Q86JA1
Gene name |
psmC2 (DDB_G0276917) |
Protein name |
26S proteasome regulatory subunit 7 |
Names |
26S proteasome AAA-ATPase subunit RPT1, Proteasome 26S subunit ATPase 2 |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0276917 |
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 Q86JA1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q86JA1-F1 | Predicted | AlphaFoldDB |
No variants for Q86JA1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q86JA1 | |||||
No associated diseases with Q86JA1
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| phagocytic vesicle | A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis. |
| 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. |
| proteasome regulatory particle, base subcomplex | The subcomplex of the proteasome regulatory particle that directly associates with the proteasome core complex. |
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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVNKEDVEDE | LLNETAPVAL | DEGDIALLKS | YGVGPYSKSI | RILEEDIKKM | TSKVNELCGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KESDTGIGPP | SQWDLVVDKT | SAHEEPPLQV | ARCTKIIDVG | KPNAKYIITV | KQIAKFVVAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GDKLSPTDVE | EGIRVGVDRN | KYQIQIPLPP | KIDASVTMMQ | VEEKPDITYK | DVGGCKEQIE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLREVVEMPL | LHPEKFVNLG | IDPPKGVLMY | GPPGTGKTLC | ARAVANRTDA | AFVRVIGSEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VQKYVGEGAR | MVRDLFQMAR | SKKACIIFFD | EVDAIGGARF | DDGAGGDNEV | QRTMLELINQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LDGFDPRGNI | KVLMATNRPD | TLDPALLRPG | RLDRKVEFGL | PDLEGRAHIF | TIHAKTMSCA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RDIRFELLAR | LCPNSTGADI | RSVCTEAGMF | AIRARRKVVS | EKDFLEAIDK | VIKSYAKFSA |
| TSRYMHYN |