CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.10 | Thrombin, subunit H | |
2.40.10.120 |
Domain Context
CATH Clusters
Superfamily | 2.40.10.120 |
Functional Family |
Enzyme Information
2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P17763
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.
|
3.4.21.91 |
Flavivirin.
based on mapping to UniProt P17763
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
|
3.6.1.15 |
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P17763
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.
|
3.6.4.13 |
RNA helicase.
based on mapping to UniProt P17763
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).
|
2.1.1.57 |
Methyltransferase cap1.
based on mapping to UniProt P17763
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)- (purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- [mRNA].
-!- This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine. -!- This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. -!- The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine. -!- Formerly EC 2.1.1.58.
|
2.1.1.56 |
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt P17763
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
-!- Adds an N(7)-methylguanine cap to mRNA. -!- The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
|
2.1.1.57 |
Methyltransferase cap1.
based on mapping to UniProt P33478
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)- (purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)- methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)- [mRNA].
-!- This enzyme catalyzes the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine. -!- This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. -!- The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine. -!- Formerly EC 2.1.1.58.
|
2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P33478
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.
|
2.1.1.56 |
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt P33478
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
-!- Adds an N(7)-methylguanine cap to mRNA. -!- The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
|
3.4.21.91 |
Flavivirin.
based on mapping to UniProt P33478
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
|
3.6.4.13 |
RNA helicase.
based on mapping to UniProt P33478
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 P33478
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.
|
UniProtKB Entries (2)
P17763 |
POLG_DEN1W
Dengue virus 1 Nauru/West Pac/1974
Genome polyprotein
|
P33478 |
POLG_DEN1S
Dengue virus 1 Singapore/S275/1990
Genome polyprotein
|
PDB Structure
PDB | 3LKW |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family.
J.Virol.
|