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P12848

- RIR1_VACCW

UniProt

P12848 - RIR1_VACCW

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

VACWR073

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Oct 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. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.By similarity

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

    Cofactori

    Mg2+. Maximal ribonucleotide reductase activity requires the presence of magnesium ions.1 Publication

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, whereas dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.By similarity

    pH dependencei

    Optimum pH is 8.0 and above.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei202 – 2021SubstrateBy similarity
    Sitei218 – 2181Important for hydrogen atom transferBy similarity
    Sitei226 – 2261Allosteric effector bindingBy similarity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Sitei256 – 2561Allosteric effector bindingBy similarity
    Active sitei427 – 4271Proton acceptorBy similarity
    Active sitei429 – 4291Cysteine radical intermediateBy similarity
    Active sitei431 – 4311Proton acceptorBy similarity
    Sitei444 – 4441Important for hydrogen atom transferBy similarity
    Sitei735 – 7351Important for electron transferBy similarity
    Sitei736 – 7361Important for electron transferBy similarity
    Sitei766 – 7661Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei769 – 7691Interacts 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, Magnesium, 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 large subunit
    Gene namesi
    Ordered Locus Names:VACWR073
    ORF Names:I4L
    OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
    Taxonomic identifieri10254 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000000344: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 771771Ribonucleoside-diphosphate reductase large subunitPRO_0000187232Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi218 ↔ 444Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Expressed early in the viral replicative cycle.1 Publication

    Keywords - Developmental stagei

    Early protein

    Interactioni

    Subunit structurei

    Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-2158N.
    IntActiP12848. 1 interaction.
    MINTiMINT-131002.

    Structurei

    3D structure databases

    ProteinModelPortaliP12848.
    SMRiP12848. Positions 15-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 2182Substrate bindingBy similarity
    Regioni427 – 4315Substrate bindingBy similarity
    Regioni602 – 6065Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P12848-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFVIKRNGYK ENVMFDKITS RIRKLCYGLN TDHIDPIKIA MKVIQGIYNG    50
    VTTVELDTLA AEIAATCTTQ HPDYAILAAR IAVSNLHKET KKLFSEVMED 100
    LFNYVNPKNG KHSPIISSIT MDIVNKYKDK LNSVIIYERD FSYNYFGFKT 150
    LEKSYLLKIN NKIVERPQHM LMRVAVGIHQ WDIDSAIETY NLLSEKWFTH 200
    ASPTLFNAGT SRHQMSSCFL LNMIDDSIEG IYDTLKRCAL ISKMAGGIGL 250
    SISNIRASGS YISGTNGISN GIIPMLRVYN NTARYIDQGG NKRPGVMAIY 300
    LEPWHSDIMA FLDLKKNTGN EEHRTRDLFI ALWIPDLFMK RVKDDGEWSL 350
    MCPDECPGLD NVWGDEFERL YTLYERERRY KSIIKARVVW KAIIESQIET 400
    GTPFILYKDA CNKKSNQQNL GTIKCSNLCT EIIQYADANE VAVCNLASVA 450
    LNMFVIDGRF DFLKLKDVVK VIVRNLNKII DINYYPIPEA EISNKRHRPI 500
    GIGVQGLADA FILLNYPFDS LEAQDLNKKI FETIYYGALE ASCELAEKEG 550
    PYDTYVGSYA SNGILQYDLW NVVPSDLWNW EPLKDKIRTY GLRNSLLVAP 600
    MPTASTAQIL GNNESVEPYT SNIYTRRVLS GEFQVVNPHL LRVLTERKLW 650
    NDEIKNRIMA DGGSIQNTNL PEDIKRVYKT IWEIPQKTII KMAADRGAFI 700
    DQSQSMNIHI ADPSYSKLTS MHFYGWSLGL KTGMYYLRTK PASAPIQFTL 750
    DKDKIKPPVV CDSEICTSCS G 771
    Length:771
    Mass (Da):87,738
    Last modified:October 1, 1989 - v1
    Checksum:i6CA07F0C58F6A8F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti447 – 4471A → G in AAA48274. (PubMed:3284177)Curated
    Sequence conflicti467 – 4671D → V in AAA48274. (PubMed:3284177)Curated
    Sequence conflicti526 – 5261L → I in AAA48274. (PubMed:3284177)Curated
    Sequence conflicti601 – 6066MPTAST → LPLHQH in AAA48274. (PubMed:3284177)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03399 Genomic DNA. Translation: AAB59806.1.
    M20299 Genomic DNA. Translation: AAA48274.1.
    AY243312 Genomic DNA. Translation: AAO89352.1.
    PIRiA28611. WZVZH4.
    RefSeqiYP_232955.1. NC_006998.1.

    Genome annotation databases

    GeneIDi3707606.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03399 Genomic DNA. Translation: AAB59806.1 .
    M20299 Genomic DNA. Translation: AAA48274.1 .
    AY243312 Genomic DNA. Translation: AAO89352.1 .
    PIRi A28611. WZVZH4.
    RefSeqi YP_232955.1. NC_006998.1.

    3D structure databases

    ProteinModelPortali P12848.
    SMRi P12848. Positions 15-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-2158N.
    IntActi P12848. 1 interaction.
    MINTi MINT-131002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3707606.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment."
      Schmitt J.F.C., Stunnenberg H.G.
      J. Virol. 62:1889-1897(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    2. "Nucleotide sequence and molecular genetic analysis of the large subunit of ribonucleotide reductase encoded by vaccinia virus."
      Tengelsen L.A., Slabaugh M.B., Bibler J.K., Hruby D.E.
      Virology 164:121-131(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
      Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Vaccinia virus ribonucleotide reductase expression and isolation of the recombinant large subunit."
      Slabaugh M.B., Davis R.E., Roseman N.A., Mathews C.K.
      J. Biol. Chem. 268:17803-17810(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.

    Entry informationi

    Entry nameiRIR1_VACCW
    AccessioniPrimary (citable) accession number: P12848
    Secondary accession number(s): Q76ZU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 91 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

    Allosteric enzyme, 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