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 P54814
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P54814-F1 | Predicted | AlphaFoldDB |
No variants for P54814
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P54814 | |||||
No associated diseases with P54814
5 regional properties for P54814
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AAA+ ATPase domain | 178 - 317 | IPR003593 |
| domain | ATPase, AAA-type, core | 182 - 314 | IPR003959 |
| conserved_site | ATPase, AAA-type, conserved site | 285 - 303 | IPR003960 |
| domain | Proteasomal ATPase OB C-terminal domain | 69 - 124 | IPR032501 |
| domain | AAA ATPase, AAA+ lid domain | 338 - 380 | IPR041569 |
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. |
| 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. |
| proteasome complex | A large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. In eukaryotes, this complex consists of the barrel shaped proteasome core complex and one or two associated proteins or complexes that act in regulating entry into or exit from the core. |
3 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. |
| proteasome-activating activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTLTKMEVDS | TKGEGFRPYY | ITKIEELQLI | VAEKSQNLRR | LQAQRNELNA | KVRMLREELQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLQEQGSYVG | EVVKPMDKKK | VLVKVHPEGK | FVVDLDKNVD | INDVTANCRV | ALRNESYTLH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KILPNKVDPL | VSLMMVEKVP | DSTYEMVGGL | DKQIKEIKEV | IELPVKHPEL | FDALGIAQPK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GVLLYGPPGT | GKTLLARAVA | HHTECTFIRV | SGSELVQKFI | GEGSRMVREL | FVMAREHAPS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IIFMDEIDSI | GSSRIESGSG | GDSEVQRTML | ELLNQLDGFE | ATKNIKVIMA | TNRIDILDPA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLRPGRIDRK | IEFPPPNEEA | RLDILKIHSR | KMNLTRGINL | RKIAELMPGA | SGAEVKGVCT |
| 370 | 380 | 390 | 400 | ||
| EAGMYALRER | RVHVTQEDFE | MAVAKVMQKD | SEKNMSIKKL | WK |