Ribonucleoside-diphosphate reductase small chain - Varicella-zoster virus (strain Oka vaccine) (HHV-3)

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Q4JQV7 (RIR2_VZVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 32. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase small chain
Short name=R2
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

ORF Names:

ORF18

Organism

Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3) [Complete proteome]

Taxonomic identifier

341980 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability 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 ORF19 (R1) and a homodimer of the small subunit ORF18 (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.
Subcellular location	Host membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Host membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ORF23	Q4JQV2	3	EBI-2532450,EBI-2532547
ORF26	Q4JQU9	3	EBI-2532450,EBI-2532467

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 306

306

Ribonucleoside-diphosphate reductase small chain

PRO_0000385164

Regions

Transmembrane

153 – 173

Helical; Potential

Sites

Active site

103

By similarity

Metal binding

Iron 1 By similarity

Metal binding

Iron 1 By similarity

Metal binding

Iron 2 By similarity

Metal binding

Iron 1 By similarity

Metal binding

159

Iron 2 By similarity

Metal binding

193

Iron 2 By similarity

Metal binding

196

Iron 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q4JQV7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 76CD3F8BB8C1B094
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FASTA

306

35,397

        10         20         30         40         50         60 
MDQKDCSHFF YRPECPDINN LRALSISNRW LESDFIIEDD YQYLDCLTED ELIFYRFIFT 

        70         80         90        100        110        120 
FLSAADDLVN VNLGSLTQLF SQKDIHHYYI EQECIEVVHA RVYSQIQLML FRGDESLRVQ 

       130        140        150        160        170        180 
YVNVTINNPS IQQKVQWLEE KVRDNPSVAE KYILMILIEG IFFVSSFAAI AYLRNNGLFV 

       190        200        210        220        230        240 
VTCQFNDLIS RDEAIHTSAS CCIYNNYVPE KPAITRIHQL FSEAVEIECA FLKSHAPKTR 

       250        260        270        280        290        300 
LVNVDAITQY VKFSADRLLS AINVPKLFNT PPPDSDFPLA FMIADKNTNF FERHSTSYAG 


TVINDL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the complete DNA sequences of the Oka varicella vaccine and its parental virus." Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K. J. Virol. 76:11447-11459(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Isolate Human/Japan/P-Oka/1970 and Oka varicella vaccine Biken (V-Oka-Biken).
[2]	"Complete DNA sequences of two oka strain varicella-zoster virus genomes." Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M., Vassilev V. J. Virol. 82:11023-11044(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oka varicella vaccine VarilRix (V-Oka-GSK) and Oka varicella vaccine Varivax (V-Oka-Merk).
[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	AB097932 Genomic DNA. No translation available. AB097933 Genomic DNA. No translation available. DQ008354 Genomic DNA. Translation: AAY57634.1. DQ008355 Genomic DNA. Translation: AAY57705.1.
RefSeq	NP_040141.1. NC_001348.1.
3D structure databases
ProteinModelPortal	Q4JQV7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q4JQV7. 22 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1487715.
Phylogenomic databases
ProtClustDB	CLSP2509600.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_VZVO

Accession

Primary (citable) accession number: Q4JQV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents