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:
"Vaccinia Virus protein VP39
".
FunFam 321: Protein arginine N-methyltransferase
Please note: GO 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.
There are 11 GO terms relating to "molecular function"
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.
GO Term | Annotations | Evidence |
---|---|---|
Protein-arginine omega-N monomethyltransferase activity GO:0035241
Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine +
|
3 | P38274 (/IDA) P38274 (/IDA) P46580 (/IDA) |
Protein-arginine omega-N symmetric methyltransferase activity GO:0035243
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues.
|
3 | P38274 (/IDA) P38274 (/IDA) P46580 (/IDA) |
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
2 | P38274 (/IPI) P38274 (/IPI) |
Histone methyltransferase activity GO:0042054
Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.
|
2 | P38274 (/IDA) P38274 (/IDA) |
P53 binding GO:0002039
Interacting selectively and non-covalently with one of the p53 family of proteins.
|
1 | P46580 (/IPI) |
Histone-arginine N-methyltransferase activity GO:0008469
Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine.
|
1 | P46580 (/IDA) |
Protein-arginine N-methyltransferase activity GO:0016274
Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.
|
1 | P46580 (/IDA) |
Protein-arginine N-methyltransferase activity GO:0016274
Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.
|
1 | P46580 (/ISS) |
[myelin basic protein]-arginine N-methyltransferase activity GO:0016277
Catalysis of the reaction: S-adenosyl-L-methionine + (myelin basic protein)-arginine = S-adenosyl-L-homocysteine + (myelin basic protein)-N(omega)-methyl-arginine.
|
1 | P46580 (/IDA) |
Activating transcription factor binding GO:0033613
Interacting selectively and non-covalently with an activating transcription factor, any protein whose activity is required to initiate or upregulate transcription.
|
1 | P46580 (/IPI) |
Histone methyltransferase activity (H4-R3 specific) GO:0044020
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to arginine at position 3 of histone H4.
|
1 | P46580 (/IDA) |
There are 13 GO terms relating to "biological process"
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.
GO Term | Annotations | Evidence |
---|---|---|
G2/M transition of mitotic cell cycle GO:0000086
The mitotic cell cycle transition by which a cell in G2 commits to M phase. The process begins when the kinase activity of M cyclin/CDK complex reaches a threshold high enough for the cell cycle to proceed. This is accomplished by activating a positive feedback loop that results in the accumulation of unphosphorylated and active M cyclin/CDK complex.
|
2 | P38274 (/IMP) P38274 (/IMP) |
Cell morphogenesis GO:0000902
The developmental process in which the size or shape of a cell is generated and organized.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Cellular protein catabolic process GO:0044257
The chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
|
2 | P38274 (/IMP) P38274 (/IMP) |
Positive regulation of mitotic nuclear division GO:0045840
Any process that activates or increases the frequency, rate or extent of mitosis.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Regulation of cell cycle GO:0051726
Any process that modulates the rate or extent of progression through the cell cycle.
|
2 | P38274 (/IMP) P38274 (/IMP) |
Locomotory behavior GO:0007626
The specific movement from place to place of an organism in response to external or internal stimuli. Locomotion of a whole organism in a manner dependent upon some combination of that organism's internal state and external conditions.
|
1 | P46580 (/IMP) |
Intrinsic apoptotic signaling pathway in response to DNA damage GO:0008630
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the detection of DNA damage, and ends when the execution phase of apoptosis is triggered.
|
1 | P46580 (/IMP) |
Peptidyl-arginine methylation, to symmetrical-dimethyl arginine GO:0019918
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N'(omega)-dimethyl-L-arginine.
|
1 | P46580 (/IDA) |
Histone arginine methylation GO:0034969
The modification of a histone by addition of a methyl group to an arginine residue.
|
1 | P46580 (/IDA) |
Peptidyl-arginine N-methylation GO:0035246
The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
|
1 | P46580 (/IDA) |
Negative regulation of DNA damage response, signal transduction by p53 class mediator GO:0043518
Any process that stops, prevents, or reduces the frequency, rate or extent of the cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
|
1 | P46580 (/IGI) |
Negative regulation of transcription, DNA-templated GO:0045892
Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
|
1 | P46580 (/IDA) |
Response to odorant GO:1990834
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an odorant stimulus. An odorant is any substance capable of stimulating the sense of smell.
|
1 | P46580 (/IMP) |
There are 8 GO terms relating to "cellular component"
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.
GO Term | Annotations | Evidence |
---|---|---|
Cellular bud neck septin ring GO:0000144
A ring-shaped structure that forms at the site of cytokinesis in the bud neck of a budding cell; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins. In S. cerevisiae, this structure forms at the time of bud emergence and the septins show a high rate of exchange.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Cellular bud neck septin ring GO:0000144
A ring-shaped structure that forms at the site of cytokinesis in the bud neck of a budding cell; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins. In S. cerevisiae, this structure forms at the time of bud emergence and the septins show a high rate of exchange.
|
2 | P38274 (/IMP) P38274 (/IMP) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | P38274 (/HDA) P38274 (/HDA) |
Outer plaque of spindle pole body GO:0005824
One of three laminate structures that form the spindle pole body; the outer plaque is in the cytoplasm.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Cellular bud neck GO:0005935
The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
|
2 | P38274 (/HDA) P38274 (/HDA) |
Cellular bud neck GO:0005935
The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Cellular bud neck septin collar GO:0032174
A tubular structure with flared ends, shaped like an hourglass and composed of highly ordered arrays of septin filaments, that forms at the bud neck of a dividing cell. In S. cerevisiae, this structure is located at the bud neck throughout most of the cell cycle and the septins are fixed within the structure, not exchanging with soluble septins. This septin structure acts as a scaffold for other proteins that function at the bud neck.
|
2 | P38274 (/IDA) P38274 (/IDA) |
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
1 | P46580 (/IDA) |