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Q6R7K3 (RIR2_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

Names and origin

Protein attributes

Sequence length579 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.

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 (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 small chain family.

Contains 1 fido domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Ribonucleoside-diphosphate reductase small chain
PRO_0000385024

Regions

Domain435 – 579145Fido

Sites

Active site1671 By similarity
Metal binding1301Iron 1 By similarity
Metal binding1601Iron 1 By similarity
Metal binding1601Iron 2 By similarity
Metal binding1631Iron 1 By similarity
Metal binding2251Iron 2 By similarity
Metal binding2581Iron 2 By similarity
Metal binding2611Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6R7K3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E7B90F9E49DF0791

FASTA57966,994
        10         20         30         40         50         60 
MSQSTIKFDL GELTTTQCAR LLSKFIRKAT LTPEQFEILN TSYDELTEFD DHPLYGGATD 

        70         80         90        100        110        120 
HHKDIVGKYD HALLKPAVYQ QLRDFATKME SSSWQQTEID AESDIPTWEQ ISENERDCVR 

       130        140        150        160        170        180 
KVLAFFAVGD TLVKDRIAIF ADEFPLPECK DFIDWQTVNE GVHQRVYNNY LDALVKDKIY 

       190        200        210        220        230        240 
LADLVNAYKD PEFAPIKKKV DWLGKIISVE NDSRGEMVVG QVCTEAIMFA ASFAILLKFR 

       250        260        270        280        290        300 
APYMRALVLG NEFIRRDETL HFRFYAELLR LMPDRPSDER IAELLTEATE IELEFAEYVV 

       310        320        330        340        350        360 
PEGVKYITKD RLIQHVKANT NQVCEMLDIN PIYFDQKGNV LLSPLLYMNT LESEQKINFF 

       370        380        390        400        410        420 
EGKATEYNTK QYKVDFNNLF PPVKKMIEFA DEEEFIAAIV EGEGLSKDRN KDIVKQQLCL 

       430        440        450        460        470        480 
AWDHLSSHDM EGLVDMTWTL KDVHRIAMNH VIFNNGEFSN GYKFTVIDSG KVMYPTYETV 

       490        500        510        520        530        540 
EILESAVQGL IDDYNRDFSA LDKGVEKFDK DKIRVAARFI LDLLYIHPFS DGNGRTARLI 

       550        560        570 
MAHLIGKMTT PINREEYLKS IYHYRQTGDV SVFVDQFYR 

« 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: AAS00912.1.
RefSeqYP_024565.1. NC_005881.2.

3D structure databases

ProteinModelPortalQ6R7K3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2948202.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

Gene3D1.10.3290.10. 1 hit.
1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR003812. Fido.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF02661. Fic. 1 hit.
PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF140931. SSF140931. 1 hit.
SSF47240. SSF47240. 1 hit.
PROSITEPS51459. FIDO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2_OSHVF
AccessionPrimary (citable) accession number: Q6R7K3
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