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:

"
Cyclophilin-like
".

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 7135: Peptidyl-prolyl cis-trans isomerase E

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
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.
7548 A0A010Q978 A0A010R2U0 A0A010R6C7 A0A014QY75 A0A015IIJ7 A0A015ISM8 A0A015JQG6 A0A015KCN2 A0A015KVN5 A0A015L138
(7538 more...)
Transaldolase. [EC: 2.2.1.2]
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
    1 A0A081CPC2
    Molybdenum cofactor sulfurtransferase. [EC: 2.8.1.9]
    Molybdenum cofactor + L-cysteine + reduced acceptor + 2 H(+) = thio- molybdenum cofactor + L-alanine + H(2)O + oxidized acceptor.
    • Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide.
    • The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes.
    • In prokaryotes the reaction is catalyzed by two enzymes: EC 2.8.1.7, which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
    1 A0A0W8C5L5
    DNA-directed DNA polymerase. [EC: 2.7.7.7]
    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
    • Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
    • Cannot initiate a chain de novo.
    • Requires a primer which may be DNA or RNA.
    • See also EC 2.7.7.49.
    1 G0QL59