CATH Superfamily 1.20.120.1630
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: waiting to be named.
FunFam 18: Protein-S-isoprenylcysteine O-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 3 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 C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity GO:0004671
Catalysis of the reaction: S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.
|
3 | P32584 (/IMP) P32584 (/IMP) P87014 (/IMP) |
Protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity GO:0004671
Catalysis of the reaction: S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.
|
2 | P32584 (/IDA) P32584 (/IDA) |
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
|
1 | Q5LPJ6 (/ISS) |
There are 3 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 |
---|---|---|
C-terminal protein methylation GO:0006481
The methylation of the C-terminal amino acid of a protein.
|
2 | P32584 (/IMP) P32584 (/IMP) |
Peptide pheromone maturation GO:0007323
The generation of a mature, active peptide pheromone via processes unique to its processing and modification. An example of this process is found in Saccharomyces cerevisiae.
|
2 | P32584 (/IMP) P32584 (/IMP) |
Peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion GO:0071432
The formation of a mature peptide mating pheromone by proteolysis and/or modification of a peptide precursor, occurring in the context of conjugation with cellular fusion.
|
1 | P87014 (/IMP) |
There are 4 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 |
---|---|---|
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
3 | P32584 (/HDA) P32584 (/HDA) P87014 (/HDA) |
Nuclear inner membrane GO:0005637
The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
|
2 | P32584 (/IMP) P32584 (/IMP) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
2 | P32584 (/IDA) P32584 (/IDA) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P87014 (/ISO) |