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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 145579: Pentatricopeptide (PPR) repeat-containing protein-...

There are 9 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
Microtubule-severing ATPase. [EC: 3.6.4.3]
ATP + H(2)O = ADP + phosphate.
  • Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
 111 A0A0B2NQA7 A0A0B2NSG9 A0A0B2NU54 A0A0B2NU81 A0A0B2NUG2 A0A0B2NWU5 A0A0B2NYZ2 A0A0B2P0Z9 A0A0B2P108 A0A0B2P166
(101 more...)
TRNA (guanine(37)-N(1))-methyltransferase. [EC: 2.1.1.228]
S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.
  • This enzyme is important for the maintenance of the correct reading frame during translation.
  • Unlike TrmD from Escherichia coli, which recognizes the G(36)pG(37) motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37.
  • Formerly EC 2.1.1.31.
 10 A0A0D3EP41 A0A0D3EP42 A0A0E0C292 A0A0E0C294 A0A0E0C295 A0A0E0C296 A0A0E0MWP9 A0A0E0MWQ0 A0A0E0MWQ1 A0A0E0MWQ2
Diacylglycerol kinase (ATP). [EC: 2.7.1.107]
ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.
  • Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol.
  • Activity is stimulated by certain phospholipids.
  • In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger.
  • cf. EC 2.7.1.174.
 4 A0A0D9X5T9 A0A0E0I994 I1I2B8 K3YG04
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 3 A0A0D3G0P4 A0A0D9ZR35 A0A0E0PEF6
    UMP/CMP kinase. [EC: 2.7.4.14]
    (1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
    • Formerly EC 2.7.4.5.
    		 2 A0A061FZF0 D7MG22
    Protein disulfide-isomerase. [EC: 5.3.4.1]
    Catalyzes the rearrangement of -S-S- bonds in proteins.
    • Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
    		 2 A0A0E0DEI0 A0A0E0DEI1
    Glucan 1,4-alpha-maltotetraohydrolase. [EC: 3.2.1.60]
    Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
    • Compare EC 3.2.1.2, which removes successive maltose residues, and EC 3.2.1.98 and EC 3.2.1.116.
    		 1 B9R7C6
    Glycerol-3-phosphate dehydrogenase (NAD(+)). [EC: 1.1.1.8]
    sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH.
    • Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
    		 1 F6HC70
    Homoserine dehydrogenase. [EC: 1.1.1.3]
    L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
    • The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).
    • The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
    		 1 M0TNY9