Structural Classification of Proteins
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Fold: Reductase/isomerase/elongation factor common domain

barrel, closed; n=6, S=10; greek-key

Lineage:

  1. Root: scop
  2. Class: All beta proteins [48724]
  3. Fold: Reductase/isomerase/elongation factor common domain [50412]
    barrel, closed; n=6, S=10; greek-key

Superfamilies:

  1. Riboflavin synthase domain-like [63380] (3)
    link to SUPERFAMILY database - Superfamily
    1. Riboflavin synthase [63783] (2) picpic
      duplication: consists of two homologous domains
    2. Ferredoxin reductase FAD-binding domain-like [63381] (19) picpic
      coupled with a NADP-binding domain of alpha/beta class
    3. NADPH-cytochrome p450 reductase FAD-binding domain-like [50438] (3) picpic
      there is an alpha-helical subdomain inserted in this domain
  2. Riboflavin kinase-like [82114] (2)
    link to SUPERFAMILY database - Superfamily
    1. ATP-dependent riboflavin kinase-like [82115] (3) picpic
    2. CTP-dependent riboflavin kinase-like [159154] (2) picpic
      Pfam 01982; newly characterized archaeal family (formerly DUF120)
  3. FucI/AraA C-terminal domain-like [50443] (2)
    link to SUPERFAMILY database - Superfamily
    1. L-fucose isomerase, C-terminal domain [50444] (1) picpic
    2. AraA C-terminal domain-like [141331] (1) picpic
      C-terminal part of Pfam 02610
  4. Translation proteins [50447] (6)
    link to SUPERFAMILY database - Superfamily
    1. Elongation factors [50448] (18) picpic
    2. Ribosomal protein L3 [50461] (4) picpic
    3. Ribosomal protein L35ae [117220] (1) picpic
      Pfam 01247
    4. RimM N-terminal domain-like [141338] (1) picpic
      Pfam 01782
    5. Gar1-like SnoRNP [141341] (1) picpic
      stand alone proteins, which are similar structurally but not sequentially to the elongation factor domains, unlike PF0907
    6. AlaX-M N-terminal domain-like [159161] (1) picpic
      Does NOT belong to Pfam 01411

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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