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P50646 (RIR1_BHV1C) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. 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 large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase large subunit
Gene names
Name:UL39
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 length787 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.

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 large chain family.

Ontologies

Keywords
   Biological processDNA replication
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 787787Ribonucleoside-diphosphate reductase large subunit
PRO_0000187240

Regions

Region224 – 2252Substrate binding By similarity
Region436 – 4405Substrate binding By similarity
Region618 – 6225Substrate binding By similarity

Sites

Active site4361Proton acceptor By similarity
Active site4381Cysteine radical intermediate By similarity
Active site4401Proton acceptor By similarity
Binding site2091Substrate By similarity
Binding site2551Substrate; via amide nitrogen By similarity
Site2251Important for hydrogen atom transfer By similarity
Site4531Important for hydrogen atom transfer By similarity
Site7621Important for electron transfer By similarity
Site7631Important for electron transfer By similarity
Site7821Interacts with thioredoxin/glutaredoxin By similarity
Site7851Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond225 ↔ 453Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50646 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8DB0F6327862333E

FASTA78786,010
        10         20         30         40         50         60 
MASDAFMQTA CPADAAEQLE AEHAEWAQLG CGAVPPPPAA ASRPSRAAVA AYVGEVVDRM 

        70         80         90        100        110        120 
RAQSRADERV YVKCGQLVHL RVRARSVPLD DWLTSAELAL VSEVAEPVRA NRAFVEVSLR 

       130        140        150        160        170        180 
YFELTEYATL RALGLQSALK YEEMYLAKLE GGAIESMGQF FVRIAATAAT WTMREPAFGR 

       190        200        210        220        230        240 
ALVGEGATWC AVFNAYLTAL YRQLVVPATP IMLFAGRARG SLASCYLLNP QVSSSTEAVE 

       250        260        270        280        290        300 
AITTEVARIL LNRGGIGISF QSFDRAVSRD CKRGIMGALK LLDSMAMAIN SDSERPTGIC 

       310        320        330        340        350        360 
VYLEPWHCDV RAVLNMRGLL ARDESTRCDN LFSCLWVPDL LFDRYLAHLE GREGVVWTLF 

       370        380        390        400        410        420 
DDRASHLSRL HGPAFTAEYE RLEREGLGVE TVPVQDLAFL IVRSIVMTGS PFVMFKDACN 

       430        440        450        460        470        480 
RHYHMDTAGD ALTGSNLCTE IVQRASPDAH GVCNLASVNL PRCVREGEGG ALAFDFAALS 

       490        500        510        520        530        540 
TAAATAAIFV NAMMLGGQYP TEKAARGVAR HRSLGIGFQG LHTLLLELGM DMLSPAARRL 

       550        560        570        580        590        600 
NVEIAERLLL AVMATSATLC EYGCAPFEDF ARSKFARGLM PFDGYEGVVL SLPRAWARLR 

       610        620        630        640        650        660 
EKVARHGLYN AQFVALMPTV SSSQVTEGSE GFSPVFTNMF SKVTMSGELL RPNLPLMRAL 

       670        680        690        700        710        720 
RKHFTREASR LGAVRALDRE QWSVAAALGD LAPGHPLAKF KTAFEYDQER LIDLCADRAP 

       730        740        750        760        770        780 
FVDQSQSMSL FVTEPMDGKV PASQIMNLLV YAYKKGLKTG LYYCKIRKAT NNGVFTGGDL 


VCSGCHL 

« Hide

References

[1]"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].
[2]"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].
[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
Z54206 Genomic DNA. Translation: CAA90929.1.
Z49078 Genomic DNA. Translation: CAA88900.1.
AJ004801 Genomic DNA. Translation: CAA06094.1.
RefSeqNP_045319.1. NC_001847.1.

3D structure databases

ProteinModelPortalP50646.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1487390.

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_BHV1C
AccessionPrimary (citable) accession number: P50646
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 69 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