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CATH Superfamily 3.30.2010.10

Metalloproteases ("zincins"), catalytic domain

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 named:

"
Metalloproteases ("zincins"), catalytic domain
".

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 4972: CAAX prenyl protease 1

There are 3 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
Ste24 endopeptidase. [EC: 3.4.24.84]
The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
  • One of two enzymes that can catalyze this processing step for mating a-factor in Saccharomyces cerevisiae.
  • Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane- anchor.
  • Belongs to peptidase family M48.
 38 A0A074T2N7 A0A084FVI9 A0A086KSC0 A0A086QPB6 A0A0B2NQL0 A0A0B2R4Y6 A0A0B7FYF1 A0A0F4YUN9 A0A0F8DJW7 A0A0J5PDK0
(28 more...)
H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
  • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
  • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
  • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
  • This movement is driven by the H(+) electrochemical potential gradient.
  • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
  • Formerly EC 3.6.1.34.
 1 A0A099P2Z5
Alpha,alpha-trehalase. [EC: 3.2.1.28]
Alpha,alpha-trehalose + H(2)O = beta-D-glucose + alpha-D-glucose.
  • The enzyme is an anomer-inverting glucosidase that catalyzes the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha- trehalose, releasing initially equimolar amounts of alpha- and beta- D-glucose.
  • It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
 1 A0A0B2VC73
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