Q6CKF0
Gene name |
RRD2 (KLLA0F11187g) |
Protein name |
Serine/threonine-protein phosphatase 2A activator 2 |
Names |
Peptidyl-prolyl cis-trans isomerase PTPA-2, PPIase PTPA-2, Rotamase PTPA-2, Phosphotyrosyl phosphatase activator 2 |
Species |
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) |
KEGG Pathway |
kla:KLLA0_F11187g |
EC number |
5.2.1.8: Cis-trans isomerases |
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 Q6CKF0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6CKF0-F1 | Predicted | AlphaFoldDB |
No variants for Q6CKF0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6CKF0 | |||||
No associated diseases with Q6CKF0
No regional properties for Q6CKF0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q6CKF0 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| 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. |
| protein phosphatase type 2A complex | A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
| phosphatase activator activity | Binds to and increases the activity of a phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a substrate molecule. |
| protein phosphatase regulator activity | Binds to and modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| mitotic spindle organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. |
| response to osmotic stress | 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 a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAIKRLINEH | DMELWNNSKT | FEDVIGFINT | LALSVRGREN | NDYTQPISDN | VQRVSNLLSK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VTEIIGKHEV | IKDANTSRFG | KIEFRDFYDD | ISEHSNELIS | KIFEGIEKPD | TGKLDDICTY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FINSWGDRSR | IDYGSGHELN | FICFLYCLTE | SKVFDLENDS | SNIVLMLFIK | YLGIMRSLEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KYWLEPAGSH | GVWGLDDYHF | LPFLFGAFQL | STHKHLKPKS | IHNPEVVEMF | QDRYLYFGCI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AFINKVKTTA | SLRWHSPMLD | DISGVKRWSK | VAEGMVKMYK | AEVLQKLPIM | QHFYFGYFLK |
| 310 | 320 | 330 | 340 | 350 | |
| CPEGVSEPSA | RAQDHHEDDS | CCTDGSHGHS | TWADCCGIAV | PSAIAASQMA | NKDVRLFPFD |