Q4WUR1
Gene name |
cnaA (AFUA_5G09360) |
Protein name |
Serine/threonine-protein phosphatase 2B catalytic subunit |
Names |
Calmodulin-dependent calcineurin A subunit |
Species |
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
KEGG Pathway |
afm:AFUA_5G09360 |
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
3 structures for Q4WUR1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6TZ7 | X-ray | 250 A | A | 2-370 | PDB |
| 7U0U | X-ray | 190 A | A | 335-370 | PDB |
| AF-Q4WUR1-F1 | Predicted | AlphaFoldDB |
No variants for Q4WUR1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4WUR1 | |||||
No associated diseases with Q4WUR1
1 regional properties for Q4WUR1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphoribulokinase/uridine kinase | 90 - 244 | 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 | |
2 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
2 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. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEDGTQVSTL | ERVIKEVQAP | ALSTPTDEMF | WSPEDPSKPN | LQFLKQHFYR | EGRLTEEQAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WIIHAGTQIL | RSEPNLLEMD | APITVCGDVH | GQYYDLMKLF | EVGGDPSETR | YLFLGDYVDR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GYFSIECVLY | LWALKIWYPN | SLWLLRGNHE | CRHLTDYFTF | KLECKHKYSE | RIYEACIESF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CALPLAAVMN | KQFLCIHGGL | SPELHTLEDI | KSIDRFREPP | THGLMCDILW | ADPLEEFGQE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KTGDYFVHNS | VRGCSYFFSY | PAACAFLEKN | NLLSIIRAHE | AQDAGYRMYR | KTRTTGFPSV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MTIFSAPNYL | DVYNNKAAVL | KYENNVMNIR | QFNCTPHPYW | LPNFMDVFTW | SLPFVGEKIT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DMLIAILNTC | SKEELEDETP | TSVSPSAPSP | PLPMDVESSE | FKRRAIKNKI | LAIGRLSRVF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QVLREESERV | TELKTAAGGR | LPAGTLMLGA | EGIKQAITNF | EDARKVDLQN | ERLPPSHEEV |
| 490 | 500 | 510 | 520 | 530 | |
| IKRSEEERRA | ALERAQQEAD | NDTGLATVAR | RISMSAGSGR | SRRQRDAARE | TREA |