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 47407: Replication factor C 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.
140 A0A060T3P6 A0A060T3P6 A0A074T0B0 A0A074T0B0 A0A074T5P5 A0A074T5P5 A0A074TPD6 A0A074TPD6 A0A081RKN9 A0A081RKN9
(130 more...)
Amino-acid N-acetyltransferase. [EC: 2.3.1.1]
Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
  • Also acts with L-aspartate and, more slowly, with some other amino acids.
8 A0A136J8H6 A0A136J8H6 A0A1J7JIY8 A0A1J7JIY8 G0SGJ3 G0SGJ3 M7SJ62 M7SJ62
Glutamate N-acetyltransferase. [EC: 2.3.1.35]
N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate.
  • Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
8 A0A136J8H6 A0A136J8H6 A0A1J7JIY8 A0A1J7JIY8 G0SGJ3 G0SGJ3 M7SJ62 M7SJ62
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.
6 A0A0L1HXW7 A0A0L1HXW7 A0A0P4UF26 A0A0P4UF26 A0A170VCE8 A0A170VCE8
Diacylglycerol O-acyltransferase. [EC: 2.3.1.20]
Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol.
  • Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
2 B0EMU2 B0EMU2
Acid phosphatase. [EC: 3.1.3.2]
A phosphate monoester + H(2)O = an alcohol + phosphate.
  • Wide specificity.
  • Also catalyzes transphosphorylations.
2 A0A060T9W1 A0A060T9W1
Adenosinetriphosphatase. [EC: 3.6.1.3]
ATP + H(2)O = ADP + phosphate.
  • Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39.
  • The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA.
  • Formerly EC 3.6.1.4.
2 A0A170VCE8 A0A170VCE8
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).
2 A8Y3K6 A8Y3K6