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P0CAP6

- RIR2_EBVB9

UniProt

P0CAP6 - RIR2_EBVB9

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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: 4 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.

Catalytic activityi

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

Cofactori

Binds 2 iron ions per subunit.1 Publication

Pathwayi

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 – 9811 Publication
Metal bindingi154 – 1541Iron 2
Metal bindingi188 – 1881Iron 2
Metal bindingi191 – 1911Iron 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. DNA replication Source: UniProtKB-UniPathway
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: 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.

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:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[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

MSKLLYVRDH EGFACLTVET HRNRWFAAHI VLTKDCGCLK LLNERDLEFY    50
KFLFTFLAMA EKLVNFNIDE LVTSFESHDI DHYYTEQKAM ENVHGETYAN 100
ILNMLFDGDR AAMNAYAEAI MADEALQAKI SWLRDKVAAA VTLPEKILVF 150
LLIEGIFFIS SFYSIALLRV RGLMPGICLA NNYISRDELL HTRAASLLYN 200
SMTAKADRPR ATWIQELFRT AVEVETAFIE ARGEGVTLVD VRAIKQFLEA 250
TADRILGDIG QAPLYGTPPP KDCPLTYMTS IKQTNFFEQE SSDYTMLVVD 300
DL 302
Length:302
Mass (Da):34,359
Last modified:May 26, 2009 - v1
Checksum:i473BF0BDFB7F0637
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221A → T no nucleotide entry 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V01555 Genomic DNA. Translation: CAA24843.1 .
AJ507799 Genomic DNA. Translation: CAD53406.1 .
PIRi A00530. WMBE12.
RefSeqi YP_401656.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A58 X-ray 1.68 A/B 1-302 [» ]
4A5C X-ray 2.01 A/B 1-302 [» ]
4A5D X-ray 1.79 A/B 1-302 [» ]
4A5E X-ray 2.01 A/B 1-302 [» ]
4A5F X-ray 2.14 A/B 1-302 [» ]
4A5H X-ray 1.85 A/B 1-302 [» ]
4A5I X-ray 2.05 A/B 1-302 [» ]
4A5J X-ray 1.88 A/B 1-302 [» ]
ProteinModelPortali P0CAP6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3783683.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 14, 2014
This is version 35 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