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Q8SR37

- RIR1_ENCCU

UniProt

Q8SR37 - RIR1_ENCCU

Protein

Ribonucleoside-diphosphate reductase large chain

Gene

ECU10_0920

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. 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 to separate specificity and activation sites on the large subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei196 – 1961SubstrateBy similarity
    Sitei212 – 2121Important for hydrogen atom transferBy similarity
    Sitei220 – 2201Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei241 – 2411Substrate; via amide nitrogenBy similarity
    Sitei250 – 2501Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei420 – 4201Proton acceptorBy similarity
    Active sitei422 – 4221Cysteine radical intermediateBy similarity
    Active sitei424 – 4241Proton acceptorBy similarity
    Sitei437 – 4371Important for hydrogen atom transferBy similarity
    Sitei729 – 7291Important for electron transferBy similarity
    Sitei730 – 7301Important for electron transferBy similarity
    Sitei763 – 7631Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei766 – 7661Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

    GO - Biological processi

    1. deoxyribonucleotide biosynthetic process Source: UniProtKB
    2. 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 chain (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase
    Gene namesi
    Ordered Locus Names:ECU10_0920
    OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
    Taxonomic identifieri284813 [NCBI]
    Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
    ProteomesiUP000000819: Chromosome X

    Organism-specific databases

    EuPathDBiMicrosporidiaDB:ECU10_0920.

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 768768Ribonucleoside-diphosphate reductase large chainPRO_0000187200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi212 ↔ 437Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ8SR37.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.By similarity

    Protein-protein interaction databases

    STRINGi6035.ECU10_0920.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8SR37.
    SMRiQ8SR37. Positions 79-734.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni211 – 2122Substrate bindingBy similarity
    Regioni279 – 2824Allosteric effector binding, determines substrate specificityBy similarity
    Regioni420 – 4245Substrate bindingBy similarity
    Regioni595 – 5995Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000057035.
    KOiK10807.
    OMAiDELIHQR.
    OrthoDBiEOG7C5MHR.

    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.

    Q8SR37-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENFSNSKRI KSEKLGIDLI RSRIEGYVKD LKLRHVDVDE LVERIVSGWC    50
    EDMTRKETID YCSETAASMI TKHPEYGQIS SRIIVSYIHE ITMDSFVEKI 100
    KYIQKHRGMV SEEMYGIILE HGETIEGMIN YENDFLFSYF GILTLMKSYL 150
    IKVGEEIIER PQDMFMRVAL QIHKTDFEKV REVYNLLSGH YFTHATPTLY 200
    NSCLKNPQLA SCFLITPRED SIEGVYHMIN QAAIITKYSG GIGLNLHGIR 250
    SKGSSLRSTG GRSNGIIPLI QVLNATKRYI NQGAERRPGS IAIFLEPWHM 300
    EIFDFLELRK NTGPEEFRAR DIFTALWIND LFMERVKNNE EWSLFCPSQA 350
    VGLSDVWGEE FNALYCKYEK TISRTVVPAQ KLWKAIIEAQ IETGTPYMCY 400
    KDACNRLSNQ QHLGTIKSSN LCAEIVEYSS GEETSVCNLA SICLPMFVKD 450
    GWFDFEAFRR VVKILTVNLN RVIDFNYYPV EEARRSNMRN RPIGIGVQGL 500
    ADLFAILRLA FESDGARSLN QDIFEAMYYS AMEASCELAE KEGPFPSYEG 550
    SPISKGIFHF ELAGRKASGN WDWEGLRERI RRHGVRNSLL IALMPTAGTS 600
    QIFGNNEAFE PHASNIYTRR THAGEFQIVN QHLVNDLVRL GLWSYEMKNL 650
    VIENEGSIQN ITSIPHEIRE IYKTAWEIKM KSVIDLAADR QVFVDQSQSL 700
    NIFIAKPTYS QLTSMHFYGY HCGLKTGMYY LRTRPITSAI KFTVDKKLAE 750
    KTLSSMNDTD DPCSMCSS 768
    Length:768
    Mass (Da):87,941
    Last modified:June 1, 2002 - v1
    Checksum:i3E6BF6826805E20D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590449 Genomic DNA. Translation: CAD25811.1.
    RefSeqiNP_586207.1. NM_001042040.1.

    Genome annotation databases

    GeneIDi859856.
    KEGGiecu:ECU10_0920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590449 Genomic DNA. Translation: CAD25811.1 .
    RefSeqi NP_586207.1. NM_001042040.1.

    3D structure databases

    ProteinModelPortali Q8SR37.
    SMRi Q8SR37. Positions 79-734.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6035.ECU10_0920.

    Proteomic databases

    PRIDEi Q8SR37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 859856.
    KEGGi ecu:ECU10_0920.

    Organism-specific databases

    EuPathDBi MicrosporidiaDB:ECU10_0920.

    Phylogenomic databases

    eggNOGi COG0209.
    HOGENOMi HOG000057035.
    KOi K10807.
    OMAi DELIHQR.
    OrthoDBi EOG7C5MHR.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GB-M1.

    Entry informationi

    Entry nameiRIR1_ENCCU
    AccessioniPrimary (citable) accession number: Q8SR37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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