Q75B89
Gene name |
FES1 (ADL319W) |
Protein name |
Hsp70 nucleotide exchange factor FES1 |
Names |
|
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_ADL319W |
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 Q75B89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q75B89-F1 | Predicted | AlphaFoldDB |
No variants for Q75B89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q75B89 | |||||
No associated diseases with Q75B89
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| adenyl-nucleotide exchange factor activity | Binds to and stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cytoplasm protein quality control by the ubiquitin-proteasome system | The chemical reactions and pathways resulting in the breakdown of misfolded proteins in the cytoplasm, which are targeted to cytoplasmic proteasomes for degradation. |
| regulation of translation | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDKLLHWSIA | NAQGDKEAAA | KAGAPDPKLL | QQLFGGGPDE | PALMRDAMAV | IMNPEATVDN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLVAFDNFEM | LIENLDNANN | IENMRLWAPL | ISILESEEEQ | LRECALSVVG | TAVQNNEKSQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SNFLKHDGAM | KKIIELARKD | SESEQVRTKA | FYALSNIVRH | NKDASALFVD | NGGLEIMAPV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKHQNTGEKM | KIRALALLTS | VLTSLSADEK | FSDRIREDKI | LEASLEHLAP | SANPYLIDRV |
| 250 | 260 | 270 | 280 | ||
| LNLLVLMKGS | GAKFDTDELS | KIRKSFASLY | PVKDQLNEDD | YNAVKEMLG |