Fold: all-alpha NTP pyrophosphatases

multihelical: dimeric 4-helical bundle surrounded by other helices; oligomerizes further in a tetramer

Lineage:

1. Root: scop
2. Class: All alpha proteins [46456]
3. Fold: all-alpha NTP pyrophosphatases [101385]
   multihelical: dimeric 4-helical bundle surrounded by other helices; oligomerizes further in a tetramer

Superfamilies:

1. all-alpha NTP pyrophosphatases [101386] (4)
   basic module consist of 5 active site-forming helices; four from one subunit/structural repeat; the fifth from the other subunit/repeat
   uperfamily
   1. MazG-like [116993] (3)
      Pfam 03819
   2. AF0060-like [140794] (1)
      consists of a single member with an orphan sequence; "circular permutation" of putative active site residues: the catalytic lysine resides in the N-terminal helix instead of the missing in this family C-terminal helix; probable biological unit is a tertramer, distinct from the MazG family tetramer
   3. Type II deoxyuridine triphosphatase [101387] (2)
      one subunit comprises two degenerate structural repeats, organised into the "rigid" and "mobile" subdomains
   4. HisE-like (PRA-PH) [140797] (5)
      Pfam 01503

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