RVG4 2-184
      4. Hypothetical protein ExigDRAFT_2445 [158517]
        1. Exiguobacterium sibiricum 255-15 [TaxId: 262543] [158518] (1) picpic
          SQ Q41IB9 1-147
    3. Sden0562-like [158519] (1)
      Pfam 09351; DUF1993
      1. Hypothetical protein Sden0562 [158520]
        1. Shewanella denitrificans [TaxId: 192073] [158521] (4) picpic
          SQ Q12RS4 1-171
    4. Maleylpyruvate isomerase-like [158522] (1)
      1. Micothiol-dependent maleylpyruvate isomerase [158523]
        1. Corynebacterium glutamicum [TaxId: 1718] [158524] (2) picpic
          SQ Q8NLC1 1-160
          Cgl3021
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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