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P09248 (RIR1_VZVD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase large subunit
Short name=R1
EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase large subunit
Gene names
ORF Names:ORF19
OrganismVaricella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) [Reference proteome]
Taxonomic identifier10338 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus ›
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability By similarity.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterotetramer composed of a homodimer of the large subunit ORF19 (R1) and a homodimer of the small subunit ORF18 (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Ontologies

Keywords
   Biological processDNA replication
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 775775Ribonucleoside-diphosphate reductase large subunit
PRO_0000187245

Regions

Region215 – 2162Substrate binding By similarity
Region427 – 4315Substrate binding By similarity
Region606 – 6105Substrate binding By similarity

Sites

Active site4271Proton acceptor By similarity
Active site4291Cysteine radical intermediate By similarity
Active site4311Proton acceptor By similarity
Binding site2001Substrate By similarity
Binding site2461Substrate; via amide nitrogen By similarity
Site2161Important for hydrogen atom transfer By similarity
Site4441Important for hydrogen atom transfer By similarity
Site7501Important for electron transfer By similarity
Site7511Important for electron transfer By similarity
Site7701Interacts with thioredoxin/glutaredoxin By similarity
Site7731Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond216 ↔ 444Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P09248 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 187695A65EB91B9D

FASTA77586,828
        10         20         30         40         50         60 
MEFKRIFNTV HDIINRLCQH GYKEYIIPPE STTPVELMEY ISTIVSKLKA VTRQDERVYR 

        70         80         90        100        110        120 
CCGELIHCRI NLRSVSMETW LTSPILCLTP RVRQAIEGRR DEIRRAILEP FLKDQYPALA 

       130        140        150        160        170        180 
TLGLQSALKY EDFYLTKLEE GKLESLCQFF LRLAATVTTE IVNLPKIATL IPGINDGYTW 

       190        200        210        220        230        240 
TDVCRVFFTA LACQKIVPAT PVMMFLGRET GATASCYLMD PESITVGRAV RAITGDVGTV 

       250        260        270        280        290        300 
LQSRGGVGIS LQSLNLIPTE NQTKGLLAVL KLLDCMVMAI NSDCERPTGV CVYIEPWHVD 

       310        320        330        340        350        360 
LQTVLATRGM LVRDEIFRCD NIFCCLWTPD LFFERYLSYL KGASNVQWTL FDNRADILRT 

       370        380        390        400        410        420 
LHGEAFTSTY LRLEREGLGV SSVPIQDIAF TIIRSAAVTG SPFLMFKDAC NRNYHMNTQG 

       430        440        450        460        470        480 
NAITGSNLCT EIVQKADAHQ HGVCNLASIN LTTCLSKGPV SFNLNDLQLT ARTTVIFLNG 

       490        500        510        520        530        540 
VLAAGNFPCK KSCKGVKNNR SLGIGIQGLH TTCLRLGFDL TSQPARRLNV QIAELMLYET 

       550        560        570        580        590        600 
MKTSMEMCKI GGLAPFKGFT ESKYAKGWLH QDGFSTISYL DLPWCTLRDD ICAYGLYNSQ 

       610        620        630        640        650        660 
FLALMPTVSS AQVTECSEGF SPIYNNMFSK VTTSGELLRP NLDLMDELRD MYSCEEKRLE 

       670        680        690        700        710        720 
VINILEKNQW SVIRSFGCLS NSHPLLKYKT AFEYEQEDLV DMCAERAPFI DQSQSMTLFI 

       730        740        750        760        770 
EERPDGTIPA SKIMNLLIRA YKAGLKTGMY YCKIRKATNS GLFAGGELTC TSCAL

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of varicella-zoster virus."
Davison A.J., Scott J.E.
J. Gen. Virol. 67:1759-1816(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Tinkering with a viral ribonucleotide reductase."
Lembo D., Brune W.
Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04370 Genomic DNA. Translation: CAA27902.1.
PIRWMBE19. A27343.

3D structure databases

ProteinModelPortalP09248.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBCLSP2509601.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_VZVD
AccessionPrimary (citable) accession number: P09248
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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