View in Gene3D

CATH Superfamily 3.30.420.10

Ribonuclease H-like superfamily/Ribonuclease H

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:

"
Ribonuclease H-like superfamily/Ribonuclease H
".

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.
« Back to all FunFams

FunFam 45903: DNA polymerase I PolA

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
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.
 3590 A0A009FUN5 A0A009FUN5 A0A009G6M5 A0A009G6M5 A0A009G9H2 A0A009G9H2 A0A009I4I2 A0A009I4I2 A0A009INL3 A0A009INL3
(3580 more...)
Anaerobic carbon-monoxide dehydrogenase. [EC: 1.2.7.4]
CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 H(+).
  • This prokaryotic enzyme catalyzes the reversible reduction of CO(2) to CO.
  • The electrons are transferred to redox proteins such as ferredoxin.
  • In purple sulfur bacteria and methanogenic archaea it catalyzes the oxidation of CO to CO(2), which is incorporated by the Calvin-Benson- Basham cycle or released, respectively.
  • In acetogenic and sulfate-reducing microbes it catalyzes the reduction of CO(2) to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, with which the enzyme forms a tight complex in those organisms.
  • In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2 which catalyze the overall reaction: CO + H(2)O = CO(2) + H(2).
  • Cf. EC 1.2.5.3.
  • Formerly EC 1.2.99.2.
 10 A0A1B3RWH2 A0A1B3RWH2 C0RGI4 C0RGI4 C4IP22 C4IP22 C4WGU1 C4WGU1 M5JRF6 M5JRF6
Exodeoxyribonuclease (lambda-induced). [EC: 3.1.11.3]
Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.
  • Preference for double-stranded DNA.
  • Does not attack single-strand breaks.
  • Similar enzymes: T4, T5 and T7 exonucleases, mammalian DNase IV.
  • Formerly EC 3.1.4.28.
 2 Q3IJF9 Q3IJF9
N-acetylmuramoyl-L-alanine amidase. [EC: 3.5.1.28]
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
  • Formerly EC 3.4.12.5, EC 3.4.17.7 and EC 3.4.19.10.
 2 G8PX52 G8PX52
CATH-Gene3D is a Global Biodata Core Resource Learn more...