Q6AY63 (NUDT5_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 62.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: ADP-sugar pyrophosphatase EC=3.6.1.- EC=3.6.1.13 Alternative name(s): Nucleoside diphosphate-linked moiety X motif 5 Short name=Nudix motif 5 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 219 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Hydrolyzes with similar activities ADP-ribose, ADP-mannose, and ADP-glucose. Can also hydrolyze other nucleotide sugars with low activity By similarity. |
| Catalytic activity | ADP-ribose + H2O = AMP + D-ribose 5-phosphate. ADP-sugar + H2O = AMP + alpha-D-aldose 5-phosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | ribonucleoside diphosphate catabolic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 219 | 219 | ADP-sugar pyrophosphatase | PRO_0000250703 | |||||
Regions | |||||||||
| Domain | 57 – 197 | 141 | Nudix hydrolase | ||||||
| Region | 46 – 47 | 2 | Substrate binding; shared with dimeric partner By similarity | ||||||
| Motif | 97 – 118 | 22 | Nudix box | ||||||
Sites | |||||||||
| Metal binding | 96 | 1 | Magnesium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 166 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 28 | 1 | Substrate By similarity | ||||||
| Binding site | 84 | 1 | Substrate By similarity | ||||||
| Binding site | 98 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 133 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 9 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 10 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 42 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 210 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 218 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC079176 mRNA. Translation: AAH79176.1. |
| IPI | IPI00364928. |
| RefSeq | NP_001007734.1. NM_001007733.1. |
| UniGene | Rn.55388. |
3D structure databases | |
| ProteinModelPortal | Q6AY63. |
| SMR | Q6AY63. Positions 14-219. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6AY63. |
Proteomic databases | |
| PRIDE | Q6AY63. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000068551; ENSRNOP00000060464; ENSRNOG00000017741. |
| GeneID | 361274. |
| KEGG | rno:361274. |
| UCSC | NM_001007733. rat. |
Organism-specific databases | |
| CTD | 11164. |
| RGD | 1359284. Nudt5. |
Phylogenomic databases | |
| eggNOG | roNOG08100. |
| GeneTree | ENSGT00390000006280. |
| HOVERGEN | HBG052691. |
| InParanoid | Q6AY63. |
| OrthoDB | EOG46Q6TG. |
| PhylomeDB | Q6AY63. |
Gene expression databases | |
| ArrayExpress | Q6AY63. |
| Genevestigator | Q6AY63. |
| GermOnline | ENSRNOG00000017741. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR020476. Nudix_hydrolase. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view] |
| Gene3D | G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit. |
| KO | K13987. |
| Pfam | PF00293. NUDIX. 1 hit. [Graphical view] |
| PRINTS | PR00502. NUDIXFAMILY. |
| SUPFAM | SSF55811. NUDIX_hydrolase. 1 hit. |
| PROSITE | PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 675785. |
Entry information
| Entry name | NUDT5_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6AY63 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with