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Q01319 (RIR2_BHV1C) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 83. 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
Name:UL40
OrganismBovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Taxonomic identifier10323 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length314 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 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

Heterodimer of a large and a small chain.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Ribonucleoside-diphosphate reductase small chain
PRO_0000190507

Sites

Active site1101 By similarity
Metal binding731Iron 1 By similarity
Metal binding1031Iron 1 By similarity
Metal binding1031Iron 2 By similarity
Metal binding1061Iron 1 By similarity
Metal binding1661Iron 2 By similarity
Metal binding2001Iron 2 By similarity
Metal binding2031Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01319 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 257FB0E91111632E

FASTA31435,251
        10         20         30         40         50         60 
MAEAADAATL TRKYKYFYET ECPDLDHLRS LSVANRWLET EFPLADDAKD VARLSGAELE 

        70         80         90        100        110        120 
FYRFLFAFLS AADDLVNVNL GDLSELFTQK DILHYYIEQE SIEVVHSRVY SAIQLLLFRN 

       130        140        150        160        170        180 
DAVARAGYVE GALGDPAVRR KVDWLERRVA AAESVAEKYV LMILIEGIFF SSSFAAIAYL 

       190        200        210        220        230        240 
RTHNLFVVTC QTNDLISRDE AVHTAASCCI FDNYLGGERP PPARIYELFR EAWKLSASLF 

       250        260        270        280        290        300 
GCAPRGSHIL DVEAISAYVE YSADRLLAAI QLPPLFGTPP PGTDFPLALM TAEKHTNFFE 

       310 
RRSTNYTGTV INDL 

« Hide

References

[1]"Sequencing and 5'- and 3'-end transcript mapping of the gene encoding the small subunit of ribonucleotide reductase from bovine herpesvirus type-1."
Simard C., Bastien N., Trudel M.
Virology 190:689-701(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Cooper / 34.
[2]"Sequence analysis of the UL39, UL38, and UL37 homologues of bovine herpesvirus 1 and expression studies of UL40 and UL39, the subunits of ribonucleotide reductase."
Simard C., Langlois I., Styger D., Vogt B., Vlcek C., Chalifour A., Trudel M., Schwyzer M.
Virology 212:734-740(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Gene contents in a 31-kb segment at the left genome end of bovine herpesvirus-1."
Schwyzer M., Styger D., Vogt B., Lowery D.E., Simard C., LaBoissiere S., Misra V., Vlcek C., Paces V.
Vet. Microbiol. 53:67-77(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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
Z54206 Genomic DNA. Translation: CAA90928.1.
M84470 Genomic DNA. Translation: AAA46063.1.
Z49078 Genomic DNA. Translation: CAA88899.1.
AJ004801 Genomic DNA. Translation: CAA06093.1.
PIRWMBEB4. A43367.
RefSeqNP_045318.1. NC_001847.1.

3D structure databases

ProteinModelPortalQ01319.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4783423.

Phylogenomic databases

ProtClustDBCLSP2509600.

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_BHV1C
AccessionPrimary (citable) accession number: Q01319
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 11, 2013
This is version 83 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