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Q01038 (RIR2_SHV21) 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:60
Synonyms:EELF3
OrganismSaimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri) [Reference proteome]
Taxonomic identifier10383 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus
Virus hostSaimiri sciureus (Common squirrel monkey) [TaxID: 9521]

Protein attributes

Sequence length305 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

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Ribonucleoside-diphosphate reductase small chain
PRO_0000190510

Sites

Active site1011 By similarity
Metal binding641Iron 1 By similarity
Metal binding941Iron 1 By similarity
Metal binding941Iron 2 By similarity
Metal binding971Iron 1 By similarity
Metal binding1571Iron 2 By similarity
Metal binding1911Iron 2 By similarity
Metal binding1941Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01038 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 484B019D1755B92D

FASTA30535,167
        10         20         30         40         50         60 
MDSVKKYLYT CDHVGFLELT KETWKNRWFP SQVPLQGDVC CVDMLNERDL EFYKFLFTFL 

        70         80         90        100        110        120 
GMAEKLVNIN IEDLLSQFDS HDISHYYAEQ MAMENIHGKV YANILNMLFK NNITEVYSYA 

       130        140        150        160        170        180 
CDIMNDSALQ EKLRWLNGRV TEASDKAEKI LLFLLVEGIF FISSFFSIGL FRVRGIMNGI 

       190        200        210        220        230        240 
CLANDYIARD EMLHTSAAAL LYNTMTKSSE RPSEDWIYKL FREAVEVEFK FIAAKGYGVS 

       250        260        270        280        290        300 
LVNVHEIRQF LQATADRILE SINLNPIYGS LPPENCPLAY TSSTKSVNFF ERDNSDYTGT 


LTNDL 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the herpesvirus saimiri genome."
Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B., Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B., Honess R.W.
J. Virol. 66:5047-5058(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus saimiri (HVS) L-DNA: general conservation of genetic organization between HVS and Epstein-Barr virus."
Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.
Virology 188:296-310(1992) [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
X64346 Genomic DNA. Translation: CAA45683.1.
M86409 Genomic DNA. Translation: AAA46136.1.
RefSeqNP_040262.1. NC_001350.1.

3D structure databases

ProteinModelPortalQ01038.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1682509.

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_SHV21
AccessionPrimary (citable) accession number: Q01038
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