Q2SU52
Gene name |
rpsD |
Protein name |
30S ribosomal protein S4 |
Names |
|
Species |
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) |
KEGG Pathway |
bte:BTH_I3043 |
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 Q2SU52
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2SU52-F1 | Predicted | AlphaFoldDB |
No variants for Q2SU52
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2SU52 | |||||
No associated diseases with Q2SU52
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| small ribosomal subunit | The smaller of the two subunits of a ribosome. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| rRNA binding | Binding to a ribosomal RNA. |
| structural constituent of ribosome | The action of a molecule that contributes to the structural integrity of the ribosome. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| translation | The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MARYIGPKAK | LSRREGTDLF | LKSARRSLAD | KCKLDSKPGQ | HGRTSGARTS | DYGTQLREKQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KVKRIYGVLE | RQFRRYFAEA | DRRKGNTGEN | LLQLLESRLD | NVVYRMGFGS | TRAEARQLVS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HKAITVNGIV | ANIPSQQVKA | GDVISIREKA | KKQARIVEAL | SLAEQGGMPS | WVAVDAKKFE |
| 190 | 200 | ||||
| GTFKQVPERA | DIAGDINESL | IVELYSR |