Q5RFQ5
Gene name |
DDX6 |
Protein name |
Probable ATP-dependent RNA helicase DDX6 |
Names |
DEAD box protein 6 |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100190811 |
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 Q5RFQ5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RFQ5-F1 | Predicted | AlphaFoldDB |
No variants for Q5RFQ5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RFQ5 | |||||
No associated diseases with Q5RFQ5
5 regional properties for Q5RFQ5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 244 - 252 | IPR000629 |
| domain | Helicase, C-terminal | 308 - 468 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 121 - 286 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 115 - 312 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 96 - 124 | IPR014014 |
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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic stress granule | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. |
| 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. |
| P-body | A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. |
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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| miRNA-mediated gene silencing by inhibition of translation | An RNA interference pathway in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs. |
| negative regulation of translation | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| P-body assembly | The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTARTENPV | IMGLSSQNGQ | LRGPVKPTGG | PGGGGTQTQQ | QMNQLKNTNT | INNGTQQQAQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SMTTTIKPGD | DWKKTLKLPP | KDLRIKTSDV | TSTKGNEFED | YCLKRELLMG | IFEMGWEKPS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PIQEESIPIA | LSGRDILARA | KNGTGKSGAY | LIPLLERLDL | KKDNIQAMVI | VPTRELALQV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SQICIQVSKH | MGGAKVMATT | GGTNLRGDIM | RLDDTVHVVI | ATPGRILDLI | KKGVAKVDHV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QMIVLDEADK | LLSQDFVQIM | EDIILTLPKN | RQILLYSATF | PLSVQKFMNS | HLQKPYEINL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MEELTLKGVT | QYYAYVTERQ | KVHCLNTLFS | RLQINQSIIF | CNSSQRVELL | AKKISQLGYS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| CFYIHAKMRQ | EHRNRVFHDF | RNGLCRNLVC | TDLFTRGIDI | QAVNVVINFD | FPKLAETYLH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RIGGSGRFGH | LGLAINLITY | DDRFNLKSIE | EQLGTEIKPI | PSNIDKSLYV | AEYHSEPVED |
| EKP |