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 Q58FG0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58FG0-F1 | Predicted | AlphaFoldDB |
No variants for Q58FG0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58FG0 | |||||
No associated diseases with Q58FG0
No regional properties for Q58FG0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q58FG0 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 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. |
| unfolded protein binding | Binding to an unfolded protein. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGFHHVGQAG | LELLTSGHPA | LERRPEYLEE | RRIKEIVKKH | SQFIGYPITL | FVEKKRNKQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SDAEAEKKED | KRKKKKESND | KPEIEDVGSD | EEEEKKDADK | KKKKSKEKYI | DQELNKTKPI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WTRNPDAITN | EEYGEFHQSL | TNNWEDHLAV | KHFSVEGQLE | ELKDSRRVMK | ANQKHIYYIT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GETKDQVANS | AFVECLQKHG | LEVIYMIELI | DKYCVQQLKE | LESKTVVSVA | KEGLELPEDE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EEKKKQEEKK | TKFENLCKIM | KDMLEKKVKK | VVVSNCMEDP | QRHTNKIYRM | IKLGLGVDEY |
| 310 | 320 | 330 | |||
| DPTANDINAA | ITKEMPPLRG | GDDTSRMEEV | GGSG |