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CATH Superfamily 1.10.287.560

Histidine kinase CheA-like, homodimeric 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:

"
Histidine kinase CheA-like, homodimeric 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 1015: CheA signal transduction histidine kinase

There are 2 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.
 450 A0A017IEH0 A0A022PNG4 A0A023YYN7 A0A024KXS7 A0A025CR60 A0A026UX01 A0A027TSP7 A0A028ATQ9 A0A028E3Q6 A0A029HX94
(440 more...)
Peptidylprolyl isomerase. [EC: 5.2.1.8]
Peptidylproline (omega=180) = peptidylproline (omega=0).
  • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
  • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
  • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
 1 A0A0B2WGA3