Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C702 (RIR1_EBVA8) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 27. 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 140 kDa subunit
Ribonucleotide reductase large subunit
Gene names
ORF Names:BORF2
OrganismEpstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier82830 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length826 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 (R1) and a homodimer of the small subunit BaRF1 (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

   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 – 826826Ribonucleoside-diphosphate reductase large subunit
PRO_0000375965

Regions

Region186 – 1872Substrate binding By similarity
Region387 – 3915Substrate binding By similarity
Region594 – 5985Substrate binding By similarity

Sites

Active site3871Proton acceptor By similarity
Active site3891Cysteine radical intermediate By similarity
Active site3911Proton acceptor By similarity
Binding site1711Substrate By similarity
Binding site2171Substrate; via amide nitrogen By similarity
Site1871Important for hydrogen atom transfer By similarity
Site4031Important for hydrogen atom transfer By similarity
Site7251Important for electron transfer By similarity
Site7261Important for electron transfer By similarity
Site8221Interacts with thioredoxin/glutaredoxin By similarity
Site8251Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond187 ↔ 403Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C702 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 6E5C25623D371EF1

FASTA82693,031
        10         20         30         40         50         60 
MATTSHVEHE LLSKLIDELK VKANSDPEAD VLAGRLLHRL KAESVTHTVA EYLEVFSDKF 

        70         80         90        100        110        120 
YDEEFFQMHR DELETRVSAF AQSPAYERIV SSGYLSALRY YDTYLYVGRS GKQESVQHFY 

       130        140        150        160        170        180 
MRLAGFCAST TCLYAGLRAA LQRARPEIES DMEVFDYYFE HLTSQTVCCS TPFMRFAGVE 

       190        200        210        220        230        240 
NSTLASCILT TPDLSSEWDV TQALYRHLGR YLFQRAGVGV GVTGAGQDGK HISLLMRMIN 

       250        260        270        280        290        300 
SHVEYHNYGC KRPVSVAAYM EPWHSQIFKF LETKLPENHE RCPGIFTGLF VPELFFKLFR 

       310        320        330        340        350        360 
DTPWSDWYLF DPKDAGDLER LYGEEFEREY YRLVTAGKFC GRVSIKSLMF SIVNCAVKAG 

       370        380        390        400        410        420 
SPFILLKEAC NAHFWRDLQG EAMNAANLCA EVLQPSRKSV ATCNLANICL PRCLVNAPLA 

       430        440        450        460        470        480 
VRAQRADTQG DELLLALPRL SVTLPGEGAV GDGFSLARLR DATQCATFVV ACSILQGSPT 

       490        500        510        520        530        540 
YDSRDMASMG LGVQGLADVF ADLGWQYTDP PSRSLNKEIF EHMYFTALCT SSLIGLHTRK 

       550        560        570        580        590        600 
IFPGFKQSKY AGGWFHWHDW AGTDLSIPRE IWSRLSERIV RDGLFNSQFI ALMPTSGCAQ 

       610        620        630        640        650        660 
VTGCSDAFYP FYANASTKVT NKEEALRPNR SFWRHVRLDD REALNLVGGR VSCLPEALRQ 

       670        680        690        700        710        720 
RYLRFQTAFD YNQEDLIQMS RDRAPFVDQS QSHSLFLREE DAARASTLAN LLVRSYELGL 

       730        740        750        760        770        780 
KTIMYYCRIE KAADLGVMEC KASAALSVPR EEQNERSPAE QMPPRPMEPA QVAGPVDIMS 

       790        800        810        820 
KGPGEGPGGW CVPGGLEVCY KYRQLFSEDD LLETDGFTER ACESCQ 

« Hide

References

« Hide 'large scale' references
[1]"The genome of Epstein-Barr virus type 2 strain AG876."
Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.
Virology 350:164-170(2006) [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
DQ279927 Genomic DNA. Translation: ABB89232.1.
RefSeqYP_001129452.1. NC_009334.1.
YP_401655.1. NC_007605.1.

3D structure databases

ProteinModelPortalP0C702.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3783725.
5176186.

Phylogenomic databases

ProtClustDBCLSP2509697.

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_EBVA8
AccessionPrimary (citable) accession number: P0C702
Secondary accession number(s): Q777G1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: May 26, 2009
Last modified: October 16, 2013
This is version 27 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