Structural Classification of Proteins




Fold: P-loop containing nucleotide triphosphate hydrolases
- 3 layers: a/b/a, parallel or mixed beta-sheets of variable sizes
Lineage:
- Root: scop
- Class: Alpha and beta proteins (a/b)
Mainly parallel beta sheets (beta-alpha-beta units)
- Fold: P-loop containing nucleotide triphosphate hydrolases
3 layers: a/b/a, parallel or mixed beta-sheets of variable sizes
Superfamilies:
- P-loop containing nucleotide triphosphate hydrolases (14)
division into families based on beta-sheet topologies
- Nucleotide and nucleoside kinases (16)


parallel beta-sheet of 5 strands, order 23145
- Shikimate kinase (1)

similar to the nucleotide/nucleoside kinases but acts on different substrate
- Chloramphenicol phosphotransferase (1)

similar to the nucleotide/nucleoside kinases but acts on different substrate
- Adenosine-5'phosphosulfate kinase (APS kinase) (1)

- PAPS sulfotransferase (4)

similar to the nucleotide/nucleoside kinases but transfer sulphate group
- Phosphoribulokinase/pantothenate kinase (2)

- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain (1)

- G proteins (28)


core: mixed beta-sheet of 6 strands, order 231456; strand 2 is antiparallel to the rest
- Motor proteins (7)

- Nitrogenase iron protein-like (10)

core: parallel beta-sheet of 7 strands; order 3241567
- RecA protein-like (ATPase-domain) (9)


core: mixed beta-sheet of 8 strands, order 32451678; strand 7 is antiparallel to the rest
- ABC transporter ATPase domain-like (7)

there are two additional subdomains inserted into the central core that has a RecA-like topology
- Extended AAA-ATPase domain (13)

fold is similar to that of RecA, but lacks the last two strands, followed by a family-specific all-alpha Arg-finger domain
- RNA helicase (1)

duplication: consists of two similar domains, one binds NTP and the other binds RNA; also contains an all-alpha subdomain in the C-terminal extension
Generated from scop database 1.55 with scopm 1.095 on Mon Jul 9 18:35:50 2001
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© 1994-2001 The scop authors /
scop@mrc-lmb.cam.ac.uk