O57476
Gene name |
CDC37 |
Protein name |
Hsp90 co-chaperone Cdc37 |
Names |
Hsp90 chaperone protein kinase-targeting subunit, p50Cdc37 |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:395430 |
EC number |
|
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 O57476
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O57476-F1 | Predicted | AlphaFoldDB |
No variants for O57476
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O57476 | |||||
No associated diseases with O57476
1 regional properties for O57476
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | YqgF/RNase H-like domain | 4 - 104 | IPR006641 |
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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| unfolded protein binding | Binding to an unfolded protein. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P06101 | CDC37 | Hsp90 co-chaperone Cdc37 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q5EAC6 | CDC37 | Hsp90 co-chaperone Cdc37 | Bos taurus (Bovine) | PR |
| Q24276 | Cdc37 | Hsp90 co-chaperone Cdc37 | Drosophila melanogaster (Fruit fly) | PR |
| Q16543 | CDC37 | Hsp90 co-chaperone Cdc37 | Homo sapiens (Human) | PR |
| Q61081 | Cdc37 | Hsp90 co-chaperone Cdc37 | Mus musculus (Mouse) | PR |
| Q63692 | Cdc37 | Hsp90 co-chaperone Cdc37 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVDYSVWDHI | EVSDDEDETH | PNIDTASLFR | WRHQARVERM | EQFQKEKEEL | DKGCRECKRK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAECQKKLKE | LEVAEPGGGS | GGGRGERERL | QAEAQQLRHE | ERNWESKMEE | LRKKEKNMPW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NVHTLSKDGF | SKSVFNVKAE | EKEETEEQKE | QKHKTFVERH | EKQIKHFGML | RRWDDSQKYL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SDNPHLVCEE | TANYLVIWCI | DLEVEEKQAL | MEQVAHQTIV | MQFILELAKS | LKVDPRACFR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QFFTKIKTAD | QQYMEGFNDE | LEAFKERVRG | RAKARIERAM | REYEEEERQK | RLGPGGLDPV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVYESLPPEL | QKCFDAKDVQ | MLQDTISRMD | PTEAKYHMQR | CIDSGLWVPN | AKAAAEGGGQ |
| 370 | 380 | 390 | |||
| GGAHGQPGGA | DSEALYEEIP | KESGEEEGGE | GKA |