Q9VXA8
Gene name |
CG9125 |
Protein name |
Decapping nuclease DXO homolog |
Names |
Dom-3 homolog Z, NAD-capped RNA hydrolase CG9125, DeNADding enzyme CG9125 |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG9125 |
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 Q9VXA8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9VXA8-F1 | Predicted | AlphaFoldDB |
No variants for Q9VXA8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9VXA8 | |||||
No associated diseases with Q9VXA8
1 regional properties for Q9VXA8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | RAI1-like | 224 - 295 | IPR013961 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5'-3' exonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 5' end. |
| 5'-3' exoribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of an RNA molecule. |
| metal ion binding | Binding to a metal ion. |
| mRNA 5'-diphosphatase activity | Catalysis of the removal of a 5' terminal diphosphate from the 5'-triphosphate end of an mRNA, leaving a 5'-monophosphate end. |
| nucleotide binding | Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| RNA NAD-cap (NAD-forming) hydrolase activity | Catalysis of the reaction: a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA catabolic process | The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes. |
| NAD-cap decapping | Cleavage of the 5'-NAD-cap of an RNA. The NAD-cap is present at the 5'-end of some RNAs in both bacetria and eukaryotes. While it promotes RNA stability in bacteria, it promotes RNA decay in eukaryotes. |
| nuclear-transcribed mRNA catabolic process | The chemical reactions and pathways resulting in the breakdown of nuclear-transcribed mRNAs in eukaryotic cells. |
| nucleic acid phosphodiester bond hydrolysis | The nucleic acid metabolic process in which the phosphodiester bonds between nucleotides are cleaved by hydrolysis. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAENAGFISV | PWGQHKLGAM | YNTPFPSISR | PKCIGVCSIN | ASREFVDDAS | CASYLAGQPW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PPLPFDLNGG | IEDVIRKPVE | NGKRDLEIML | TYIKQHQKEL | LRQSSSDARN | LRLDSDFVTL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RGILRQIMCL | QYDNRSFRVK | ATLLNGNVYM | CKEETPEQQL | ENANMSRAQR | VMCSWGFKFE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QYLTSAQAQG | KPVTNVPVNE | AEEFMGVYRT | NLAGILMLYG | AELDCVDSKE | PVDFKDCRVL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DSLKFVELKT | SVFNMNPHQI | RTFKSFKSAN | WWSQSFLVGI | TTLYVGLRDT | KGMLQRIDEI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVATLARNKP | WSASAMAWYL | EQFLRNLKKL | LVNINDPFAV | VQVTFLNKHA | SYEVLRGPEH |
| 370 | |||||
| QILPNWYRDL | LKTRS |