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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 632012: ATP-dependent RNA helicase HrpA

There are 5 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
RNA helicase. [EC: 3.6.4.13]
ATP + H(2)O = ADP + phosphate.
  • RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.
  • Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity.
  • Some helicases unwind DNA as well as RNA.
  • May be identical with EC 3.6.4.12 (DNA helicase).
 398 A0A011NRB0 A0A011PVR9 A0A011PXY7 A0A022PRU4 A0A024HE44 A0A024L2B5 A0A031GW90 A0A060JKG9 A0A061HUE5 A0A062IS46
(388 more...)
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.
 35 A0A085AJD6 A0A085GC56 A0A085GEJ4 A0A085GTK2 A0A085HJU6 A0A085HTH8 A0A085ICW4 A0A085JEJ7 A0A0B2WGN5 A0A0D5Y4V0
(25 more...)
Nuclear-inclusion-a endopeptidase. [EC: 3.4.22.44]
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
  • The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei, protein a of these being the endopeptidase.
  • The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage.
  • It is also reported that transgenic plants expressing the enzyme are resistant to viral infection.
  • Belongs to peptidase family C4.
 5 D2TAR6 D4I372 E5B5G4 F5SXI3 V5Z8P5
Glucose-6-phosphate isomerase. [EC: 5.3.1.9]
D-glucose 6-phosphate = D-fructose 6-phosphate.
  • Also catalyzes the anomerization of D-glucose 6-phosphate.
 1 A0A066Z2E4
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).
 1 M5BAP3