Q66663 (RIR1_EHV2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 69.
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: Ribonucleoside-diphosphate reductase large subunit EC=1.17.4.1 Alternative name(s): Ribonucleotide reductase large subunit | ||
| Gene names |
| ||
| Organism | Equine herpesvirus 2 (strain 86/87) (EHV-2) [Reference proteome] | ||
| Taxonomic identifier | 82831 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Percavirus › ![]() | ||
| Virus host | Equus caballus (Horse) [TaxID: 9796] |
Protein attributes
| Sequence length | 799 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. |
| Pathway | |
| Sequence similarities | Belongs to the ribonucleoside diphosphate reductase large chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Developmental stage | Early protein |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorInferred 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 – 799 | 799 | Ribonucleoside-diphosphate reductase large subunit | PRO_0000405987 | |||||||
Regions | |||||||||||
| Region | 207 – 208 | 2 | Substrate binding By similarity | ||||||||
| Region | 408 – 412 | 5 | Substrate binding By similarity | ||||||||
| Region | 612 – 616 | 5 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 408 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 410 | 1 | Cysteine radical intermediate By similarity | ||||||||
| Active site | 412 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 192 | 1 | Substrate By similarity | ||||||||
| Binding site | 238 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Site | 208 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 424 | 1 | Important for hydrogen atom transfer By similarity | ||||||||
| Site | 743 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 744 | 1 | Important for electron transfer By similarity | ||||||||
| Site | 795 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
| Site | 798 | 1 | Interacts with thioredoxin/glutaredoxin By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 208 ↔ 424 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The DNA sequence of equine herpesvirus 2." Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J. J. Mol. Biol. 249:520-528(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U20824 Genomic DNA. Translation: AAC13849.1. |
| PIR | S55656. |
| RefSeq | NP_042658.1. NC_001650.1. |
3D structure databases | |
| ProteinModelPortal | Q66663. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1461053. |
Phylogenomic databases | |
| ProtClustDB | CLSP2509697. |
Enzyme and pathway databases | |
| UniPathway | UPA00326. |
Family and domain databases | |
| InterPro | IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. [Graphical view] |
| Pfam | PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view] |
| PRINTS | PR01183. RIBORDTASEM1. |
| TIGRFAMs | TIGR02506. NrdE_NrdA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RIR1_EHV2 | ||||||||
| Accession | Primary (citable) accession number: Q66663 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
