Q09637
Gene name |
cyn-9 (cyp-9, T27D1.1) |
Protein name |
Peptidyl-prolyl cis-trans isomerase 9 |
Names |
PPIase 9, Cyclophilin-9, Rotamase 9 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_T27D1.1 |
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 Q09637
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q09637-F1 | Predicted | AlphaFoldDB |
No variants for Q09637
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q09637 | |||||
No associated diseases with Q09637
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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cyclosporin A binding | Binding to cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids. |
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| extracellular matrix organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein peptidyl-prolyl isomerization | The modification of a protein by cis-trans isomerization of a proline residue. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAEKRVFLD | ISVDENLIGR | IEIRLFVEDA | PKTCENFRAL | CTGEVGMTPN | NKARLHYKQN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EFHRIVKKFM | IQGGDITEGD | GRGGFSIYGR | YFDDEKFKLK | HSRPYLLSMA | NKGPNSNSSQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FFITTAAAPH | CNGKHVVFGE | VVKGQNVVDY | IDNLAVDDKS | KPLAKVLISN | CGELVKKKKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKTDEELAAA | LEEKNNNARD | NEIPKCPKSW | LYRDDDNEKK | HEMRNDKRRE | YRSRRSRSRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HEKNRDYKKE | NRGDSSRSQP | RRDENGITVR | GRGGVRFRRE | RSATPEHWRR | NAPTKWVHDS |
| HKHPEEDLV |