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 C5FRQ0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5FRQ0-F1 | Predicted | AlphaFoldDB |
No variants for C5FRQ0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5FRQ0 | |||||
No associated diseases with C5FRQ0
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchored component of membrane | The component of a membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
1 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRGDSFIWSL | TTAASLLYAT | VESLQVVKRD | NPSIVGFDIE | RFQVAKPVHR | DIIAKRASGK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TVSQDLDNQT | IRAHIDTGSS | DLWVNTDDSQ | FCSSRRSPCR | EGGTFDSSSS | STYQLVSNDF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NISYVDGSGA | SGDYVTDVIE | VGGIQLKEFQ | FAIGHTSSSP | LGVLGIGYEA | GEALVSRFGD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ESYPNLPAAL | VKAGHIRSNA | YSLWLNDLSA | SRGQILFGGV | DTGKFEGKLQ | TVPVLHTSGG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYTSLVIALT | SVGIRTASEG | SLDTFPAQPV | AVAMDSGSSL | SYLPDALAAK | IYNSIDAVFD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PSNNLAFVPC | SMVNDDRKLV | FTFSSPQITV | GMDELVIDLG | PDANGNEATF | RDGSKACVFG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IAPAGRSISI | LGDTVLRSAY | LVYDLDNNEI | SIAPTRFNST | VTNIMEIGTG | KNSVPDATGV |
| 430 | 440 | 450 | 460 | 470 | |
| PNAVTSAPIT | QATGLSGIET | GVPGARPTSR | GAAPTMRPDV | TFGVAAAGLA | GAGILFAFM |