O61125
Gene name |
krsA (krs1, DDB_G0284181) |
Protein name |
Serine/threonine-protein kinase 4 homolog A |
Names |
Kinase responsive to stress A, STE20-like kinase krsA |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0284181 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
156-179 (Activation loop from InterPro)
Target domain |
20-273 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for O61125
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O61125-F1 | Predicted | AlphaFoldDB |
No variants for O61125
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O61125 | |||||
No associated diseases with O61125
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell cortex | The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| aggregation involved in sorocarp development | The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug. |
| hyperosmotic response | 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 detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| protein tetramerization | The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits. |
| regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway | Any process that modulates the frequency, rate or extent of an adenylate cyclase-activating G protein-coupled receptor signaling pathway. |
| regulation of MAPK cascade | Any process that modulates the frequency, rate or extent of signal transduction mediated by the MAP kinase (MAPK) cascade. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTLNVPKET | MSRKDPEKFF | TIVEKLGEGS | YGSVYKAINI | STGIVVAIKK | VSVDNDLEDM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKEISFMKQC | KSPYIVTYYA | SFRKENEVWI | VMEHCGAGSV | CDAMKITDKT | LSEDQIAVVS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDVLQGLAYL | HSVRKIHRDI | KAGNILMNHK | GESKLADFGV | SGQLSDTMAK | RQTVIGTPFW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MAPEVIQEIG | YDYKADIWSY | GITCIEMAES | KPPLFNVHPM | RVIFMIPNPS | RPPPKLTEPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KWSPEFNDFL | AKCLTRKPEL | RPSAEELLKH | PFITKAKSHS | LLVPLIDEQD | IIINEKGREV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALGIEQRDEE | EEDEDEDSED | SDDNRGTMVR | AKPRSMQNSG | GEDNDEEYDT | GTMVITDNKN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SYDTVVFNND | DEDSGTMKLK | NTMPSNKKNF | VPDYMNQFKK | SDDDVTNVPL | SDKYSSYSLE |
| 430 | 440 | 450 | 460 | ||
| ELKKMLAELE | IEREKEVQKT | LEKFSINRQA | LLAVIDEKKS | K |