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CATH Superfamily 1.25.10.10

Leucine-rich Repeat Variant

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:

"
Leucine-rich Repeat Variant
".

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 69983: V-type proton ATPase subunit H

There are 4 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
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.
 37 A0A024WL76 A0A060S259 A0A0B2SJM2 A0A0J9R3A5 A0A0J9R497 A0A0J9TPK3 A0A0N8NZJ1 A0A0P8XHX6 A0A0P8XY88 A0A0Q5VN59
(27 more...)
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.
 1 A0A161M902
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.
 1 A0A161M902
Proton-exporting ATPase. [EC: 3.6.3.6]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • Generates an electrochemical potential gradient of protons across the plasma membrane.
  • Formerly EC 3.6.1.35.
 1 Q8GUB3