Q9CWD3
Gene name |
Nudt17 |
Protein name |
Nucleoside diphosphate-linked moiety X motif 17 |
Names |
Nudix motif 17 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:78373 |
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 Q9CWD3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9CWD3-F1 | Predicted | AlphaFoldDB |
17 variants for Q9CWD3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388652123 | 29 | A>E | No | EVA | |
| rs3393158676 | 41 | S>R | No | EVA | |
| rs3388647686 | 47 | L>I | No | EVA | |
| rs258539282 | 85 | P>L | No | EVA | |
| rs3388651818 | 91 | V>M | No | EVA | |
| rs3393368797 | 96 | A>V | No | EVA | |
| rs3388652066 | 101 | S>T | No | EVA | |
| rs3388651752 | 104 | Q>K | No | EVA | |
| rs3388638348 | 138 | C>R | No | EVA | |
| rs3388654060 | 210 | A>D | No | EVA | |
| rs3393384132 | 214 | L>Q | No | EVA | |
| rs3388653994 | 222 | V>M | No | EVA | |
| rs3388632108 | 230 | R>S | No | EVA | |
| rs3388632103 | 237 | Q>R | No | EVA | |
| rs3388648108 | 267 | T>R | No | EVA | |
| rs3393158579 | 272 | A>T | No | EVA | |
| rs3388638391 | 273 | E>K | No | EVA |
No associated diseases with Q9CWD3
1 regional properties for Q9CWD3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | NUDIX hydrolase domain | 90 - 236 | IPR000086 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| NADH pyrophosphatase activity | Catalysis of the reaction: NADH + H2O = AMP + NMNH + 2 H+. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| NAD catabolic process | The chemical reactions and pathways resulting in the breakdown of nicotinamide adenine dinucleotide, a coenzyme present in most living cells and derived from the B vitamin nicotinic acid; catabolism may be of either the oxidized form, NAD, or the reduced form, NADH. |
| NADH metabolic process | The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid. |
| NADP catabolic process | The chemical reactions and pathways resulting in the breakdown of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; catabolism may be of either the oxidized form, NADP, or the reduced form, NADPH. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P0C025 | NUDT17 | Nucleoside diphosphate-linked moiety X motif 17 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAARLLLRL | AGRLESVSFT | QSVCGLLGAG | QRPGPWHTHC | SLERGQLVLS | SNPFPGASER |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LPIQRPLFCP | FAALDQQPEV | SKTEPLTNRG | VDLGVAVILQ | SSDQTVLLTR | RTCTLRISPN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LWVPPGGHME | PDEEILECGF | RELWEECGLQ | LPKNQFSCVL | LGLWESAYPP | RLSWGFPKYH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HLILYVLVIS | QESQEQLQAR | IQVNPNEVNA | FMWLGPDVAA | AVVATEDGTR | TPGLFSQDLP |
| 250 | 260 | 270 | 280 | 290 | |
| LSVCATELKD | DGGTQPLVLP | MPTLMRTTPT | TAEEDKERIG | AGTKFALQLW | LQHLGR |