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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 634733: RPP1 disease resistance protein-like

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
Ribonuclease P. [EC: 3.1.26.5]
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
  • Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
 8 A0A0B2P1Q1 A0A0B2PNV7 A0A0B2PTX1 A0A0B2PTX5 A0A0B2PU82 A0A0B2QST0 A0A0B2S4S0 A0A0B2S619
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 A0A0B2PU93 A0A0B2Q7Z2 A0A0B2QXI6 A0A0B2RHB6 B9RIH0 B9S9E3
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.
 5 A0A078IP99 A0A0D3B1S5 D1GED3 M4CD72 M4CQG3
Sucrose synthase. [EC: 2.4.1.13]
NDP-glucose + D-fructose = NDP + sucrose.
  • Although UDP is generally considered to be the preferred nucleoside diphosphate for sucrose synthase, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose.
  • Sucrose synthase has a dual role in producing both UDP-glucose (necessary for cell wall and glycoprotein biosynthesis) and ADP- glucose (necessary for starch biosynthesis).
 1 A0A072UAS1
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