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CATH Superfamily 1.10.8.60

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 46850: 26S protease regulatory subunit 7

There are 7 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Proteasome ATPase. [EC: 3.6.4.8]
ATP + H(2)O = ADP + phosphate.
  • Belongs to the AAA-type superfamily and, like EC 3.6.4.5, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome.
  • Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
 50 A0A024V2T0 A0A024V2T0 A0A024VYV2 A0A024VYV2 A0A024WMP1 A0A024WMP1 A0A024X2U0 A0A024X2U0 A0A060S211 A0A060S211
(40 more...)
Proteasome endopeptidase complex. [EC: 3.4.25.1]
Cleavage of peptide bonds with very broad specificity.
  • A 20-S protein composed of 28 subunits arranged in four rings of seven.
  • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
  • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
  • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
  • Terminal apertures restrict access of substrates to the active sites.
  • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
  • Belongs to peptidase family T1.
  • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
 20 A0A100IRG2 A0A100IRG2 A0A146FEC2 A0A146FEC2 A0A1L9N9E0 A0A1L9N9E0 A0A1L9UVK0 A0A1L9UVK0 A0A1M3TR60 A0A1M3TR60
(10 more...)
Microtubule-severing ATPase. [EC: 3.6.4.3]
ATP + H(2)O = ADP + phosphate.
  • Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
 14 A0A0D2MKU1 A0A0D2MKU1 B0EPQ3 B0EPQ3 B9RR13 B9RR13 B9T505 B9T505 E0W1J4 E0W1J4
(4 more...)
Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
NTP + H(2)O = NDP + phosphate.
  • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
  • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
  • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
 6 A0A060TBW7 A0A060TBW7 A0A0L1HJA9 A0A0L1HJA9 A0A0P4U2U6 A0A0P4U2U6
Adenosinetriphosphatase. [EC: 3.6.1.3]
ATP + H(2)O = ADP + phosphate.
  • Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39.
  • The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA.
  • Formerly EC 3.6.1.4.
 6 A0A0J9TVH6 A0A0J9TVH6 L7JUS1 L7JUS1 Q7KMQ0 Q7KMQ0
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
 6 A0A0E9NPU4 A0A0E9NPU4 A0A0G2EH26 A0A0G2EH26 A0A179U5S9 A0A179U5S9
Vesicle-fusing ATPase. [EC: 3.6.4.6]
ATP + H(2)O = ADP + phosphate.
  • A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments.
  • They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily.
  • They include peroxin, which apparently is involved in Zellweger's syndrome.
 2 B0EMS1 B0EMS1