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P69520 (RIR2_HHV23) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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 38 kDa subunit
Ribonucleotide reductase small subunit
OrganismHuman herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifier10313 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length337 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.

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 UL39 (R1) and a homodimer of the small subunit UL40 (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Ribonucleoside-diphosphate reductase small chain
PRO_0000190505

Sites

Active site1281 By similarity
Metal binding911Iron 1 By similarity
Metal binding1211Iron 1 By similarity
Metal binding1211Iron 2 By similarity
Metal binding1241Iron 1 By similarity
Metal binding1841Iron 2 By similarity
Metal binding2181Iron 2 By similarity
Metal binding2211Iron 2 By similarity

Experimental info

Sequence conflict1731I → V in CAA24930. Ref.2
Sequence conflict2351G → D in CAA24930. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P69520 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 1E27E96599EE2120

FASTA33737,626
        10         20         30         40         50         60 
MDPAVSPAST DPLDTHASGA GAAPIPVCPT PERYFYTSQC PDINHLRSLS ILNRWLETEL 

        70         80         90        100        110        120 
VFVGDEEDVS KLSEGELGFY RFLFAFLSAA DDLVTENLGG LSGLFEQKDI LHYYVEQECI 

       130        140        150        160        170        180 
EVVHSRVYNI IQLVLFHNND QARRAYVART INHPAIRVKV DWLEARVREC DSIPEKFILM 

       190        200        210        220        230        240 
ILIEGVFFAA SFAAIAYLRT NNLLRVTCQS NDLISRDEAV HTTASCYIYN NYLGGHAKPE 

       250        260        270        280        290        300 
AARVYRLFRE AVDIEIGFIR SQAPTDSSIL SPGALAAIEN YVRFSADRLL GLIHMQPLYS 

       310        320        330 
APAPDASFPL SLMSTDKHTN FFECRSTSYA GAVVNDL 

« Hide

References

[1]"Organization of the left-hand end of the herpes simplex virus type 2 BglII N fragment."
Galloway D.A., Swain M.A.
J. Virol. 49:724-730(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities."
McLauchlan J., Clements J.B.
EMBO J. 2:1953-1961(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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
M12700 Genomic DNA. Translation: AAA45807.1.
X00048 Genomic DNA. Translation: CAA24930.1.
PIRWMBE32. A00528.
WMBEB2. A00529.
RefSeqNP_044510.1. NC_001798.1.

3D structure databases

ProteinModelPortalP69520.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP69520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1487327.

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_HHV23
AccessionPrimary (citable) accession number: P69520
Secondary accession number(s): P03174
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 53 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