Q55BV5
Gene name |
psmC1 (DDB_G0270784) |
Protein name |
26S proteasome regulatory subunit 4 homolog |
Names |
Tat-binding protein alpha, DdTBPalpha |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0270784 |
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 Q55BV5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q55BV5-F1 | Predicted | AlphaFoldDB |
No variants for Q55BV5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q55BV5 | |||||
No associated diseases with Q55BV5
5 regional properties for Q55BV5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AAA+ ATPase domain | 217 - 356 | IPR003593 |
| domain | ATPase, AAA-type, core | 221 - 354 | IPR003959 |
| conserved_site | ATPase, AAA-type, conserved site | 324 - 342 | IPR003960 |
| domain | Proteasomal ATPase OB C-terminal domain | 108 - 162 | IPR032501 |
| domain | AAA ATPase, AAA+ lid domain | 376 - 420 | IPR041569 |
3 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 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mitotic cytokinesis | A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. |
| 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. |
| sorocarp development | The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGNNQSQGQG | DKGEKKDQPK | YQPPPPPTQF | GKKKKRRGAE | TSTKLPVITP | HSKCKLKQLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LERIKDYLLM | EQEFLQNYDL | NQPKVDENSK | EQADEKIIEE | LRGDPLTVGN | LEEIIDDNHA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IVSSTVGPEH | YVRIMSFVDK | SKLYLGATVL | LNNKTLSVVG | VIDGEVDPMV | NVMKVEKAPT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ESYSDIGGLE | AQVQEMKEAI | ELPLTHPELY | EEIGIKPPKG | VILYGEPGTG | KTLLAKAVAN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QTSATFLRVV | GSELIQKYLG | DGPKLVRELF | RVADECAPSI | VFIDEIDAVG | TKRYDSQSGG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EREIQRTMLE | LLNQLDGFDA | RTDVKVIMAT | NRIETLDPAL | IRPGRIDRKI | EFPLPDIKTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RKIFEIHTAK | MNLSEDVNLE | EFVMSKDDLS | GADIKAICTE | SGLLALRERR | MRVTHTDFKK |
| 430 | |||||
| AKEKVLYRKT | AGAPEGLYM |