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 151866: Hybrid sensor histidine kinase

There are 6 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
Histidine kinase. [EC: 2.7.13.3]
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
  • This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine).
  • A number of histones can act as acceptor.
2882 A0A010P9P1 A0A010Q7S1 A0A010QIB5 A0A011MKX1 A0A014NNN1 A0A017I7L0 A0A022PEH6 A0A023BMT1 A0A023E1B5 A0A023RH79
(2872 more...)
Protein-glutamate methylesterase. [EC: 3.1.1.61]
Protein L-glutamate O(5)-methyl ester + H(2)O = protein L-glutamate + methanol.
  • Hydrolyzes the products of EC 2.1.1.77, EC 2.1.1.78, EC 2.1.1.80 and EC 2.1.1.100.
19 A0A073CYB6 A0A0M1JL92 A0A0V7ZN96 A0A1F3Q8I5 A0A1F3Q966 A0A1G0B512 A0A1J1JI93 A0A1J1KG58 A0A1J1KS37 A0A1J1LBK7
(9 more...)
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
4 A0A084G6V4 A0A120F330 A0A120F6N7 M6KAN3
Phosphatidylinositol-4,5-bisphosphate 4-phosphatase. [EC: 3.1.3.78]
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1-phosphatidyl- 1D-myo-inositol 5-phosphate + phosphate.
  • Two pathways exist in mammalian cells to degrade 1-phosphatidyl- 1D-myo-inositol 4,5-bisphosphate (PtdIns(4,5)P(2)).
  • One is catalyzed by this enzyme and the other by EC 3.1.3.36, where the product is PtdIns4P.
  • The enzyme from human is specific for PtdIns(4,5)P(2) as substrate, as it cannot use PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(3,5)P(2), PtdIns5P, PtdIns4P or PtdIns3P.
  • In humans, the enzyme is localized to late endosomal/lysosomal membranes.
  • It can control nuclear levels of PtdIns5P and thereby control p53- dependent apoptosis.
  • Formerly EC 3.1.3.n3.
1 A0A120F330
Cyclic-guanylate-specific phosphodiesterase. [EC: 3.1.4.52]
Cyclic di-3',5'-guanylate + H(2)O = 5'-phosphoguanylyl(3'->5')guanosine.
  • Inhibited by Ca(2+) and Zn(2+).
  • Linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65 and an allosteric activator of EC 2.4.1.12 rendering it inactive.
  • It is the balance between these two enzymes that determines the cellular level of cyclic di-3',5'-guanylate.
1 A0A120F330
Phosphatidylserine decarboxylase. [EC: 4.1.1.65]
Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2).
    1 A9E1I8