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P0C8H7

- RIR1_ASFK5

UniProt

P0C8H7 - RIR1_ASFK5

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

Ken-057

Organism
African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (25 Nov 2008)
      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 sitei178 – 1781SubstrateBy similarity
    Sitei194 – 1941Important for hydrogen atom transferBy similarity
    Sitei201 – 2011Allosteric effector bindingBy similarity
    Binding sitei222 – 2221Substrate; via amide nitrogenBy similarity
    Sitei231 – 2311Allosteric effector bindingBy similarity
    Active sitei420 – 4201Proton acceptorBy similarity
    Active sitei422 – 4221Cysteine radical intermediateBy similarity
    Active sitei424 – 4241Proton acceptorBy similarity
    Sitei440 – 4401Important for hydrogen atom transferBy similarity
    Sitei748 – 7481Important for electron transferBy similarity
    Sitei749 – 7491Important for electron transferBy similarity
    Sitei774 – 7741Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei777 – 7771Interacts 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:Ken-057
    OrganismiAfrican swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV)
    Taxonomic identifieri561445 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
    Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
    Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
    Phacochoerus africanus (Warthog) [TaxID: 41426]
    Potamochoerus larvatus (Bushpig) [TaxID: 273792]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000000861: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 779779Ribonucleoside-diphosphate reductase large subunitPRO_0000355219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi194 ↔ 440Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP0C8H7.

    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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni193 – 1942Substrate bindingBy similarity
    Regioni420 – 4245Substrate bindingBy similarity
    Regioni614 – 6185Substrate 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.

    P0C8H7-1 [UniParc]FASTAAdd to Basket

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    MENFFIVKKL ASDTYGKALN VDLDRLLQAQ NKYTLQELIS YCSALTILHY    50
    DYSTLAARLS VYLLHQSTAS SFSEAVSLQA AQSCSRLSPQ FVDVVYKYKA 100
    IFDSYIDYSR DYKLTLLGIE TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI 150
    YGMGRVVNMK MILLTYDLLS RHVITHASPT MFNAGTKKPQ LSSCFLLNVN 200
    DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS GLRSNGIQNY 250
    IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL 300
    NAPNLKYGLW VPDLFMEILE DQIHDRGDGT WYLFSPDQAP NLHKVFDLER 350
    SRHKNAHREF RKLYYQYVAE KRYTGVTTAK EIIKEWFKTV IQVGNPYIGF 400
    KDAINRKSNL SHVGTITNSN LCIEITIPCW EGSEAEQGVC NLAAVNLAAF 450
    IRENSYDYRG LIEAAGNVTE NLDNIIDNGY YPTEATRRSN MRHRPIGIGV 500
    FGLADVFASF KMKFGSPEAI AMDEAIHAAL YYGAMRRSVE LAKEKGSHPS 550
    FPGSAASKGL LQPDLWVRCD DLVFSWEERV AQTTQGVLTP KKWWQLRLAA 600
    MQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIVLNK 650
    YLIDDLKEIN LWTEAIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK 700
    ILTKHAAARN PFVSQSMSLN YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC 750
    HFSPGAGTQK KIIRNSEKAC SADCEACLL 779
    Length:779
    Mass (Da):87,767
    Last modified:November 25, 2008 - v1
    Checksum:i7FF7134ECDC5C861
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY261360 Genomic DNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY261360 Genomic DNA. No translation available.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P0C8H7.

    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.
    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. "African swine fever virus genomes."
      Kutish G.F., Rock D.L.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_ASFK5
    AccessioniPrimary (citable) accession number: P0C8H7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 22 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