Q9NJU9
Gene name |
CDPK3 |
Protein name |
Calcium-dependent protein kinase 3 |
Names |
PfCDPK3 |
Species |
Plasmodium falciparum (isolate 3D7) |
KEGG Pathway |
pfa:PF3D7_0310100 |
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
277-281 (Activation loop from InterPro)
Target domain |
118-373 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
258-266 (Activation loop from InterPro)
Target domain |
118-373 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
2 structures for Q9NJU9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3K21 | X-ray | 115 A | A | 388-560 | PDB |
| AF-Q9NJU9-F1 | Predicted | AlphaFoldDB |
No variants for Q9NJU9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9NJU9 | |||||
No associated diseases with Q9NJU9
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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent protein serine/threonine kinase activity | Calcium-dependent catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| calmodulin-dependent protein kinase activity | Calmodulin-dependent catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cell differentiation | The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. |
| 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. |
| peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNDLIIKNNK | KGSCDVIIKY | KCKKSDENIK | RRKSSHKYIK | NKSVVLGRSI | MTNKKEKLKG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALKYKGSKKE | IKICNKKSMI | KNDKDENTTL | KSMKSDNFKF | SRRGFILSFT | GNLEDFYNLS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KEPLGKGTYG | CVYKATDKLL | KISRAVKVVS | KKKLKNIPRF | RQEIDIMKNL | DHPNVVKLLE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TFEDSNQIYL | VMELCTGGEL | FDKIVKKGCF | VETFASFIMK | QIFSVLNYLH | IRNICHRDIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PENFLFYDMT | PESLIKIIDF | GLASYFTHNN | YEMKTKAGTP | YYVAPQVLTG | SYNYKCDMWS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SGVLFYILLC | GYPPFFGESD | HEILSMVKKG | KYQFKGKEWN | NISEEAKDLI | KRCLTMDADK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RICASEALQH | PWFKKKKYAF | NMDMKMDIHV | LENFKNYGLL | LKFQKLAMTI | IAQQSNDYDV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EKLKSTFLVL | DEDGKGYITK | EQLKKGLEKD | GLKLPYNFDL | LLDQIDSDGS | GKIDYTEFIA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AALDRKQLSK | KLIYCAFRVF | DVDNDGEITT | AELAHILYNG | NKKGNITQRD | VNRVKRMIRD |
| 550 | 560 | ||||
| VDKNNDGKID | FHEFSEMMKL | KF |