CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.1.1.-
Methyltransferases.
based on mapping to UniProt P03317
3.1.3.84
ADP-ribose 1''-phosphate phosphatase.
based on mapping to UniProt P03317
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt P03317
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).
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P03317
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.
3.1.3.33
Polynucleotide 5'-phosphatase.
based on mapping to UniProt P03317
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.
-!- Does not act on nucleoside monophosphates. -!- Induced in Escherichia coli by T-even phages.
2.7.7.19
Polynucleotide adenylyltransferase.
based on mapping to UniProt P03317
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P03317
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.
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt P03317
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P03317

UniProtKB Entries (1)

P03317
POLN_SINDV
Sindbis virus
Polyprotein P1234

PDB Structure

PDB 4GUA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural and functional insights into alphavirus polyprotein processing and pathogenesis.
Shin, G., Yost, S.A., Miller, M.T., Elrod, E.J., Grakoui, A., Marcotrigiano, J.
Proc.Natl.Acad.Sci.USA