Structural Classification of Proteins
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Fold: EreA/ChaN-like

Core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order:51423;

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: EreA/ChaN-like [159500]
    Core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order:51423;

Superfamilies:

  1. EreA/ChaN-like [159501] (3)
    there are four conserved residues in the putative active site: two His and two Glu
    1. ChaN-like [159502] (1)
      Pfam 04187; DUF399; Ferric uptake regulator CjrA
      1. Heme transport protein ChaN [159503]
        1. Campylobacter jejuni [TaxId: 197] [159504] (1) picpic
          SQ Q0PBW2 27-281
    2. PMT domain-like [159505] (1)
      This is the second from the PMT C-terminus; it retains the superfamily fold and the active site mainchain conformation but lacks the conserved in the other two families His and Glu residues
      1. Dermonecrotic toxin, ToxA [159506]
        Synonym: Mitogenic toxin PMT
        1. Pasteurella multocida [TaxId: 747] [159507] (4) picpic
          SQ P17452 875-1093
    3. EreA-like [159508] (2)
      Pfam 05139; Erythromycin esterase-like; the superfamily core is decorated with insertion of a four-helical bundle and a C-terminal alpha+beta extension
      1. Succinoglycan biosynthesis protein BC3120 [159509]
        1. Bacillus cereus [TaxId: 1396] [159510] (3) picpic
          SQ Q81BN2 40-442
      2. Succinoglycan biosynthesis protein BC3205 [159511]
        1. Bacillus cereus [TaxId: 1396] [159512] (1) picpic
          SQ Q81BF7 33-445

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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