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:
"Divalent-metal-dependent TIM barrel enzymes
".
FunFam 23: 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 4 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 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) |
|
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 +
|
2 | P38274 (/IDA) P38274 (/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.
|
2 | P38274 (/IDA) P38274 (/IDA) |
|
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) |
There are 5 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) |
There are 7 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) |
