O94641
Gene name |
hsp104 (SPBC16D10.08c) |
Protein name |
Heat shock protein 104 |
Names |
Protein aggregation-remodeling factor hsp104 |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC16D10.08c |
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 O94641
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O94641-F1 | Predicted | AlphaFoldDB |
No variants for O94641
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O94641 | |||||
No associated diseases with O94641
9 regional properties for O94641
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AAA+ ATPase domain | 201 - 348 | IPR003593-1 |
| domain | AAA+ ATPase domain | 613 - 787 | IPR003593-2 |
| domain | ATPase, AAA-type, core | 206 - 339 | IPR003959-1 |
| domain | ATPase, AAA-type, core | 613 - 778 | IPR003959-2 |
| domain | Clp, repeat (R) domain | 2 - 149 | IPR004176 |
| conserved_site | ClpA/B, conserved site 1 | 298 - 310 | IPR018368 |
| domain | Clp ATPase, C-terminal | 785 - 876 | IPR019489 |
| conserved_site | ClpA/B, conserved site 2 | 647 - 665 | IPR028299 |
| domain | ClpA/ClpB, AAA lid domain | 346 - 447 | IPR041546 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nuclear envelope | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). |
| nucleolar ring | Ring-like structures located at the nucleolar periphery where several nuclear factors are reversibly aggregated and sequestered during acute heat stress. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| protein aggregate center | Reversible aggregate of misfolded proteins and chaperones formed to shield thermosensitive proteins from degradation until conditions allow disaggregation and refolding. |
6 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 disaggregase activity | An ATP-dependent molecular chaperone activity that mediates the solubilization of ordered protein aggregates. |
| chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| misfolded protein binding | Binding to a misfolded protein. |
| unfolded protein binding | Binding to an unfolded protein. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular heat acclimation | Any process that increases heat tolerance of a cell in response to high temperatures. |
| cellular response to heat | 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 a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| cellular response to misfolded 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 a misfolded 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. |
| protein unfolding | The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADYPFTDKA | AKTLSDAYSI | AQSYGHSQLT | PIHIAAALLS | DSDSNGTTLL | RTIVDKAGGD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GQKFERSVTS | RLVRLPAQDP | PPEQVTLSPE | SAKLLRNAHE | LQKTQKDSYI | AQDHFIAVFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KDDTLKSLLA | EAGVTPKAFE | FAVNNVRGNK | RIDSKNAEEG | FDALNKFTVD | LTELARNGQL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DPVIGREDEI | RRTIRVLSRR | TKNNPVLIGE | PGVGKTSIAE | GLARRIIDDD | VPANLSNCKL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSLDVGSLVA | GSKFRGEFEE | RIKSVLKEVE | ESETPIILFV | DEMHLLMGAG | SGGEGGMDAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NLLKPMLARG | KLHCIGATTL | AEYKKYIEKD | AAFERRFQII | LVKEPSIEDT | ISILRGLKEK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YEVHHGVTIS | DRALVTAAHL | ASRYLTSRRL | PDSAIDLVDE | AAAAVRVTRE | SQPEVLDNLE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RKLRQLRVEI | RALEREKDEA | SKERLKAARK | EAEQVEEETR | PIREKYELEK | SRGSELQDAK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RRLDELKAKA | EDAERRNDFT | LAADLKYYGI | PDLQKRIEYL | EQQKRKADAE | AIANAQPGSE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PLLIDVVGPD | QINEIVARWT | GIPVTRLKTT | EKERLLNMEK | VLSKQVIGQN | EAVTAVANAI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RLSRAGLSDP | NQPIASFLFC | GPSGTGKTLL | TKALASFMFD | DENAMIRIDM | SEYMEKHSVS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RLIGAPPGYV | GHEAGGQLTE | QLRRRPYSVI | LFDEIEKAAP | EVLTVLLQVL | DDGRITSGQG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| QVVDAKNAVI | IMTSNLGAEY | LTTDNESDDG | KIDSTTREMV | MNSIRGFFRP | EFLNRISSIV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IFNRLRRVDI | RNIVENRILE | VQKRLQSNHR | SIKIEVSDEA | KDLLGSAGYS | PAYGARPLNR |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VIQNQVLNPM | AVLILNGQLR | DKETAHVVVQ | NGKIFVKPNH | EANANGSADI | DMDGIDDDVN |
| DEELE |