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P89462

- RIR1_HHV2H

UniProt

P89462 - RIR1_HHV2H

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

UL39

Organism
Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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.
    ATP + a protein = ADP + a phosphoprotein.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei571 – 5711SubstrateBy similarity
    Sitei587 – 5871Important for hydrogen atom transferBy similarity
    Binding sitei617 – 6171Substrate; via amide nitrogenBy similarity
    Active sitei796 – 7961Proton acceptorBy similarity
    Active sitei798 – 7981Cysteine radical intermediateBy similarity
    Active sitei800 – 8001Proton acceptorBy similarity
    Sitei813 – 8131Important for hydrogen atom transferBy similarity
    Sitei1116 – 11161Important for electron transferBy similarity
    Sitei1117 – 11171Important for electron transferBy similarity
    Sitei1137 – 11371Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei1140 – 11401Interacts 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):
    ICP10
    Ribonucleotide reductase 136 kDa subunit
    Ribonucleotide reductase large subunit
    Gene namesi
    ORF Names:UL39
    OrganismiHuman herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
    Taxonomic identifieri10315 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000001874: Genome

    Subcellular locationi

    Host cell membrane 1 Publication. Host endosome membrane 1 Publication
    Note: Associates with the host cytoskeleton.Curated

    GO - Cellular componenti

    1. host cell endosome membrane Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cell membrane, Host endosome, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11421142Ribonucleoside-diphosphate reductase large subunitPRO_0000385162Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi587 ↔ 813Redox-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

    BioGridi1677930. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP89462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni294 – 400107alpha-crystallin domainAdd
    BLAST
    Regioni586 – 5872Substrate bindingBy similarity
    Regioni796 – 8005Substrate bindingBy similarity
    Regioni973 – 9775Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi151 – 1599Poly-Pro
    Compositional biasi186 – 23954Asp/Ser-richAdd
    BLAST

    Domaini

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

    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.

    P89462-1 [UniParc]FASTAAdd to Basket

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    MANRPAASAL AGARSPSERQ EPREPEVAPP GGDHVFCRKV SGVMVLSSDP     50
    PGPAAYRISD SSFVQCGSNC SMIIDGDVAR GHLRDLEGAT STGAFVAISN 100
    VAAGGDGRTA VVALGGTSGP SATTSVGTQT SGEFLHGNPR TPEPQGPQAV 150
    PPPPPPPFPW GHECCARRDA RGGAEKDVGA AESWSDGPSS DSETEDSDSS 200
    DEDTGSETLS RSSSIWAAGA TDDDDSDSDS RSDDSVQPDV VVRRRWSDGP 250
    APVAFPKPRR PGDSPGNPGL GAGTGPGSAT DPRASADSDS AAHAAAPQAD 300
    VAPVLDSQPT VGTDPGYPVP LELTPENAEA VARFLGDAVD REPALMLEYF 350
    CRCAREESKR VPPRTFGSAP RLTEDDFGLL NYALAEMRRL CLDLPPVPPN 400
    AYTPYHLREY ATRLVNGFKP LVRRSARLYR ILGVLVHLRI RTREASFEEW 450
    MRSKEVDLDF GLTERLREHE AQLMILAQAL NPYDCLIHST PNTLVERGLQ 500
    SALKYEEFYL KRFGGHYMES VFQMYTRIAG FLACRATRGM RHIALGRQGS 550
    WWEMFKFFFH RLYDHQIVPS TPAMLNLGTR NYYTSSCYLV NPQATTNQAT 600
    LRAITGNVSA ILARNGGIGL CMQAFNDASP GTASIMPALK VLDSLVAAHN 650
    KQSTRPTGAC VYLEPWHSDV RAVLRMKGVL AGEEAQRCDN IFSALWMPDL 700
    FFKRLIRHLD GEKNVTWSLF DRDTSMSLAD FHGEEFEKLY EHLEAMGFGE 750
    TIPIQDLAYA IVRSAATTGS PFIMFKDAVN RHYIYDTQGA AIAGSNLCTE 800
    IVHPASKRSS GVCNLGSVNL ARCVSRQTFD FGRLRDAVQA CVLMVNIMID 850
    STLQPTPQCT RGNDNLRSMG IGMQGLHTAC LKMGLDLESA EFRDLNTHIA 900
    EVMLLAAMKT SNALCVRGAR PFSHFKRSMY RAGRFHWERF SNASPRYEGE 950
    WEMLRQSMMK HGLRNSQFIA LMPTAASAQI SDVSEGFAPL FTNLFSKVTR 1000
    DGETLRPNTL LLKELERTFG GKRLLDAMDG LEAKQWSVAQ ALPCLDPAHP 1050
    LRRFKTAFDY DQELLIDLCA DRAPYVDHSQ SMTLYVTEKA DGTLPASTLV 1100
    RLLVHAYKRG LKTGMYYCKV RKATNSGVFA GDDNIVCTSC AL 1142
    Length:1,142
    Mass (Da):124,923
    Last modified:May 1, 1997 - v1
    Checksum:i5A46D3985338BB21
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z86099 Genomic DNA. Translation: CAB06725.1.
    PIRiA05247.
    RefSeqiNP_044509.1. NC_001798.1.

    Genome annotation databases

    GeneIDi1487325.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z86099 Genomic DNA. Translation: CAB06725.1 .
    PIRi A05247.
    RefSeqi NP_044509.1. NC_001798.1.

    3D structure databases

    ProteinModelPortali P89462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1677930. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1487325.

    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 genome sequence of herpes simplex virus type 2."
      Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.
      J. Virol. 72:2010-2021(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10)."
      Hunter J.C., Smith C.C., Bose D., Kulka M., Broderick R., Aurelian L.
      Virology 210:345-360(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    3. "The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway."
      Perkins D., Pereira E.F., Gober M., Yarowsky P.J., Aurelian L.
      J. Virol. 76:1435-1449(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27."
      Chabaud S., Lambert H., Sasseville A.M., Lavoie H., Guilbault C., Massie B., Landry J., Langelier Y.
      FEBS Lett. 545:213-218(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALPHA-CRYSTALLIN DOMAIN.
    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_HHV2H
    AccessioniPrimary (citable) accession number: P89462
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 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