A2RB17
Gene name |
rrp3 |
Protein name |
ATP-dependent rRNA helicase rrp3 |
Names |
|
Species |
Aspergillus niger (strain CBS 51388 / FGSC A1513) |
KEGG Pathway |
ang:ANI_1_682164 |
EC number |
3.6.4.13: Acting on ATP; involved in cellular and subcellular movement |
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 A2RB17
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2RB17-F1 | Predicted | AlphaFoldDB |
No variants for A2RB17
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2RB17 | |||||
No associated diseases with A2RB17
6 regional properties for A2RB17
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 196 - 204 | IPR000629 |
| domain | Helicase, C-terminal | 262 - 422 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 72 - 238 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 67 - 266 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 48 - 76 | IPR014014 |
| domain | DDX47/Rrp3, DEAD-box helicase domain | 49 - 251 | IPR044765 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.13 | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| small-subunit processome | A large ribonucleoprotein complex that is an early preribosomal complex. In S. cerevisiae, it has a size of 80S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| RNA helicase activity | Unwinding of an RNA helix, driven by ATP hydrolysis. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | Any process involved in the maturation of a precursor Small SubUnit (SSU) ribosomal RNA (rRNA) molecule into a mature SSU-rRNA molecule from the pre-rRNA molecule originally produced as a tricistronic rRNA transcript that contains the Small Subunit (SSU) rRNA, 5.8S rRNA, and the Large Subunit (LSU) in that order from 5' to 3' along the primary transcript. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPGVKKRKVA | REAPAPAPAQ | ESDVESSTPE | QTQEPEAQEQ | EQEEGQSKTF | KELGIIEQLC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EACETMGYKA | PTPIQRESIP | LALKGRDLIG | LAETGSGKTA | AFALPILQAL | MEKPQPFFGL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLAPTRELAY | QISKSFESLG | ASMGVRSCVI | VGGMDMVSQS | ISLGKKPHII | VATPGRLLDH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LENTKGFSLR | NLKYLVMDEA | DRLLDMDFGP | LLDKILKVLP | RERRTFLFSA | TMSSKVESLQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RASLSNPLRV | SVSTSKYQTV | STLLQSYLFI | PQKHKDLYLV | YLLNEFAGQS | TIIFTRTVNE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQRLAFLLRA | LGFGAIPLHG | QLSQSARLGA | LGKFRARSRN | ILVATDVAAR | GLDIPSVDVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LNFDLPGDSP | SYVHRVGRTA | RAGKSGLAIS | FVAQYDVEVW | LRIEGALGKK | LKEYDCPKDE |
| 430 | 440 | 450 | 460 | ||
| VMVLGENVAE | AQRQAIMDMK | DYNEKKGSRG | KKFGGKRSRD | EMDQEEG |