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P20503

- RIR1_VACCC

UniProt

P20503 - RIR1_VACCC

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

I4L

Organism
Vaccinia virus (strain Copenhagen) (VACV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

    Catalytic activityi

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

    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, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.By similarity

    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, 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
    ORF Names:I4L
    OrganismiVaccinia virus (strain Copenhagen) (VACV)
    Taxonomic identifieri10249 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008269: 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_0000187231Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP20503.

    Expressioni

    Inductioni

    Expressed early in the viral replicative cycle.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP20503.
    SMRiP20503. 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.

    P20503-1 [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
    DKDKIKPLVV CDSEICTSCS G 771
    Length:771
    Mass (Da):87,754
    Last modified:February 1, 1991 - v1
    Checksum:i6CA07F0C58EDC4F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35027 Genomic DNA. Translation: AAA48059.1.
    PIRiI42510. WMVZ9J.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35027 Genomic DNA. Translation: AAA48059.1 .
    PIRi I42510. WMVZ9J.

    3D structure databases

    ProteinModelPortali P20503.
    SMRi P20503. Positions 15-752.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P20503.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Appendix to 'The complete DNA sequence of vaccinia virus'."
      Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., Paoletti E.
      Virology 179:517-563(1990)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_VACCC
    AccessioniPrimary (citable) accession number: P20503
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 79 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

    Documents

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

    External Data

    Dasty 3