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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).By similarity

Catalytic activityi

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

Cofactori

Fe cationBy similarityNote: Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

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

Structurei

3D structure databases

ProteinModelPortaliP69520.
ModBaseiSearch...
MobiDBiSearch...

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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        10         20         30         40         50
MDPAVSPAST DPLDTHASGA GAAPIPVCPT PERYFYTSQC PDINHLRSLS
60 70 80 90 100
ILNRWLETEL VFVGDEEDVS KLSEGELGFY RFLFAFLSAA DDLVTENLGG
110 120 130 140 150
LSGLFEQKDI LHYYVEQECI EVVHSRVYNI IQLVLFHNND QARRAYVART
160 170 180 190 200
INHPAIRVKV DWLEARVREC DSIPEKFILM ILIEGVFFAA SFAAIAYLRT
210 220 230 240 250
NNLLRVTCQS NDLISRDEAV HTTASCYIYN NYLGGHAKPE AARVYRLFRE
260 270 280 290 300
AVDIEIGFIR SQAPTDSSIL SPGALAAIEN YVRFSADRLL GLIHMQPLYS
310 320 330
APAPDASFPL SLMSTDKHTN FFECRSTSYA GAVVNDL
Length:337
Mass (Da):37,626
Last modified:July 21, 1986 - v1
Checksum:i1E27E96599EE2120
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731I → V in CAA24930. (PubMed:6315408)Curated
Sequence conflicti235 – 2351G → D in CAA24930. (PubMed:6315408)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...

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: November 26, 2014
This is version 55 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