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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 17103: Ubiquitin carboxyl-terminal hydrolase 7

There are 16 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.
 31 A0A061I0T2 A0A061IH73 A0A061II77 A0A0C3PM13 A0A0P8Y2K1 A0A0R3NH45 A0A0R3NKZ7 A0A162YHD8 A0A165CCQ5 A0A1E3P9D4
(21 more...)
Deleted entry. [EC: 3.1.2.15]
    		21 B0EFF4 B0EMM7 B6A9H1 B7PN15 B7PV17 B7Q3J7 B9S2Y0 D8LE96 E0VC08 E0VIF8
    (11 more...)
    CCA tRNA nucleotidyltransferase. [EC: 2.7.7.72]
    A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.
    • The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence.
    • The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms.
    • Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition.
    • Formerly EC 2.7.7.21 and EC 2.7.7.25.
    		 1 G0QKQ4
    Bontoxilysin. [EC: 3.4.24.69]
    Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
    • Belongs to peptidase family M27.
    		 1 G0QZS1
    Hydrogen dehydrogenase. [EC: 1.12.1.2]
    H(2) + NAD(+) = H(+) + NADH.
      		 1 G0QZS1
      Exodeoxyribonuclease V. [EC: 3.1.11.5]
      Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.
      • Preference for double-stranded DNA.
      • Possesses DNA-dependent ATPase activity.
      • Acts endonucleolytically on single-stranded circular DNA.
      • Similar enzyme: Haemophilus influenzae ATP-dependent DNase.
      		 1 G0R248
      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 G0QKQ4
      NADH:ubiquinone reductase (H(+)-translocating). [EC: 1.6.5.3]
      NADH + ubiquinone + 5 H(+)(In) = NAD(+) + ubiquinol + 4 H(+)(Out).
      • The complex is present in mitochondria and aerobic bacteria.
      • Breakdown of the complex can release EC 1.6.99.3.
      • In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD(+) to NADH.
      		 1 G0R3M0
      Type I site-specific deoxyribonuclease. [EC: 3.1.21.3]
      Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.
      • Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine.
      • They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence.
      • Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.
      • Formerly EC 3.1.24.1 and EC 3.1.24.2.
      • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
      		 1 G0QYH3
      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).
      		 1 G0QZS1
      Type 1 galactoside alpha-(1,2)-fucosyltransferase. [EC: 2.4.1.69]
      GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D- glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N- acetyl-beta-D-glucosaminyl-R.
      • The enzyme acts on a glycoconjugates where the substituent group is a glycoprotein or glycosphingolipid.
      • The recognized moiety of the substrate is known as a type 1 histo- blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen.
      • The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates (see EC 2.4.1.344).
      • Formerly EC 2.4.1.89.
      		 1 G0QZS1
      Tentoxilysin. [EC: 3.4.24.68]
      Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.
      • Belongs to peptidase family M27.
      		 1 G0QYH3
      3',5'-cyclic-nucleotide phosphodiesterase. [EC: 3.1.4.17]
      Nucleoside 3',5'-cyclic phosphate + H(2)O = nucleoside 5'-phosphate.
      • Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.
      		 1 B0EMM7
      Exodeoxyribonuclease I. [EC: 3.1.11.1]
      Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
      • Preference for single-stranded DNA.
      • The Escherichia coli enzyme hydrolyzes glucosylated DNA.
      • Similar enzymes; mammalian DNase III, exonuclease IV, T2- and T4-induced exodeoxyribonucleases.
      • Formerly EC 3.1.4.25.
      		 1 G0R1Q4
      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.
      		 1 G0QKQ4
      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 G0QZS1
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