Structural Classification of Proteins
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Fold: GINS/PriA/YqbF domain

beta(4)-alpha-beta; 3-stranded antiparallel beta-sheet (strands 4,1 and 5) are covered on the same side by the helix and beta hairpin of strands 2 and 3; similarity to the L9 N-domain-like fold (scop_cf 55657) and the PsaD fold (scop_sf 64243)

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: GINS/PriA/YqbF domain [160058]
    beta(4)-alpha-beta; 3-stranded antiparallel beta-sheet (strands 4,1 and 5) are covered on the same side by the helix and beta hairpin of strands 2 and 3; similarity to the L9 N-domain-like fold (scop_cf 55657) and the PsaD fold (scop_sf 64243)

Superfamilies:

  1. PriA/YqbF domain [160059] (4)
    associated with known or presumed DNA-binding domains; this superfamily also includes the C-terminal domain of PriA (PDB entry 1zt2)
    1. YqbF N-terminal domain-like [160060] (2)
      1. Hypothetical protein YqbF [160061]
        1. Bacillus subtilis [TaxId: 1423] [160062] (1) picpic
          SQ P45922 1-49
      2. Mu-like prophage FluMu protein gp35, HI1506 [160063]
        1. Haemophilus influenzae [TaxId: 727] [160064] (1) picpic
          SQ P44228 1-67
    2. PSF2 N-terminal domain-like [160065] (1)
      N-terminal part of Pfam 04128
      1. DNA replication complex GINS protein PSF2 [160066]
        1. Human (Homo sapiens) [TaxId: 9606] [160067] (7) picpic
          SQ Q9Y248 1-61
    3. SLD5 C-terminal domain-like [160068] (1)
      C-terminal part of Pfam 05916
      1. GINS complex subunit 4, SLD5 [160069]
        1. Human (Homo sapiens) [TaxId: 9606] [160070] (4) picpic
          SQ Q9BRT9 166-223
    4. PSF3 N-terminal domain-like [160071] (1)
      N-terminal part of Pfam 06425
      1. GINS complex subunit 3, PSF3 [160072]
        1. Human (Homo sapiens) [TaxId: 9606] [160073] (7) picpic
          SQ Q9BRX5 1-87

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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