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Q6R7H4 (RIR1_OSHVF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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

Protein attributes

Sequence length835 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. 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 (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
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

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 – 835835Ribonucleoside-diphosphate reductase large subunit
PRO_0000385023

Regions

Region237 – 2382Substrate binding By similarity
Region447 – 4515Substrate binding By similarity
Region660 – 6645Substrate binding By similarity

Sites

Active site4471Proton acceptor By similarity
Active site4491Cysteine radical intermediate By similarity
Active site4511Proton acceptor By similarity
Binding site2221Substrate By similarity
Binding site2661Substrate; via amide nitrogen By similarity
Site2381Important for hydrogen atom transfer By similarity
Site4641Important for hydrogen atom transfer By similarity
Site7971Important for electron transfer By similarity
Site7981Important for electron transfer By similarity
Site8301Interacts with thioredoxin/glutaredoxin By similarity
Site8331Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond238 ↔ 464Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6R7H4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4C5813635B9E5F47

FASTA83593,356
        10         20         30         40         50         60 
MACSMANAVR PGLSDLPEGV DLSNPKEVRS LLIKLTHARK STVYDTKIRR LHGVIVNSIM 

        70         80         90        100        110        120 
ENYNSAEGEL DMAITPLIPS HPDYAFLAGR VSAYMTQINT PKTFTDAVYG IQMAVGETNG 

       130        140        150        160        170        180 
FRSPMKPVKG GLSDEIVDFV NEHGARLDGM IDDVRDYSHN YMGITGLLNG VAIKVNKKLY 

       190        200        210        220        230        240 
ERPQYVFMRV AMAMTDLSSE TALEDIWQTY MLISGQCLSM ASPVLFNGGT SSSNTASCFL 

       250        260        270        280        290        300 
LDMGDNMVSI TKKVAQTMTL IAKNGGIGIN FSKLRATGSK IGMAGKSSGI GGKLNLFDRV 

       310        320        330        340        350        360 
AQSVDQGENK RPGAIAGYLT DWHADMYDWL YSRYSGSGNE VNKRHVLNMG LVMSDLFMER 

       370        380        390        400        410        420 
VENDKEWSLF SPNDVVGLEE LYGEKFVRAY RAHEANPKIK RTTVSARKLF SDIANMMWST 

       430        440        450        460        470        480 
GEPYILFKDA VNERSNHKHL GTIKNSNLCC EIVQYCDTNE IAVCNLATIC VSNFVNVETG 

       490        500        510        520        530        540 
EIDFEGIADA AGVACKGINN LIDKQNYDLG NEQLMRLADE RTEEVVEVNG IKFDAKYNLV 

       550        560        570        580        590        600 
SYSNLKHRPQ GIGMQGLHDV FMKLKIPYDS EMAFRLAALI QEAIYYGAVR ESVKIAEEKG 

       610        620        630        640        650        660 
PYPSYYWDNN THREGKLQFD FLEGFDRDRD LTHELFNWRE VLKKFEKFGI NNSVVTAQPP 

       670        680        690        700        710        720 
SASSSQLNDN VESIEAITSN RFTKGIKDGK FIIINKHLQK DLEDLGMWDA QMVGDIEAND 

       730        740        750        760        770        780 
GSIQNIERIP KNIREIYKTA REIDHKAVVK ICAAIQPFID QTISKNMFVP KNVDNPVQLI 

       790        800        810        820        830 
MENVILGHKM KLKTGMYYTR GIPAMKQQNF GKMNFQDKDI GKPVPELVDC EACSA 

« Hide

References

« Hide 'large scale' references
[1]"A novel class of herpesvirus with bivalve hosts."
Davison A.J., Trus B.L., Cheng N., Steven A.C., Watson M.S., Cunningham C., Le Deuff R.M., Renault T.
J. Gen. Virol. 86:41-53(2005) [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
AY509253 Genomic DNA. Translation: AAS00941.1.
RefSeqYP_024594.1. NC_005881.2.

3D structure databases

ProteinModelPortalQ6R7H4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2948194.

Phylogenomic databases

ProtClustDBCLSP2509774.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIR1_OSHVF
AccessionPrimary (citable) accession number: Q6R7H4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 61 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