P48457
PR
Gene name |
cnaA (AN8820) |
Protein name |
Serine/threonine-protein phosphatase 2B catalytic subunit |
Names |
Calmodulin-dependent calcineurin A subunit |
Species |
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
KEGG Pathway |
ani:AN8820.2 |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
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 P48457
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48457-F1 | Predicted | AlphaFoldDB |
No variants for P48457
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P48457 | |||||
No associated diseases with P48457
1 regional properties for P48457
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphoribulokinase/uridine kinase | 90 - 245 | IPR006083 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| calcineurin complex | A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| mitotic actomyosin contractile ring, intermediate layer | The region of the mitotic actomyosin ring in between the proximal layer and the actin filament layer. This region contains the accessory protein network, some actin filaments and connections between the proximal layer and the actin filament layer. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium-dependent protein serine/threonine phosphatase activity | Catalysis of the reactions: protein serine phosphate + H2O = protein serine + phosphate; and protein threonine phosphate + H2O = protein threonine + phosphate. These reactions require the presence of calcium ions. |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| calmodulin-dependent protein phosphatase activity | Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin. |
| metal ion binding | Binding to a metal ion. |
| myosin phosphatase activity | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| calcineurin-mediated signaling | Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression. |
| cellular response to calcium ion | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus. |
| fungal-type cell wall organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
| G1/S transition of mitotic cell cycle | The mitotic cell cycle transition by which a cell in G1 commits to S phase. The process begins with the build up of G1 cyclin-dependent kinase (G1 CDK), resulting in the activation of transcription of G1 cyclins. The process ends with the positive feedback of the G1 cyclins on the G1 CDK which commits the cell to S phase, in which DNA replication is initiated. |
| negative regulation of calcium ion import across plasma membrane | Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import across plasma membrane. |
| positive regulation of mitotic actomyosin contractile ring contraction | Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring contraction. |
| positive regulation of mitotic division septum assembly | Any process that activates or increases the frequency, rate or extent of mitotic division septum formation. Division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis. |
| regulation of cell morphogenesis | Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDRNLARAVA | DKQPVPEIDF | TLHVMEDGTQ | VSTLERVVKE | VQAPALNKPS | DDQFWDPEEP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TKPNLQFLKQ | HFYREGRLTE | DQALWIIQAG | TQILKSEPNL | LEMDAPITVC | GDVHGQYYDL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MKLFEVGGDP | AETRYLFLGD | YVDRGYFSIE | CVLYLWALKI | WYPNTLWLLR | GNHECRHLTD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YFTFKLECKH | KYSERIYEAC | IESFCALPLA | AVMNKQFLCI | HGGLSPELHT | LEDIKSIDRF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| REPPTHGLMC | DILWADPLED | FGQEKTGDYF | IHNSVRGCSY | FFSYPAACAF | LEKNNLLSVI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RAHEAQDAGY | RMYRKTRTTG | FPSVMTIFSA | PNYLDVYNNK | AAVLKYENNV | MNIRQFNCTP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HPYWLPNFMD | VFTWSLPFVG | EKITDMLIAI | LNTCSKEELE | DETPSTISPA | EPSPPMPMDT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VDTESTEFKR | RAIKNKILAI | GRLSRVFQVL | REESERVTEL | KTAAGGRLPA | GTLMLGAEGI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KQAITNFEDA | RKVDLQNERL | PPSHDEVVRR | SEEERRIALD | RAQHEADNDT | GLATVARRIS |
| MKIPSTTRR |