Q54MZ3
Gene name |
cdc20 (DDB_G0285601) |
Protein name |
Anaphase-promoting complex subunit cdc20 |
Names |
|
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0285601 |
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 Q54MZ3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54MZ3-F1 | Predicted | AlphaFoldDB |
No variants for Q54MZ3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54MZ3 | |||||
No associated diseases with Q54MZ3
7 regional properties for Q54MZ3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 212 - 291 | IPR001680-1 |
| repeat | WD40 repeat | 295 - 343 | IPR001680-2 |
| repeat | WD40 repeat | 340 - 382 | IPR001680-3 |
| repeat | WD40 repeat | 385 - 425 | IPR001680-4 |
| repeat | WD40 repeat | 428 - 468 | IPR001680-5 |
| conserved_site | WD40 repeat, conserved site | 321 - 335 | IPR019775 |
| domain | Anaphase-promoting complex subunit 4-like, WD40 domain | 212 - 275 | IPR024977 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| anaphase-promoting complex | A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B. |
| phagocytic vesicle | A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| anaphase-promoting complex binding | Binding to an anaphase-promoting complex. A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. |
| ubiquitin ligase activator activity | Binds to and increases the activity of a ubiquitin ligase. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| anaphase-promoting complex-dependent 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, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome. |
| cell cycle | The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| positive regulation of anaphase-promoting complex-dependent catabolic process | Any process that activates or increases the frequency, rate or extent of anaphase-promoting complex-dependent catabolic process. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to 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 |
| MNSNYETAEL | EQLLSLNAPL | ENVEARWQRK | ARQNNSNTNN | NNGNNGGDRF | IPNKMNIDIG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HFNLTKENSN | PNPNAINNNS | STSTSTTATS | STTNNIESTL | YKDTLANQLF | ESNSGDLESK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILSFKSKAPV | GNVSSSTNSL | RVLYSQNQVG | STPTDQSLKK | QFRQIPQQPE | RILDAPDIVD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DYYLNLLDWS | SQNVIAIPLG | QTVYLWNATT | SEIQRLFQVE | QQDDYITSLQ | WTKDGNYLAV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GTNSCTIQLW | DVAHTKKVRE | LRGHAGRVGA | LAWNDYILSS | GSSDTNIFNH | DVRVQNHHVS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TLSGHSQEVC | GLKWSHDGGQ | LASGGNDNII | NIWDINSENF | ETPAHTFEQH | TAAVRALAWC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PFQPNLLATG | GGAADRTIRF | WNTITGVCLN | TVDTMSQVCS | IQWSTTYREL | VSSHGYSQNQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LCVWKYPSMV | KCAELTGHTS | RALHTAISPD | GETVVSASAD | ETLRFWRVFE | KENKLPTANR |
| 490 | |||||
| KSKEVSDGSM | MRNINSLIR |