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P08543

- RIR1_HHV11

UniProt

P08543 - RIR1_HHV11

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

UL39

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei566 – 5661SubstrateBy similarity
    Sitei582 – 5821Important for hydrogen atom transferBy similarity
    Binding sitei612 – 6121Substrate; via amide nitrogenBy similarity
    Active sitei791 – 7911Proton acceptorBy similarity
    Active sitei793 – 7931Cysteine radical intermediateBy similarity
    Active sitei795 – 7951Proton acceptorBy similarity
    Sitei808 – 8081Important for hydrogen atom transferBy similarity
    Sitei1111 – 11111Important for electron transferBy similarity
    Sitei1112 – 11121Important for electron transferBy similarity
    Sitei1132 – 11321Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei1135 – 11351Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP 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. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication, Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Short name:
    R1
    Alternative name(s):
    ICP6
    Ribonucleotide reductase 136 kDa subunit
    Ribonucleotide reductase large subunit
    Gene namesi
    ORF Names:UL39
    OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
    Taxonomic identifieri10299 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000009294: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11371137Ribonucleoside-diphosphate reductase large subunitPRO_0000187236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi582 ↔ 808Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Keywords - Developmental stagei

    Early protein

    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

    Protein-protein interaction databases

    IntActiP08543. 4 interactions.
    MINTiMINT-6732628.

    Structurei

    3D structure databases

    ProteinModelPortaliP08543.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 393107alpha-crystallin domainBy similarityAdd
    BLAST
    Regioni581 – 5822Substrate bindingBy similarity
    Regioni791 – 7955Substrate bindingBy similarity
    Regioni968 – 9725Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi150 – 1545Poly-Pro
    Compositional biasi190 – 23950Asp/Ser-richAdd
    BLAST

    Domaini

    Contains an alpha-crystallin domain homologous to small heat-shock proteins.By similarity

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08543-1 [UniParc]FASTAAdd to Basket

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    MASRPAASSP VEARAPVGGQ EAGGPSAATQ GEAAGAPLAH GHHVYCQRVN     50
    GVMVLSDKTP GSASYRISDN NFVQCGSNCT MIIDGDVVRG RPQDPGAAAS 100
    PAPFVAVTNI GAGSDGGTAV VAFGGTPRRS AGTSTGTQTA DVPTEALGGP 150
    PPPPRFTLGG GCCSCRDTRR RSAVFGGEGD PVGPAEFVSD DRSSDSDSDD 200
    SEDTDSETLS HASSDVSGGA TYDDALDSDS SSDDSLQIDG PVCRPWSNDT 250
    APLDVCPGTP GPGADAGGPS AVDPHAPTPE AGAGLAADPA VARDDAEGLS 300
    DPRPRLGTGT AYPVPLELTP ENAEAVARFL GDAVNREPAL MLEYFCRCAR 350
    EETKRVPPRT FGSPPRLTED DFGLLNYALV EMQRLCLDVP PVPPNAYMPY 400
    YLREYVTRLV NGFKPLVSRS ARLYRILGVL VHLRIRTREA SFEEWLRSKE 450
    VALDFGLTER LREHEAQLVI LAQALDHYDC LIHSTPHTLV ERGLQSALKY 500
    EEFYLKRFGG HYMESVFQMY TRIAGFLACR ATRGMRHIAL GREGSWWEMF 550
    KFFFHRLYDH QIVPSTPAML NLGTRNYYTS SCYLVNPQAT TNKATLRAIT 600
    SNVSAILARN GGIGLCVQAF NDSGPGTASV MPALKVLDSL VAAHNKESAR 650
    PTGACVYLEP WHTDVRAVLR MKGVLAGEEA QRCDNIFSAL WMPDLFFKRL 700
    IRHLDGEKNV TWTLFDRDTS MSLADFHGEE FEKLYQHLEV MGFGEQIPIQ 750
    ELAYGIVRSA ATTGSPFVMF KDAVNRHYIY DTQGAAIAGS NLCTEIVHPA 800
    SKRSSGVCNL GSVNLARCVS RQTFDFGRLR DAVQACVLMV NIMIDSTLQP 850
    TPQCTRGNDN LRSMGIGMQG LHTACLKLGL DLESAEFQDL NKHIAEVMLL 900
    SAMKTSNALC VRGARPFNHF KRSMYRAGRF HWERFPDARP RYEGEWEMLR 950
    QSMMKHGLRN SQFVALMPTA ASAQISDVSE GFAPLFTNLF SKVTRDGETL 1000
    RPNTLLLKEL ERTFSGKRLL EVMDSLDAKQ WSVAQALPCL EPTHPLRRFK 1050
    TAFDYDQKLL IDLCADRAPY VDHSQSMTLY VTEKADGTLP ASTLVRLLVH 1100
    AYKRGLKTGM YYCKVRKATN SGVFGGDDNI VCMSCAL 1137
    Length:1,137
    Mass (Da):124,051
    Last modified:July 1, 1989 - v2
    Checksum:i8A3777F4C22D8F85
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1034 – 10341A → P in AAA45805. (PubMed:2835765)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701N → S in strain: Nonneuroinvasive mutant HF10, 17 syn+ and Isolate pYN1.
    Natural varianti1133 – 11331M → T in strain: Nonneuroinvasive mutant HF10.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32314.1.
    M18410 Genomic DNA. Translation: AAA45805.1.
    DQ889502 Genomic DNA. Translation: ABI63501.1.
    FJ593289 Genomic DNA. Translation: ACM62262.1.
    PIRiA26536. WMBEB1.
    RefSeqiNP_044641.1. NC_001806.1.

    Genome annotation databases

    GeneIDi2703361.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32314.1 .
    M18410 Genomic DNA. Translation: AAA45805.1 .
    DQ889502 Genomic DNA. Translation: ABI63501.1 .
    FJ593289 Genomic DNA. Translation: ACM62262.1 .
    PIRi A26536. WMBEB1.
    RefSeqi NP_044641.1. NC_001806.1.

    3D structure databases

    ProteinModelPortali P08543.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08543. 4 interactions.
    MINTi MINT-6732628.

    Chemistry

    BindingDBi P08543.
    ChEMBLi CHEMBL3840.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703361.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    [Graphical view ]
    Pfami PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
      McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
      J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Isolate pYN1.
    3. "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
      Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
      Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Nonneuroinvasive mutant HF10.
    4. "Herpes simplex virus type 1 bacterial artificial chromosome."
      Cunningham C., Davison A.J.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 17 syn+.
    5. "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 nameiRIR1_HHV11
    AccessioniPrimary (citable) accession number: P08543
    Secondary accession number(s): B9VQG7, Q09I94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3