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 Q56362
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q56362-F1 | Predicted | AlphaFoldDB |
No variants for Q56362
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q56362 | |||||
No associated diseases with Q56362
No regional properties for Q56362
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q56362 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartic-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. |
| enzyme activator activity | Binds to and increases the activity of an enzyme. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRSDPEILVL | GIGNLLWADE | GFGVRAVEAL | QRHWVMSSNV | QLLDGGTQGI | YLVDRVRKAD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VLVVFDAVDY | GLPPGTMKRV | EDDEVPRFLG | AKKMSLHQTG | FQEVLALAAM | LGDYPKHLLL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IGVQPVELDD | FGGSLRPQIK | ERITPAIEMA | LEYLAQFGVV | ARRREDSTVD | SPHLPHPSLD |
| 190 | 200 | 210 | 220 | ||
| LIAYESGRPG | PEIACRIGDE | RVLTSLSART | VQPGNPHGDR | Q |