Q1RJH1
Gene name |
rpsA (RBE_0412) |
Protein name |
30S ribosomal protein S1 |
Names |
|
Species |
Rickettsia bellii (strain RML369-C) |
KEGG Pathway |
rbe:RBE_0412 |
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 Q1RJH1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1RJH1-F1 | Predicted | AlphaFoldDB |
No variants for Q1RJH1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1RJH1 | |||||
No associated diseases with Q1RJH1
11 regional properties for Q1RJH1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | S1 domain | 120 - 187 | IPR003029-1 |
| domain | S1 domain | 204 - 276 | IPR003029-2 |
| domain | S1 domain | 290 - 363 | IPR003029-3 |
| domain | S1 domain | 379 - 450 | IPR003029-4 |
| domain | S1 domain | 464 - 536 | IPR003029-5 |
| domain | RNA-binding domain, S1 | 37 - 103 | IPR022967-1 |
| domain | RNA-binding domain, S1 | 119 - 187 | IPR022967-2 |
| domain | RNA-binding domain, S1 | 206 - 276 | IPR022967-3 |
| domain | RNA-binding domain, S1 | 291 - 363 | IPR022967-4 |
| domain | RNA-binding domain, S1 | 378 - 450 | IPR022967-5 |
| domain | RNA-binding domain, S1 | 465 - 536 | IPR022967-6 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| ribonucleoprotein complex | A macromolecular complex that contains both RNA and protein molecules. |
| ribosome | An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| 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 |
| MTTKLKQRFV | PQLAAVNHEF | EDDFSKMLET | VDTSHIKPGT | VVKGQVVDIN | EVVVVDVGLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NEGRIPKSEF | LLSPAHKLPE | IGDLVDVYIE | KTEGHSGKTL | SREKAIKEEL | WGQLELICSK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GEFVDGTIFG | RVKGGFTVDL | SGVVAFLPGS | QVDVRPIKDP | SSIMNIRQPF | KILSMDKKLG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NIVVSRRAIL | EESRSEARDE | MLSKIKEGMI | LEGTVKNITD | YGAFIDLGSV | DGLLHLTDIS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WARVNHPSEV | LEFNQKVKVM | VIKFNEETKR | ISLGMKQLDY | NPWEKIKEEF | PVGKKMTGKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TNFADYGVFI | ELKDGLEGLV | HSSEISWLKS | NQNPRKTLTI | GQEVEFMVLE | VDTEKHRVSL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SIKQCQQNPL | IKFAETNPVG | TVIKAPIRNI | TDFGIFVALS | DNLDGMIHEG | DITWEDNGNE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LLKTYKKGDE | VECKVLTINI | EKEQISLGIK | QLTPNPYQGI | ADEYKKGTVV | KAVVTAIKDD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GLEVLVNDKA | AGFIKKSDLS | DEKEEQKPEM | FAVDQEIEAK | VASIEKSTNK | ILLSIKAYKI |
| 550 | 560 | 570 | |||
| AERQKALKEY | GSSDNTTNMG | DILANALEDS | KK |