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CATH Superfamily 1.20.900.10

Dbl homology (DH) 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:

"
Dbl homology (DH) 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 3378: Guanine nucleotide exchange factor DBS

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
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 46 A2CG49 A2CG49 A2CG49 A2CG49 A8DYP0 A8DYP0 B7PZE7 B7PZE7 B7Q4C1 B7Q4C1
(36 more...)
Protein-tyrosine-phosphatase. [EC: 3.1.3.48]
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
  • Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
 8 B7PZE7 B7PZE7 B7Q4C1 B7Q4C1 E0VF59 E0VF59 E0VF59 E0VF59
Phospholipid-translocating ATPase. [EC: 3.6.3.1]
ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other.
  • Formerly EC 3.6.3.13.
 4 A0A061IQ20 A0A061IQ20 A0A061IR14 A0A061IR14
Orotidine-5'-phosphate decarboxylase. [EC: 4.1.1.23]
Orotidine 5'-phosphate = UMP + CO(2).
  • The enzyme from higher eukaryotes is identical with EC 2.4.2.10.
 4 V8P932 V8P932 V8P932 V8P932
Ubiquitinyl hydrolase 1. [EC: 3.4.19.12]
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
  • Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides.
  • Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals.
  • Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde).
  • Belongs to peptidase family C12.
 4 A0A1B0FM68 A0A1B0FM68 A0A1B0FM68 A0A1B0FM68
Protein kinase C. [EC: 2.7.11.13]
ATP + a protein = ADP + a phosphoprotein.
  • A family of serine- and threonine-specific protein kinases that depend on lipids for activity.
  • They can be activated by calcium but have a requirement for the second messenger diacylglycerol.
  • Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell- signaling pathways.
  • Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters.
  • Formerly EC 2.7.1.37.
 2 B7QJT0 B7QJT0