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P09853

- RIR1_HHV23

UniProt

P09853 - RIR1_HHV23

Protein

Ribonucleoside-diphosphate reductase large subunit

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 84 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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 sitei573 – 5731SubstrateBy similarity
    Sitei589 – 5891Important for hydrogen atom transferBy similarity
    Binding sitei619 – 6191Substrate; via amide nitrogenBy similarity
    Active sitei798 – 7981Proton acceptorBy similarity
    Active sitei800 – 8001Cysteine radical intermediateBy similarity
    Active sitei802 – 8021Proton acceptorBy similarity
    Sitei815 – 8151Important for hydrogen atom transferBy similarity
    Sitei1118 – 11181Important for electron transferBy similarity
    Sitei1119 – 11191Important for electron transferBy similarity
    Sitei1139 – 11391Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei1142 – 11421Interacts 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    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)
    Alternative name(s):
    Ribonucleotide reductase 136 kDa subunit
    Ribonucleotide reductase large 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 – 11441144Ribonucleoside-diphosphate reductase large subunitPRO_0000187237Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi589 ↔ 815Redox-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

    Structurei

    3D structure databases

    ProteinModelPortaliP09853.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni588 – 5892Substrate bindingBy similarity
    Regioni798 – 8025Substrate bindingBy similarity
    Regioni975 – 9795Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi151 – 1599Poly-Pro
    Compositional biasi224 – 2318Poly-Asp

    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.

    P09853-1 [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
    DEDTGSGSET LSRSSSIWAA GATDDDDSDS DSRSDDSVQP DVVVRRRWSD 250
    GPAPVAFPKP RRPGDSPGNP GLGAGTGPGS ATDPRASADS DSAAHAAAPQ 300
    ADVAPVLDSQ PTVGTDPGYP VPLELTPENA EAVARFLGDA VDREPALMLE 350
    YFCRCAREES KRVPPRTFGS APRLTEDDFG LLNYALAEMR RLCLDLPPVP 400
    PNAYTPYHLR EYATRLVNGF KPLVRRSARL YRILGILVHL RIRTREASFE 450
    EWMRSKEVDL DFGLTERLRE HEAQLMILAQ ALNPYDCLIH STPNTLVERG 500
    LQSALKYEEF YLKRFGGHYM ESVFQMYTRI AGFLACRATR GMRHIALGRQ 550
    GSWWEMFKFF FHRLYDHQIV PSTPAMLNLG TRNYYTSSCY LVNPQATTNQ 600
    ATLRAITGNV SAILARNGGI GLCMQAFNDA SPGTASIMPA LKVLDSLVAA 650
    HNKQSTRPTG ACVYLEPWHS DVRAVLRMKG VLAGEEAQRC DNIFSALWMP 700
    DLFFKRLIRH LDGEKNVTWS LFDRDTSMSL ADFHGEEFEK LYEHLEAMGF 750
    GETIPIQDLA YAIVRSAATT GSPFIMFKDA VNRHYIYDTQ GAAIAGSNLC 800
    TEIVHPSSKR SSGVCNLGSV NLARCVSRRT FDFGMLRDAV QACVLMVNIM 850
    IDSTLQPTPQ CARGHDNLRS MGIGMQGLHT ACLKMGLDLE SAEFRDLNTH 900
    IAEVMLLAAM KTSNALCVRG ARPFSHFKRS MYRAGRFHWE RFSNASPRYE 950
    GEWEMLRQSM MKHGLRNSQF IALMPTAASA QISDVSEGFA PLFTNLFSKV 1000
    TRDGETLRPN TLLLKELERT FGGKRLLDAM DGLEAKQWSV AQALPCLDPA 1050
    HPLRRFKTAF DYDQELLIDL CADRAPYVDH SQSMTLYVTE KADGTLPAST 1100
    LVRLLVHAYK RGLKTGMYYC KVRKATNSGV FAGDDNIVCT SCAL 1144
    Length:1,144
    Mass (Da):125,093
    Last modified:October 1, 1996 - v2
    Checksum:i4771481C3103FC78
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12700 Genomic DNA. Translation: AAA45806.1.
    X00048 Genomic DNA. Translation: CAA24929.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12700 Genomic DNA. Translation: AAA45806.1 .
    X00048 Genomic DNA. Translation: CAA24929.1 .

    3D structure databases

    ProteinModelPortali P09853.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P09853.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3'-coterminal transcripts."
      Swain M.A., Galloway D.A.
      J. Virol. 57:802-808(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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] OF 981-1144.
    3. "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] OF 1036-1144.
    4. "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_HHV23
    AccessioniPrimary (citable) accession number: P09853
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 84 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