Fold: SAM domain-like

4-5 helices; bundle of two orthogonally packed alpha-hairpins; involved in the interactions with DNA and proteins

Lineage:

1. Root: scop
2. Class: All alpha proteins [46456]
3. Fold: SAM domain-like [47768]
   4-5 helices; bundle of two orthogonally packed alpha-hairpins; involved in the interactions with DNA and proteins

Superfamilies:

1. SAM/Pointed domain [47769] (3)
   uperfamily
   1. Pointed domain [47770] (7)
   2. SAM (sterile alpha motif) domain [47773] (16)
   3. Variant SAM domain [158526] (2)
      shares a sequence motif with Pfam 07647, but has a distinct packing of helices
2. RuvA domain 2-like [47781] (7)
   duplication: contains two helix-hairpin-helix (HhH) motifs
   uperfamily
   1. DNA helicase RuvA subunit, middle domain [47782] (3)
   2. Excinuclease UvrC C-terminal domain [81795] (1)
   3. NAD+-dependent DNA ligase, domain 3 [47786] (1)
   4. Topoisomerase V repeat domain [140626] (1)
   5. Hef domain-like [140629] (4)
      helicase/nuclease domain; forms homo and heterodimers; probably includes the Excinuclease UvrC C-terminal domain (scop_fa 81795, that contains a single NMR structure of a monomeric truncated domain, 1kft)
   6. Tex HhH-containing domain-like [158531] (1)
      tandem repeat of two Ruva_2-like domains
   7. ComEA-like [158534] (2)
      sequence similarity to the HhH-motif domains of the PsbU-like and Tex-like families
3. C-terminal domain of RNA polymerase alpha subunit [47789] (1)
   contains one classic and one pseudo HhH motifs
   uperfamily
   1. C-terminal domain of RNA polymerase alpha subunit [47790] (3)
4. Rad51 N-terminal domain-like [47794] (3)
   contains one classic and one pseudo HhH motifs
   uperfamily
   1. DNA repair protein Rad51, N-terminal domain [47795] (4)
   2. NusA extra C-terminal domains [109873] (1)
   3. Hypothetical protein AF1548, C-terminal domain [116936] (1)
5. Barrier-to-autointegration factor, BAF [47798] (1)
   contains one classic and one pseudo HhH motifs
   uperfamily
   1. Barrier-to-autointegration factor, BAF [47799] (1)
6. DNA polymerase beta, N-terminal domain-like [47802] (1)
   contains one classic and one pseudo HhH motifs
   uperfamily
   1. DNA polymerase beta, N-terminal domain-like [47803] (4)
7. PsbU/PolX domain-like [81585] (2)
   contains one classic and one pseudo HhH motifs
   uperfamily
   1. DNA polymerase beta-like, second domain [81584] (4)
      topological similarity to the N-terminal domain
   2. PsbU-like [158539] (1)
      Pfam 06514
8. 5' to 3' exonuclease, C-terminal subdomain [47807] (1)
   uperfamily
   1. 5' to 3' exonuclease, C-terminal subdomain [47808] (8)
9. HRDC-like [47819] (4)
   uperfamily
   1. HRDC domain from helicases [47820] (3)
   2. RNA polymerase II subunit RBP4 (RpoF) [69044] (3)
   3. RNase D C-terminal domains [140643] (1)
      tandem repeat of two domains of this fold, the first domain belongs to Pfam 00570
   4. EXOSC10 HRDC domain-like [140646] (2)
10. lambda integrase-like, N-terminal domain [47823] (1)
    uperfamily
    1. lambda integrase-like, N-terminal domain [47824] (3)
11. Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain [47831] (1)
    uperfamily
    1. Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain [47832] (1)
12. Hypothetical protein YjbJ [69047] (1)
    uperfamily
    1. Hypothetical protein YjbJ [69048] (1)
13. Putative methyltransferase TM0872, insert domain [81799] (1)
    uperfamily
    1. Putative methyltransferase TM0872, insert domain [81800] (2)
14. eIF2alpha middle domain-like [116742] (1)
    uperfamily
    1. eIF2alpha middle domain-like [116743] (3)
15. YozE-like [140652] (1)
    uperfamily
    1. YozE-like [140653] (2)
       Pfam 06855; DUF1250
16. GspK insert domain-like [158544] (1)
    tandem repeat of two SAM-like domains iserted into pilin fold; domain 1 contains one classic HhH motif
    1. GspK insert domain-like [158545] (1)
       middle part of Pfam 03934

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