Q8I0H7
Gene name |
mhsp70 (hsp70, DDB_G0293298) |
Protein name |
Heat shock 70 kDa protein, mitochondrial |
Names |
75 kDa glucose-regulated protein homolog, GRP-75 |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0293298 |
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 Q8I0H7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8I0H7-F1 | Predicted | AlphaFoldDB |
No variants for Q8I0H7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8I0H7 | |||||
No associated diseases with Q8I0H7
3 regional properties for Q8I0H7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 35 - 42 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 219 - 232 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 360 - 374 | IPR018181-3 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| extracellular matrix | A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| misfolded protein binding | Binding to a misfolded protein. |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
| unfolded protein binding | Binding to an unfolded protein. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to unfolded protein | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus. |
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRSLKALKL | NSLNAQKGIR | QFCSDSKISG | QVIGIDLGTT | NSCVAVMQGA | EARVLENAEG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GRTTPSVVAF | TEDNQKIVGL | PAKRQMVTNA | ENTLFATKRL | IGRRFDDPMT | KKDMTMVPYK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IVKGPNGDAW | FEVKGKMISP | SEAGAMVLQK | MKETAETNLG | GPVTDAVITV | PAYFDDSQRQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ATRDAGTIAG | LKVQRIINEP | TAAALAYGFK | KDEPKTVAVY | DLGGGTFDIS | ILEIVGGVFE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VRATNGDTFL | GGEDFDNALL | EHFVAEFKKE | KGIDLTKDTM | ATQRLREAAE | KAKCELSSTL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TTEINLPYIS | AGPSGPVHFN | MKLTRSKFEQ | LVADLIQRTI | GPCNICLKDA | GLSTSEINEV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ILVGGMTRMP | KVQELAKSTF | NKEPFKGVNP | DEAVAVGAAI | QGGVLKGDTK | GIVLVDVTPL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLGIETLGGV | FTRLIKKNTN | IPASKTDTFS | TAADGQSEVE | IKVFQGEREM | AVDNKLLAKF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TLFGLPPLPK | GVPQIEVTFD | IDVNGMLQVI | AKDKATGKAQ | QVRIQTSGGL | SKDDIARILK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ESEANAEVDR | KRKELVEARN | NGESVVYQVE | KDLVEFKDYL | SQPQTEEIKK | AVQAVRDVLA |
| 610 | 620 | 630 | 640 | 650 | |
| KEDGSAIEAE | IKKLHDLTRS | SFETAYKAKL | DSSASKSSST | ENKENKDNTT | EAEFTEKK |