Q6FQE9
Gene name |
DDI1 (CAGL0I06787g) |
Protein name |
DNA damage-inducible protein 1 |
Names |
|
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0I06787g |
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 Q6FQE9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FQE9-F1 | Predicted | AlphaFoldDB |
No variants for Q6FQE9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FQE9 | |||||
No associated diseases with Q6FQE9
5 regional properties for Q6FQE9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ubiquitin-like domain | 1 - 73 | IPR000626 |
| domain | Peptidase A2A, retrovirus, catalytic | 219 - 297 | IPR001995 |
| domain | Ubiquitin-associated domain | 387 - 426 | IPR015940 |
| domain | Aspartic peptidase, DDI1-type | 185 - 314 | IPR019103 |
| domain | DNA damage inducible protein 1 ubiquitin-like domain | 1 - 74 | IPR033882 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
6 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. |
| polyubiquitin modification-dependent protein binding | Binding to a protein upon poly-ubiquitination of the target protein. |
| proteasome regulatory particle binding | Binding to a proteasome regulatory particle. |
| protein-macromolecule adaptor activity | The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid. |
| SNARE binding | Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein. |
| ubiquitin binding | Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of DNA replication | Any process that activates or increases the frequency, rate or extent of DNA replication. |
| protein secretion | The controlled release of proteins from a cell. |
| protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway | The process of directing proteins towards the vacuole that contributes to protein catabolism via the multivesicular body (MVB) pathway. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQLTVTNDVN | GEVYGPLELS | GDMMLMDLVA | LLEVDCAFES | GKQQLYFNGK | ELKPDVEKTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EELGIGNDDL | IVIRGQPVSS | NSIANSTSAI | ELDDDAYVEQ | FRLQLLSNSA | LRNSLRMPFA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DIDSLVNDPQ | QFKTHMGPVI | IQRRRMQSAM | PTNPYGIPDE | EYKKLMTNPE | DPEHKKRLQE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LQDKQLIDEQ | LRNALEYTPE | VFAQVSMLYI | NMEINGHPVK | AFVDSGAQMT | IISPRLAEKT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ELKRFIDNRF | IGEARGVGTG | KILGRVHQVQ | VKIETQFIPC | SFVVLDSNVD | LLLGLDMLKR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HQACIDLEKN | VLRIAGTETK | FLGEAEIPKG | TSFDAVGNPQ | PPVEIKESAD | HSKKKMKTSF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TITPKVKPVK | ADNLLNNSSP | MGNTGRTFPE | KTIKQLMDLG | FSRQEVIQAL | VSTNGNAEFA |
| ASLLFQ |