Reviewed,
UniProtKB/Swiss-Prot Q7T6Y8 (RIR1_MIMIV)
Last modified
February 9, 2010.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribonucleoside-diphosphate reductase large subunit EC=1.17.4.1 Alternative name(s): Ribonucleotide reductase large subunit | ||||
| Gene names |
| ||||
| Organism | Acanthamoeba polyphaga mimivirus (APMV) [Complete proteome] | ||||
| Taxonomic identifier | 212035 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Mimiviridae › Mimivirus | ||||
| Virus host | Acanthamoeba polyphaga (Amoeba) [TaxID: 5757] |
Protein attributes
| Sequence length | 881 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity. |
| Catalytic activity | 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. |
| Enzyme regulation | Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity. |
| Pathway | |
| Subunit structure | Heterodimer of a large and a small chain By similarity. |
| Sequence similarities | Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Developmental stage | Early protein |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Allosteric enzyme Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 881 | 881 | Ribonucleoside-diphosphate reductase large subunit | PRO_0000187229 | |||||||
Regions | |||||||||||
| Domain | 69 – 160 | 92 | ATP-cone | ||||||||
| Region | 286 – 287 | 2 | Substrate binding By similarity | ||||||||
| Region | 493 – 497 | 5 | Substrate binding By similarity | ||||||||
| Region | 675 – 679 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 493 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 495 | 1 | Cysteine radical intermediate By similarity | ||||||||
| Active site | 497 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 271 | 1 | Substrate By similarity | ||||||||
| Binding site | 315 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Site | 287 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 294 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 324 | 1 | Allosteric effector binding By similarity | ||||||||
| Site | 510 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 809 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 810 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 876 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
| Site | 879 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 287 ↔ 510 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The 1.2-megabase genome sequence of Mimivirus." Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M. Science 306:1344-1350(2004) [PubMed: 15486256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Rowbotham-Bradford. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY653733 Genomic DNA. Translation: AAQ09572.2. |
| RefSeq | YP_142667.1. |
3D structure databases | |
| SMR | Q7T6Y8. Positions 145-814. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3162147. |
Enzyme and pathway databases | |
| BRENDA | 1.17.4.1. 281366. |
Family and domain databases | |
| InterPro | IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. [Graphical view] |
| PANTHER | PTHR11573. Ribncl_red_lg_C. 1 hit. |
| Pfam | PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view] |
| PRINTS | PR01183. RIBORDTASEM1. |
| TIGRFAMs | TIGR02506. NrdE_NrdA. 1 hit. |
| PROSITE | PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RIR1_MIMIV | ||||||||
| Accession | Primary (citable) accession number: Q7T6Y8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


