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CATH Superfamily 1.25.40.10

Tetratricopeptide repeat 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: waiting to be named.

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 146309: Tetratricopeptide repeat domain-containing protein

There are 7 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
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).
 632 A0A010QEN8 A0A010QEN8 A0A022W318 A0A022W318 A0A022XTH5 A0A022XTH5 A0A024G5D8 A0A024G5D8 A0A024G6Y1 A0A024G6Y1
(622 more...)
RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
  • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
  • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
  • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
  • Formerly EC 6.3.2.19 and EC 6.3.2.21.
 20 A0A0D9RIQ2 A0A0D9RIQ2 G1R9S9 G1R9S9 G3RYV0 G3RYV0 H2NPL2 H2NPL2 H2QA80 H2QA80
(10 more...)
Amidase. [EC: 3.5.1.4]
A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3).
    		 4 B9SIP6 B9SIP6 B9SWW4 B9SWW4
    Dextranase. [EC: 3.2.1.11]
    Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.
      		 2 B0EAL1 B0EAL1
      Triacylglycerol lipase. [EC: 3.1.1.3]
      Triacylglycerol + H(2)O = diacylglycerol + a carboxylate.
      • The pancreatic enzyme acts only on an ester-water interface; the outer ester links are preferentially hydrolyzed.
      		 2 G0QSQ3 G0QSQ3
      Asparaginyl-tRNA synthase (glutamine-hydrolyzing). [EC: 6.3.5.6]
      ATP + L-aspartyl-tRNA(Asn) + L-glutamine + H(2)O = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
      • This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis.
      • In the first step, a non-discriminating ligase (EC 6.1.1.23) mischarges tRNA(Asn) with aspartate, leading to the formation of aspartyl-tRNA(Asn).
      • The aspartyl-tRNA(Asn) is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNA(Asn) (aspartyl- tRNA(Asp) is not a substrate for this reaction).
      • Ammonia or asparagine can substitute for the preferred substrate glutamine.
      		 2 A0A0B2PS89 A0A0B2PS89
      Chorismate mutase. [EC: 5.4.99.5]
      Chorismate = prephenate.
        		 2 B0EAL1 B0EAL1