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P69520

- RIR2_HHV23

UniProt

P69520 - RIR2_HHV23

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Protein
Ribonucleoside-diphosphate reductase small chain
Gene
N/A
Organism
Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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. 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 activityi

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

Cofactori

Binds 2 iron ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Iron 1 By similarity
Metal bindingi121 – 1211Iron 1 By similarity
Metal bindingi121 – 1211Iron 2 By similarity
Metal bindingi124 – 1241Iron 1 By similarity
Active sitei128 – 1281 By similarity
Metal bindingi184 – 1841Iron 2 By similarity
Metal bindingi218 – 2181Iron 2 By similarity
Metal bindingi221 – 2211Iron 2 By similarity

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. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleoside diphosphate metabolic process Source: InterPro
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
OrganismiHuman herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifieri10313 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Ribonucleoside-diphosphate reductase small chain
PRO_0000190505Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of a homodimer of the large subunit UL39 (R1) and a homodimer of the small subunit UL40 (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.

Structurei

3D structure databases

ProteinModelPortaliP69520.

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.

P69520-1 [UniParc]FASTAAdd to Basket

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MDPAVSPAST DPLDTHASGA GAAPIPVCPT PERYFYTSQC PDINHLRSLS    50
ILNRWLETEL VFVGDEEDVS KLSEGELGFY RFLFAFLSAA DDLVTENLGG 100
LSGLFEQKDI LHYYVEQECI EVVHSRVYNI IQLVLFHNND QARRAYVART 150
INHPAIRVKV DWLEARVREC DSIPEKFILM ILIEGVFFAA SFAAIAYLRT 200
NNLLRVTCQS NDLISRDEAV HTTASCYIYN NYLGGHAKPE AARVYRLFRE 250
AVDIEIGFIR SQAPTDSSIL SPGALAAIEN YVRFSADRLL GLIHMQPLYS 300
APAPDASFPL SLMSTDKHTN FFECRSTSYA GAVVNDL 337
Length:337
Mass (Da):37,626
Last modified:July 21, 1986 - v1
Checksum:i1E27E96599EE2120
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731I → V in CAA24930. 1 Publication
Sequence conflicti235 – 2351G → D in CAA24930. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12700 Genomic DNA. Translation: AAA45807.1.
X00048 Genomic DNA. Translation: CAA24930.1.
PIRiA00528. WMBE32.
A00529. WMBEB2.
RefSeqiNP_044510.1. NC_001798.1.

Genome annotation databases

GeneIDi1487327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12700 Genomic DNA. Translation: AAA45807.1 .
X00048 Genomic DNA. Translation: CAA24930.1 .
PIRi A00528. WMBE32.
A00529. WMBEB2.
RefSeqi NP_044510.1. NC_001798.1.

3D structure databases

ProteinModelPortali P69520.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P69520.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1487327.

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

  1. "Organization of the left-hand end of the herpes simplex virus type 2 BglII N fragment."
    Galloway D.A., Swain M.A.
    J. Virol. 49:724-730(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities."
    McLauchlan J., Clements J.B.
    EMBO J. 2:1953-1961(1983) [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.

Entry informationi

Entry nameiRIR2_HHV23
AccessioniPrimary (citable) accession number: P69520
Secondary accession number(s): P03174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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