A8XJQ6
Gene name |
CBG14305 |
Protein name |
cAMP-dependent protein kinase, catalytic subunit-like |
Names |
|
Species |
Caenorhabditis briggsae |
KEGG Pathway |
|
EC number |
2.7.11.11: 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
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A8XJQ6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8XJQ6-F1 | Predicted | AlphaFoldDB |
No variants for A8XJQ6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8XJQ6 | |||||
No associated diseases with A8XJQ6
5 regional properties for A8XJQ6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TolB, N-terminal | 22 - 128 | IPR007195 |
| repeat | WD40-like beta propeller | 242 - 271 | IPR011659-1 |
| repeat | WD40-like beta propeller | 282 - 316 | IPR011659-2 |
| repeat | WD40-like beta propeller | 325 - 349 | IPR011659-3 |
| repeat | WD40-like beta propeller | 376 - 400 | IPR011659-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.11 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cAMP-dependent protein kinase complex | An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| AMP-activated protein kinase activity | Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of AMP. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| cAMP-dependent protein kinase activity | cAMP-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
| 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 |
| MSSSTSSVES | VEDESCSNEC | SASFTFDTNN | NSRGDQQVDE | LAEETHMKLS | ITPTRESFSL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SQLERIVTIG | KGTFGRVELA | RDKISGAHYA | LKVLNIRRVV | DMRQTQHVHN | EKRVLLQLKH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PFIVKMYASE | KDSNNLYMIM | EFVPGGEMFS | YLRASRSFSN | SMARFYASEI | VCALEYIHSL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GIVYRDLKPE | NLMLSKEGHI | KMADFGFAKE | LRDRTYTICG | TPDYLAPESL | ARTGHNKGVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WWALGILIYE | MMVGKPPFRG | KTTAEIYDSI | IEHKLKFPRS | FNLAAKDLVK | KLLEVDRTQR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGCMKNGTQD | VKDHKWFEKV | NWDDTLHLRV | EVKKLIGIFL | IPIFQPPIVP | TLYHPGDTGN |
| 370 | 380 | ||||
| FDDYEEDTTG | GPLCSQRERD | LFAEW |