CATH Classification

Domain Context

CATH Clusters

Superfamily Leucine Aminopeptidase, subunit E, domain 1
Functional Family Polyprotein P1234

Enzyme Information

3.1.3.84
ADP-ribose 1''-phosphate phosphatase.
based on mapping to UniProt Q8QZ73
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.
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt Q8QZ73
2.7.7.19
Polynucleotide adenylyltransferase.
based on mapping to UniProt Q8QZ73
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.
2.1.1.-
Methyltransferases.
based on mapping to UniProt Q8QZ73
3.6.4.13
RNA helicase.
based on mapping to UniProt Q8QZ73
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).
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt Q8QZ73
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.
3.1.3.33
Polynucleotide 5'-phosphatase.
based on mapping to UniProt Q8QZ73
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.
-!- Does not act on nucleoside monophosphates. -!- Induced in Escherichia coli by T-even phages.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt Q8QZ73
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.
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt Q8QZ73

UniProtKB Entries (1)

Q8QZ73
POLN_MAYAB
Mayaro virus (strain Brazil)
Polyprotein P1234

PDB Structure

PDB 5IQ5
External Links
Method SOLUTION NMR
Organism
Primary Citation
Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain.
Tsika, A.C., Melekis, E., Tsatsouli, S.A., Papageorgiou, N., Mate, M.J., Canard, B., Coutard, B., Bentrop, D., Spyroulias, G.A.
J.Mol.Biol.