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CATH Superfamily 3.90.70.10

Cysteine proteinases

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:

"
Cysteine proteinases
".

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 17160: Ubiquitin carboxyl-terminal hydrolase 14

There are 8 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
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.
 2540 A0A010Q809 A0A010Q809 A0A014QSP3 A0A014QSP3 A0A015JTT8 A0A015JTT8 A0A015LDW5 A0A015LDW5 A0A016SLD3 A0A016SLD3
(2530 more...)
Deleted entry. [EC: 3.1.2.15]
    		88 A0A074T3S9 A0A074T3S9 A0A086K9M3 A0A086K9M3 A0A086KJ55 A0A086KJ55 A0A086LGX2 A0A086LGX2 A0A086MAG0 A0A086MAG0
    (78 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).
    		 6 B6AFW9 B6AFW9 G0QKR6 G0QKR6 L0B3B2 L0B3B2
    Poly(A)-specific ribonuclease. [EC: 3.1.13.4]
    Exonucleolytic cleavage of poly(A) to 5'-AMP.
    • Cleaves poly(A) in either the single- or double-stranded form.
    		 2 A0A0F8D2H7 A0A0F8D2H7
    TRNA-guanine(34) transglycosylase. [EC: 2.4.2.29]
    (1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine.
    • Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34.
    • In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine.
    • In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine.
    • The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn).
    • This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway.
    		 2 A3GFE2 A3GFE2
    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.
    		 2 A0A061IHR2 A0A061IHR2
    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.
    		 2 A0A182IY54 A0A182IY54
    DNA-directed RNA polymerase. [EC: 2.7.7.6]
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
    • Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
    • Can initiate a chain de novo.
    • In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
    • See also EC 2.7.7.19 and EC 2.7.7.48.
    		 2 G0R343 G0R343
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