View in Gene3D

CATH Superfamily 3.40.220.10

Leucine Aminopeptidase, subunit E, domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Leucine Aminopeptidase, subunit E, domain 1
".

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 15: Polyprotein P1234

There are 6 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-directed RNA polymerase. [EC: 2.7.7.48]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
  • Can initiate a chain de novo.
  • See also EC 2.7.7.6.
 13 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(3 more...)
Polynucleotide adenylyltransferase. [EC: 2.7.7.19]
ATP + RNA(n) = diphosphate + RNA(n+1).
  • Also acts slowly with CTP.
  • Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time.
  • Cannot initiate a chain de novo.
  • The primer, depending on the source of the enzyme, may be an RNA or DNA fragment or oligo(A) bearing a 3'-OH terminal group.
  • See also EC 2.7.7.6.
 12 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(2 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.
 12 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(2 more...)
ADP-ribose 1''-phosphate phosphatase. [EC: 3.1.3.84]
ADP-D-ribose 1''-phosphate + H(2)O = ADP-D-ribose + phosphate.
  • The enzyme is highly specific for ADP-D-ribose 1''-phosphate.
  • Involved together with EC 3.1.4.37 in the breakdown of adenosine diphosphate ribose 1'',2''-cyclic phosphate (Appr>p), a by-product of tRNA splicing.
  • Formerly EC 3.1.3.n2.
 12 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(2 more...)
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).
 12 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(2 more...)
Polynucleotide 5'-phosphatase. [EC: 3.1.3.33]
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.
  • Does not act on nucleoside monophosphates.
  • Induced in Escherichia coli by T-even phages.
 12 A0A068FNV2 A0A068FNV2 P03317 P27282 P36327 P36328 Q5XXP4 Q87644 Q8JUX6 Q8JUX6
(2 more...)