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:
"Phosphoglycerate mutase-like
".
FunFam 9: serine/threonine-protein phosphatase PGAM5, mitoch...
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 16 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 |
---|---|---|
GTPase activator activity GO:0005096
Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
|
15 |
E1BIE7 (/ISS)
F7BWG3 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G5ANV7 (/ISS)
H0XTD8 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
(5 more) |
Phosphatase activity GO:0016791
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
|
15 |
E1BIE7 (/ISS)
F7BWG3 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G5ANV7 (/ISS)
H0XTD8 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
(5 more) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
14 |
B3MR30 (/ISS)
B3P9N0 (/ISS)
B4GXS1 (/ISS)
B4I9J6 (/ISS)
B4JMM7 (/ISS)
B4L6S9 (/ISS)
B4M7S0 (/ISS)
B4NE96 (/ISS)
B4PY69 (/ISS)
B4R313 (/ISS)
(4 more) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
4 | O46084 (/IDA) Q96HS1 (/IDA) Q96HS1 (/IDA) Q96HS1 (/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).
|
4 | O46084 (/IPI) Q96HS1 (/IPI) Q96HS1 (/IPI) Q96HS1 (/IPI) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
3 | Q96HS1 (/TAS) Q96HS1 (/TAS) Q96HS1 (/TAS) |
GTPase activator activity GO:0005096
Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
|
3 | Q96HS1 (/IMP) Q96HS1 (/IMP) Q96HS1 (/IMP) |
Phosphatase activity GO:0016791
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
|
3 | Q96HS1 (/IMP) Q96HS1 (/IMP) Q96HS1 (/IMP) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
3 | Q96HS1 (/IDA) Q96HS1 (/IDA) Q96HS1 (/IDA) |
Phosphoprotein phosphatase activity GO:0004721
Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity.
|
1 | O46084 (/IDA) |
Protein serine/threonine phosphatase activity GO:0004722
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
|
1 | Q8BX10 (/ISO) |
GTPase activator activity GO:0005096
Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
|
1 | Q8BX10 (/ISO) |
Phosphatase activity GO:0016791
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
|
1 | Q8BX10 (/ISO) |
Kinase binding GO:0019900
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
|
1 | O46084 (/IPI) |
Protein serine/threonine kinase activator activity GO:0043539
Binds to and increases the activity of a protein serine/threonine kinase.
|
1 | O46084 (/IDA) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | Q8BX10 (/ISO) |
There are 16 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 |
---|---|---|
Dephosphorylation GO:0016311
The process of removing one or more phosphoric (ester or anhydride) residues from a molecule.
|
15 |
E1BIE7 (/ISS)
F7BWG3 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G5ANV7 (/ISS)
H0XTD8 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
(5 more) |
Positive regulation of GTPase activity GO:0043547
Any process that activates or increases the activity of a GTPase.
|
15 |
E1BIE7 (/ISS)
F7BWG3 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G5ANV7 (/ISS)
H0XTD8 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
(5 more) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
14 |
B3MR30 (/ISS)
B3P9N0 (/ISS)
B4GXS1 (/ISS)
B4I9J6 (/ISS)
B4JMM7 (/ISS)
B4L6S9 (/ISS)
B4M7S0 (/ISS)
B4NE96 (/ISS)
B4PY69 (/ISS)
B4R313 (/ISS)
(4 more) |
Necroptotic process GO:0070266
A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.
|
14 |
E1BIE7 (/ISS)
F7BWG3 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G3RRP2 (/ISS)
G5ANV7 (/ISS)
H0XTD8 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
H9Z621 (/ISS)
(4 more) |
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
5 | G3V9N1 (/ISS) Q562B5 (/ISS) Q96HS1 (/ISS) Q96HS1 (/ISS) Q96HS1 (/ISS) |
Necroptotic process GO:0070266
A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.
|
4 | Q8BX10 (/IMP) Q96HS1 (/IMP) Q96HS1 (/IMP) Q96HS1 (/IMP) |
Macroautophagy GO:0016236
The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded.
|
3 | Q96HS1 (/TAS) Q96HS1 (/TAS) Q96HS1 (/TAS) |
Positive regulation of mitochondrial fission GO:0090141
Any process that increases the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
|
2 | O46084 (/IDA) Q9W173 (/IDA) |
Protein dephosphorylation GO:0006470
The process of removing one or more phosphoric residues from a protein.
|
1 | O46084 (/IDA) |
Response to heat GO:0009408
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 a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
|
1 | O46084 (/IMP) |
Regulation of mitochondrion organization GO:0010821
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a mitochondrion.
|
1 | O46084 (/IGI) |
Regulation of mitochondrion organization GO:0010821
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a mitochondrion.
|
1 | O46084 (/IMP) |
Peptidyl-threonine dephosphorylation GO:0035970
The removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine.
|
1 | O46084 (/IDA) |
Necroptotic process GO:0070266
A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.
|
1 | Q8BX10 (/ISO) |
Response to anesthetic GO:0072347
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 anesthetic stimulus. An anesthetic is a substance that causes loss of feeling, awareness, or sensation.
|
1 | O46084 (/IMP) |
Negative regulation of cold-induced thermogenesis GO:0120163
Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
|
1 | Q8BX10 (/IMP) |
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 |
---|---|---|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
3 | Q96HS1 (/IDA) Q96HS1 (/IDA) Q96HS1 (/IDA) |
Mitochondrial outer membrane GO:0005741
The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
|
3 | Q96HS1 (/TAS) Q96HS1 (/TAS) Q96HS1 (/TAS) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
1 | Q8BX10 (/ISO) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
1 | O46084 (/ISS) |
Integral component of membrane GO:0016021
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | O46084 (/ISM) |