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P06474

- RIR2_HHV1K

UniProt

P06474 - RIR2_HHV1K

Protein

Ribonucleoside-diphosphate reductase small chain

Gene

UL40

Organism
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      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 bindingi94 – 941Iron 1PROSITE-ProRule annotation
    Metal bindingi124 – 1241Iron 1PROSITE-ProRule annotation
    Metal bindingi124 – 1241Iron 2By similarity
    Metal bindingi127 – 1271Iron 1PROSITE-ProRule annotation
    Active sitei131 – 1311PROSITE-ProRule annotation
    Metal bindingi187 – 1871Iron 2By similarity
    Metal bindingi221 – 2211Iron 2By similarity
    Metal bindingi224 – 2241Iron 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
    Gene namesi
    Name:UL40
    OrganismiHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
    Taxonomic identifieri10306 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Ribonucleoside-diphosphate reductase small chainPRO_0000190504Add
    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

    ProteinModelPortaliP06474.
    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.

    P06474-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSAAPALSP ALTAHTGHSA TADLAIQIPK CPDPERYFYT SQCPDINHLR    50
    SLSILNRWLE TELVFVGDEE DVSKLSEGEL SFYRFLFAFL SAADDLVTEN 100
    LGGLSGLFEQ KDILHYYVEQ ECIEVAHSRV YNIIQLVLFH NNDQARREYV 150
    AGTINHPAIR AKVDWLEARV RECASVPEKF ILMILIEGIF FAASFAAIAY 200
    LRTNNLLRVT CQSNDLISRD EAVHTTASCY IYNNYLGGHA KPPPDRVYGL 250
    FRQAVEIEIG FIRSQAPTDS HILSPAALAA IENYVRFSAD RLLGLIHMKP 300
    LFSAPPPDAS FPLSLMSTDK HTNFFECRST SYAGAVVNDL 340
    Length:340
    Mass (Da):37,966
    Last modified:November 1, 1995 - v2
    Checksum:i921DC04B9D278DE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02212 Genomic DNA. Translation: AAA66436.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02212 Genomic DNA. Translation: AAA66436.1 .

    3D structure databases

    ProteinModelPortali P06474.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P06474.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Detailed characterization of an apparently unspliced beta herpes simplex virus type 1 gene mapping in the interior of another."
      Draper K.G., Frink R.J., Wagner E.K.
      J. Virol. 43:1123-1128(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Wagner E.K.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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_HHV1K
    AccessioniPrimary (citable) accession number: P06474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 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