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Protein

Ribonucleoside-diphosphate reductase small chain

Gene

BaRF1

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

Cofactori

Fe cation1 PublicationNote: Binds 2 iron ions per subunit.1 Publication

Pathway:iDNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Iron 1
Metal bindingi91 – 911Iron 1
Metal bindingi91 – 911Iron 2
Metal bindingi94 – 941Iron 1
Active sitei98 – 981PROSITE-ProRule annotation1 Publication
Metal bindingi154 – 1541Iron 2
Metal bindingi188 – 1881Iron 2
Metal bindingi191 – 1911Iron 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase small chain (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase 38 kDa subunit
Ribonucleotide reductase small subunit
Gene namesi
ORF Names:BaRF1
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007640 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Ribonucleoside-diphosphate reductase small chainPRO_0000190502Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of a homodimer of the large subunit BORF2 (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n (By similarity).By similarity

Protein-protein interaction databases

IntActiP0CAP6. 6 interactions.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2313
Helixi27 – 293
Helixi33 – 386
Helixi39 – 413
Helixi44 – 7229
Helixi78 – 10528
Turni106 – 1083
Helixi110 – 12112
Helixi124 – 1263
Helixi127 – 13913
Helixi143 – 15513
Turni156 – 1583
Helixi159 – 17113
Helixi175 – 20228
Helixi205 – 2073
Helixi211 – 23222
Turni233 – 2353
Helixi241 – 25818

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A58X-ray1.68A/B1-302[»]
4A5CX-ray2.01A/B1-302[»]
4A5DX-ray1.79A/B1-302[»]
4A5EX-ray2.01A/B1-302[»]
4A5FX-ray2.14A/B1-302[»]
4A5HX-ray1.85A/B1-302[»]
4A5IX-ray2.05A/B1-302[»]
4A5JX-ray1.88A/B1-302[»]
ProteinModelPortaliP0CAP6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK10808.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
IPR030475. RNR_small_AS.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CAP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLLYVRDH EGFACLTVET HRNRWFAAHI VLTKDCGCLK LLNERDLEFY
60 70 80 90 100
KFLFTFLAMA EKLVNFNIDE LVTSFESHDI DHYYTEQKAM ENVHGETYAN
110 120 130 140 150
ILNMLFDGDR AAMNAYAEAI MADEALQAKI SWLRDKVAAA VTLPEKILVF
160 170 180 190 200
LLIEGIFFIS SFYSIALLRV RGLMPGICLA NNYISRDELL HTRAASLLYN
210 220 230 240 250
SMTAKADRPR ATWIQELFRT AVEVETAFIE ARGEGVTLVD VRAIKQFLEA
260 270 280 290 300
TADRILGDIG QAPLYGTPPP KDCPLTYMTS IKQTNFFEQE SSDYTMLVVD

DL
Length:302
Mass (Da):34,359
Last modified:May 26, 2009 - v1
Checksum:i473BF0BDFB7F0637
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221A → T no nucleotide entry (PubMed:22824004).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24843.1.
AJ507799 Genomic DNA. Translation: CAD53406.1.
PIRiA00530. WMBE12.
RefSeqiYP_401656.1. NC_007605.1.

Genome annotation databases

GeneIDi3783683.
KEGGivg:3783683.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24843.1.
AJ507799 Genomic DNA. Translation: CAD53406.1.
PIRiA00530. WMBE12.
RefSeqiYP_401656.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A58X-ray1.68A/B1-302[»]
4A5CX-ray2.01A/B1-302[»]
4A5DX-ray1.79A/B1-302[»]
4A5EX-ray2.01A/B1-302[»]
4A5FX-ray2.14A/B1-302[»]
4A5HX-ray1.85A/B1-302[»]
4A5IX-ray2.05A/B1-302[»]
4A5JX-ray1.88A/B1-302[»]
ProteinModelPortaliP0CAP6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CAP6. 6 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783683.
KEGGivg:3783683.

Phylogenomic databases

KOiK10808.

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
IPR030475. RNR_small_AS.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Homology between two EBV early genes and HSV ribonucleotide reductase and 38K genes."
    Gibson T.J., Stockwell P., Ginsburg M., Barrell B.G.
    Nucleic Acids Res. 12:5087-5099(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROTEIN.
  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.
  4. "Mechanistic basis for Epstein-Barr Virus ribonucleotide-reductase small-subunit function."
    Schmitzberger F., Gurmu D., Dahlroth S.L., Nordlund P.
    ACS Chem. Biol. 7:1764-1764(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON IONS, COFACTOR, ACTIVE SITE.

Entry informationi

Entry nameiRIR2_EBVB9
AccessioniPrimary (citable) accession number: P0CAP6
Secondary accession number(s): P03175, Q777G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: May 26, 2009
Last modified: May 27, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.