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CATH Superfamily 2.60.120.10

Jelly Rolls

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:

"
Jelly Rolls
".

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 54809: Cyclic nucleotide-gated cation channel

There are 5 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
CGMP-dependent protein kinase. [EC: 2.7.11.12]
ATP + a protein = ADP + a phosphoprotein.
  • cGMP is required to activate this enzyme.
  • The enzyme occurs as a dimer in higher eukaryotes.
  • The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites.
  • This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates.
  • The enzyme also has two allosteric cGMP-binding sites (sites A and B).
  • Binding of cGMP causes a conformational change that is associated with activation of the kinase.
  • Formerly EC 2.7.1.37.
 12 B7PAP2 B7PAP2 B7PEZ1 B7PEZ1 B7PGV9 B7PGV9 B7PWJ7 B7PWJ7 B7QCN0 B7QCN0
(2 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.
 8 A0A182FTD7 A0A182FTD7 A0A182MGT8 A0A182MGT8 A0A182MXW2 A0A182MXW2 A0A182Q1X1 A0A182Q1X1
Glucose-6-phosphate dehydrogenase (NADP(+)). [EC: 1.1.1.49]
D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH.
  • The enzyme catalyzes a step of the pentose phosphate pathway.
  • The enzyme is specific for NADP(+), cf. EC 1.1.1.363 and EC 1.1.1.388.
 6 A0A177PZK9 A0A177PZK9 A0A1J4YDM2 A0A1J4YDM2 Q0F2T2 Q0F2T2
Lysophospholipase. [EC: 3.1.1.5]
2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate.
    		 4 B9T5D2 B9T5D2 B9T5G2 B9T5G2
    Non-specific protein-tyrosine kinase. [EC: 2.7.10.2]
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
    • Unlike EC 2.7.10.1, this protein-tyrosine kinase does not have a transmembrane domain.
    • In the human genome, 32 non-specific protein-tyrosine kinases have been identified and these can be divided into 10 families.
    • Formerly EC 2.7.1.112.
    		 2 B7PEW9 B7PEW9
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