Q75EC0
Gene name |
SDS23 (AAR154W) |
Protein name |
Protein SDS23 |
Names |
|
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_AAR154W |
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 Q75EC0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q75EC0-F1 | Predicted | AlphaFoldDB |
No variants for Q75EC0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q75EC0 | |||||
No associated diseases with Q75EC0
3 regional properties for Q75EC0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | CBS domain | 189 - 248 | IPR000644-1 |
| domain | CBS domain | 274 - 333 | IPR000644-2 |
| domain | CBS domain | 359 - 464 | IPR000644-3 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleotide-activated protein kinase complex | A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae). |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| AMP binding | Binding to AMP, adenosine monophosphate. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| protein kinase regulator activity | Modulates the activity of a protein kinase, an enzyme which phosphorylates a protein. |
| protein serine/threonine phosphatase inhibitor activity | Binds to and stops, prevents or reduces the activity of a serine/threonine protein phosphatase, an enzyme that catalyzes the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to glucose starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| regulation of catalytic activity | Any process that modulates the activity of an enzyme. |
| regulation of mitotic metaphase/anaphase transition | Any process that modulates the frequency, rate or extent of the cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MREKQQGTTG | AGGMSSGAAA | ASPGQRHASI | VEMLSTPPPA | IVVQTGMEDE | NVRATGGETA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADGDERRTLS | RQSSTSSTES | HASATSCLTK | VHAQKWQHIE | LSQLVEENKL | VFINAEMSVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAFNTLVEHN | LTSLPVERYP | GDMDCVTFDY | NDLNSYLLLV | LGKTTVADEE | ITRQCQSGQP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VPVGRIVKLT | PKNPFYKVPE | TEDLSTVMGI | LGSGVHRVAI | VDSTSSSIRG | ILSQRRLMKY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LWDNARQFSN | LEVLLNSSLQ | KLGIGVLDPH | TPPTSRQSRV | ISILDTEPLL | VALHKMHTER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ISSIAVIDHQ | GMLLGNISVT | DVKQVTRTSQ | YPLLHNTCRH | FISVILNNRG | LEMGKDSFPI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FHVYPTSSLA | RTVAKLVATK | AHRLWIVQPV | EQGVLVSPPV | APTTIDGSSE | FSSRHVSPSP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| APSPAGSHGP | LTTSASPLGT | LDKEYSTGKL | IGVVSLTDIL | GLLARKHTEN | KLVDPLSARR |
| QRGSVAR |