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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 633769: Replication factor C large subunit

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
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.
 5 A0A081S852 A0A087RV57 A0A087S0X6 A0A087S8S2 A0A1M4MJJ1
DNA ligase (NAD(+)). [EC: 6.5.1.2]
NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
  • The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
  • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue.
  • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
  • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
  • RNA can also act as substrate, to some extent.
  • Cf. EC 6.5.1.1, EC 6.5.1.6, and EC 6.5.1.7.
 4 B0EMT0 B7P7N8 E0VKP6 L1LDP1
DNA helicase. [EC: 3.6.4.12]
ATP + H(2)O = ADP + phosphate.
  • DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
  • Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15).
  • Some helicases unwind DNA as well as RNA (4,9).
  • May be identical with EC 3.6.4.13 (RNA helicase).
 3 A0A081S852 A0A087RNM5 A0A087S0X6
Aspartate transaminase. [EC: 2.6.1.1]
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
  • Also acts on L-tyrosine, L-phenylalanine and L-tryptophan.
  • This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
 1 F0XTY5
Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
NTP + H(2)O = NDP + phosphate.
  • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
  • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
  • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
 1 A0A060T2G1
Endopeptidase La. [EC: 3.4.21.53]
Hydrolysis of proteins in presence of ATP.
  • ATP hydrolysis is linked with peptide bond hydrolysis.
  • Vanadate inhibits both reactions.
  • A similar enzyme occurs in animal mitochondria.
  • Belongs to peptidase family S16.
 1 B0EMT0
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.
 1 G0QSZ6
Mitochondrial processing peptidase. [EC: 3.4.24.64]
Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
  • Known from the mitochondrial matrix of fungi and mammals.
  • Belongs to peptidase family M16.
  • Formerly EC 3.4.99.41.
 1 G0QSZ6