Structural Classification of Proteins
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Fold: Folate-binding domain

duplication: consists of two beta(2)-alpha-beta(3)-alpha subdomains swapped with the first strands

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Folate-binding domain [103024]
    duplication: consists of two beta(2)-alpha-beta(3)-alpha subdomains swapped with the first strands

Superfamilies:

  1. Folate-binding domain [103025] (2)
    some topological similarity to Formylmethanofuran:tetrahydromethanopterin formyltransferase
    link to SUPERFAMILY database - Superfamily
    1. Aminomethyltransferase folate-binding domain [103026] (5)
      1. N,N-dimethylglycine oxidase domain 3 [103027]
        1. Arthrobacter globiformis [TaxId: 1665] [103028] (3) picpic
      2. Hypothetical protein YgfZ, N-terminal domain [103029]
        1. Escherichia coli [TaxId: 562] [103030] (2) picpic
          SQ P39179
      3. Glycine cleavage system T protein, GcvT [111012]
        1. Thermotoga maritima [TaxId: 2336] [111013] (4) picpic
          SQ Q9WY54
        2. Escherichia coli [TaxId: 562] [111014] (1) picpic
          SQ P27248
        3. Pyrococcus horikoshii [TaxId: 53953] [117996] (1) picpic
          SQ O58888
    2. TrmE formyl-THF-binding domain [117997] (1)
      dimeric biological unit; one subunit domain corresponds to one "unswapped" subdomain of the other family
      1. TrmE formyl-THF-binding domain [117998]
        1. Thermotoga maritima [TaxId: 2336] [117999] (2) picpic
          SQ Q9WYA4
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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