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P69520

- RIR2_HHV23

UniProt

P69520 - RIR2_HHV23

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
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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

    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

    « Hide

    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

    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:
    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: October 1, 2014
    This is version 54 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