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P42491

- RIR1_ASFB7

UniProt

P42491 - RIR1_ASFB7

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

Ba71V-045

Organism
African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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.

    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 sitei177 – 1771SubstrateBy similarity
    Sitei193 – 1931Important for hydrogen atom transferBy similarity
    Sitei200 – 2001Allosteric effector bindingBy similarity
    Binding sitei221 – 2211Substrate; via amide nitrogenBy similarity
    Sitei230 – 2301Allosteric effector bindingBy similarity
    Active sitei419 – 4191Proton acceptorBy similarity
    Active sitei421 – 4211Cysteine radical intermediateBy similarity
    Active sitei423 – 4231Proton acceptorBy similarity
    Sitei439 – 4391Important for hydrogen atom transferBy similarity
    Sitei747 – 7471Important for electron transferBy similarity
    Sitei748 – 7481Important for electron transferBy similarity
    Sitei773 – 7731Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei776 – 7761Interacts 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
    Ordered Locus Names:Ba71V-045
    ORF Names:F778R
    OrganismiAfrican swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
    Taxonomic identifieri10498 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
    Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000000624: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778Ribonucleoside-diphosphate reductase large subunitPRO_0000187227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi193 ↔ 439Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP42491.

    Expressioni

    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

    ProteinModelPortaliP42491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 1932Substrate bindingBy similarity
    Regioni419 – 4235Substrate bindingBy similarity
    Regioni613 – 6175Substrate bindingBy similarity

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42491-1 [UniParc]FASTAAdd to Basket

    « Hide

    METFFIETLA SDVYGKALNV DLDRLSQAQV KYTLQELISY CSALTILHYD    50
    YSTLAARLSV YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI 100
    FDSYIDYNRD YKLSLLGIET MKNSYLLKNK DGVIMERPQD AYMRVAIMIY 150
    GMGKVVNIKM ILLTYDLLSR HVITHASPTM FNAGTKKPQL SSCFLLNVND 200
    NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG LRSNGIQNYI 250
    MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLQMPRL KGQMAEQRLN 300
    APNLKYGLWV PDLFMEILED QIHNRGDGTW YLFSPDQAPN LHKVFDLERS 350
    QHENAHREFK KLYYQYVAEK RYTGVTTAKE IIKEWFKTVI QVGNPYIGFK 400
    DAINRKSNLS HVGTITNSNL CIEVTIPCWE GDKAEQGVCN LAAVNLAAFI 450
    RENGYDYRGL IEASGNVTEN LDNIIDNGYY PTEATRRSNM RHRPIGIGVF 500
    GLADVFASLK MKFGSPEAIA MDEAIHAALY YGAMRRSIEL AKEKGSHPSF 550
    PGSAASKGLL QPDLWVRCGD LSSSWEERVA QTTQGVLTRK SWWQLRLAAM 600
    QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY 650
    LIDDLKEIDL WTEAIQQQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI 700
    LTKHAAARNP FVSQSMSLNY YFYEPELSQV LTVLVLGWKK GLTTGSYYCH 750
    FSPGAGTQKK IIRNSEKACN ADCEACLL 778
    Length:778
    Mass (Da):87,492
    Last modified:November 1, 1995 - v1
    Checksum:i9DB88008677A877F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18466 Genomic DNA. Translation: AAA65275.1.
    RefSeqiNP_042739.1. NC_001659.1.

    Genome annotation databases

    GeneIDi1488810.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18466 Genomic DNA. Translation: AAA65275.1 .
    RefSeqi NP_042739.1. NC_001659.1.

    3D structure databases

    ProteinModelPortali P42491.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P42491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1488810.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami 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 PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the complete nucleotide sequence of African swine fever virus."
      Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E.
      Virology 208:249-278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_ASFB7
    AccessioniPrimary (citable) accession number: P42491
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 73 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