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P11158 (RIR2_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase small chain

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase small subunit
Gene names
Ordered Locus Names:VACWR043
ORF Names:F4L
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Ref.4

Cofactor

Binds 2 iron ions per subunit By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

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

Induction

Expressed early in the viral replicative cycle. Ref.1 Ref.4

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Ribonucleoside-diphosphate reductase small chain
PRO_0000190498

Sites

Active site1081 By similarity
Metal binding701Iron 1 By similarity
Metal binding1011Iron 1 By similarity
Metal binding1011Iron 2 By similarity
Metal binding1041Iron 1 By similarity
Metal binding1631Iron 2 By similarity
Metal binding1971Iron 2 By similarity
Metal binding2001Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P11158 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8E296CCC5AB4F949

FASTA31936,973
        10         20         30         40         50         60 
MEPILAPNPN RFVIFPIQYY DIWNMYKKAE ASFWTVEEVD ISKDINDWNK LTPDEKYFIK 

        70         80         90        100        110        120 
HVLAFFAASD GIVNENLAER FCTEVQITEA RCFYGFQMAI ENIHSEMYSL LIDTYVKDSN 

       130        140        150        160        170        180 
EKNYLFNAIE TMPCVKKKAD WAQKWIHDSA GYGERLIAFA AVEGIFFSGS FASIFWLKKR 

       190        200        210        220        230        240 
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LLHPPSEETV RSIITDAVSI EQEFLTAALP 

       250        260        270        280        290        300 
VKLIGMNCEM MKTYIEFVAD RLISELGFKK IYNVTNPFDF MENISLEGKT NFFEKRVGEY 

       310 
QKMGVMSQED NHFSLDVDF 

« Hide

References

« Hide 'large scale' references
[1]"The vaccinia virus HindIII F fragment: nucleotide sequence of the left 6.2 kb."
Roseman N.A., Slabaugh M.B.
Virology 178:410-418(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]"Vaccinia virus-encoded ribonucleotide reductase: sequence conservation of the gene for the small subunit and its amplification in hydroxyurea-resistant mutants."
Slabaugh M., Roseman N., Davis R., Mathews C.
J. Virol. 62:519-527(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Hydroxyurea-resistant vaccinia virus: overproduction of ribonucleotide reductase."
Slabaugh M.B., Mathews C.K.
J. Virol. 60:506-514(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34368 mRNA. Translation: AAA48244.1.
M19117 Genomic DNA. Translation: AAA88680.1.
AY243312 Genomic DNA. Translation: AAO89322.1.
PIRRDVZVV. A29892.
RefSeqYP_232925.1. NC_006998.1.

3D structure databases

ProteinModelPortalP11158.
SMRP11158. Positions 2-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2157N.
IntActP11158. 1 interaction.
MINTMINT-130990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707500.

Phylogenomic databases

ProtClustDBCLSP2509773.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2_VACCW
AccessionPrimary (citable) accession number: P11158
Secondary accession number(s): Q76ZX1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 11, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways