CATH Superfamily 2.30.29.30
Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
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:
"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
".
FunFam 449: Histone-arginine methyltransferase CARMER
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 7 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 +
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
Protein-arginine omega-N asymmetric methyltransferase activity GO:0035242
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
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.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
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.
|
2 | Q9VH48 (/ISS) Q9VH48 (/ISS) |
|
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 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
|
Protein-arginine omega-N asymmetric methyltransferase activity GO:0035242
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.
|
2 | Q9VH48 (/IDA) Q9VH48 (/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 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
There are 6 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 |
|---|---|---|
|
Histone arginine methylation GO:0034969
The modification of a histone by addition of a methyl group to an arginine residue.
|
15 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(5 more) |
|
Chromatin remodeling GO:0006338
Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
Regulation of transcription, DNA-templated GO:0006355
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
Peptidyl-arginine methylation, to asymmetrical-dimethyl arginine GO:0019919
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
Histone methylation GO:0016571
The modification of histones by addition of methyl groups.
|
2 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
|
Peptidyl-arginine methylation, to asymmetrical-dimethyl arginine GO:0019919
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
|
2 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
There are 5 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 |
|---|---|---|
|
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.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
13 |
B3M1E1 (/ISS)
B3P4N5 (/ISS)
B4GZ20 (/ISS)
B4GZ20 (/ISS)
B4HJC0 (/ISS)
B4JXV2 (/ISS)
B4KA23 (/ISS)
B4LVS8 (/ISS)
B4NKI9 (/ISS)
B4PVH6 (/ISS)
(3 more) |
|
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.
|
2 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
|
Histone methyltransferase complex GO:0035097
A multimeric complex that is able to catalyze the addition of methyl groups to histone proteins.
|
2 | Q9VH48 (/IDA) Q9VH48 (/IDA) |
