Q61R02
Gene name |
CBG06798 |
Protein name |
Probable ATP-dependent RNA helicase DDX55 homolog |
Names |
DEAD box protein 55 |
Species |
Caenorhabditis briggsae |
KEGG Pathway |
cbr:CBG_06798 |
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 Q61R02
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q61R02-F1 | Predicted | AlphaFoldDB |
No variants for Q61R02
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q61R02 | |||||
No associated diseases with Q61R02
6 regional properties for Q61R02
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Receptor, ligand binding region | 60 - 458 | IPR001828 |
| domain | GPCR, family 3, nine cysteines domain | 496 - 546 | IPR011500 |
| domain | GPCR family 3, C-terminal | 562 - 833 | IPR017978 |
| conserved_site | GPCR, family 3, conserved site | 151 - 169 | IPR017979-1 |
| conserved_site | GPCR, family 3, conserved site | 518 - 540 | IPR017979-2 |
| conserved_site | GPCR, family 3, conserved site | 756 - 766 | IPR017979-3 |
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. |
| P granule | A small cytoplasmic, non-membranous RNA/protein complex aggregate in the primordial germ cells of many higher eukaryotes. |
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. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTSKVGAVAT | KTYREKLGPE | ILEVFDKSYK | SFTDVQVLAG | THLLNLSDVV | VESPTGSGKT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAFVLPMMRM | IQNARLQPNE | IGALILSPSR | ELCSQIVNVI | KPFAEKMKLN | VETVTGGQKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DKNIKMFKNK | DINILVATPG | RLFQIIQHEK | TMIARAMKGV | QLLVIDEADR | FNEIQFEDHM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| REILSCIPKQ | RRTGLFSATQ | VKEEDDLMVF | GLRNAKQVKV | SQERNSAAPS | TLKNYFVECP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ADEKTSVCLE | FIRQRTDKKV | LIFFPSCNSV | RYFHKIFERC | LTKRPLFAVH | GKCSNPHRAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QIKAFSESTN | GVMISTDVMA | RGIDITDIDW | VIQYDLPKHS | SWFVHRAGRT | ARCGRDGNAL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ILIATEQLAY | VSFLDNHEKV | KLEEVKVPTS | TSRKAEELRQ | KMIKIQVSDR | AILELGTRAF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VSHIESYAKH | DCHLICSLDD | LNVVGLANSY | ALLRLPKMRE | LAQRKDLNQF | DRSDIETSEI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KYADPKLEAN | RDTVMKEKHE | KKIETLAAKE | KKRREKEARK | MKRAGGRFKS | RATGANAEEK |
| 550 | 560 | 570 | |||
| RAKKRKSEEE | DDAQNDIRLL | KKIKRGKLSK | KEIKDVL |