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P36602

- RIR1_SCHPO

UniProt

P36602 - RIR1_SCHPO

Protein

Ribonucleoside-diphosphate reductase large chain

Gene

cdc22

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.1 Publication

    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 sitei5 – 51Allosteric activatorBy similarity
    Binding sitei53 – 531Allosteric activatorBy similarity
    Binding sitei88 – 881Allosteric activatorBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Sitei218 – 2181Important for hydrogen atom transferBy similarity
    Sitei226 – 2261Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Sitei256 – 2561Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei427 – 4271Proton acceptorBy similarity
    Active sitei429 – 4291Cysteine radical intermediateBy similarity
    Active sitei431 – 4311Proton acceptorBy similarity
    Sitei444 – 4441Important for hydrogen atom transferBy similarity
    Sitei736 – 7361Important for electron transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei806 – 8061Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei809 – 8091Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside diphosphate kinase activity Source: PomBase
    3. protein binding Source: PomBase
    4. 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
    3. dTTP biosynthetic process Source: PomBase
    4. nucleoside diphosphate phosphorylation Source: GOC
    5. purine deoxyribonucleoside triphosphate biosynthetic process Source: PomBase
    6. purine nucleoside metabolic process Source: PomBase
    7. pyrimidine nucleoside metabolic process Source: PomBase
    8. regulation of nuclear cell cycle DNA replication Source: PomBase

    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
    Name:cdc22
    ORF Names:SPAC1F7.05
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC1F7.05.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 811811Ribonucleoside-diphosphate reductase large chainPRO_0000187201Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP36602.
    PaxDbiP36602.
    PRIDEiP36602.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit. Interacts with SPD1.2 Publications

    Protein-protein interaction databases

    BioGridi278191. 25 interactions.
    IntActiP36602. 1 interaction.
    MINTiMINT-4688885.
    STRINGi4896.SPAC1F7.05-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP36602.
    SMRiP36602. 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
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni217 – 2182Substrate bindingBy similarity
    Regioni285 – 2884Allosteric effector binding, determines substrate specificityBy similarity
    Regioni427 – 4315Substrate bindingBy similarity
    Regioni602 – 6065Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000057035.
    KOiK10807.
    OMAiANGSIQH.
    OrthoDBiEOG7C5MHR.
    PhylomeDBiP36602.

    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.

    P36602-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFVYKRDGRQ EKVAFDKITA RVSRLCYGLD SDHVDPVEIT QKVISGVYPG    50
    VTTIELDNLA AETAATMTTK HPDYAILAAR IAVSNLHKQT EKVFSTVVQQ 100
    LHDYVNPKTD KPAPMISDKI YDIVMKHKDE LDSAIIYDRD FTYNFFGFKT 150
    LERSYLLRID GKVAERPQHM IMRVAVGIHG EDIEAAIETY NLMSQRYFTH 200
    ASPTLFNAGT PRPQLSSCFL VTMKDDSIEG IYDTLKMCAM ISKTAGGIGI 250
    NIHNIRATGS YIAGTNGTSN GIVPMIRVYN NTARYVDQGG NKRPGAFAAY 300
    LEPWHADVMD FLELRKTHGN EDFRAREMFY ALWIPDLFMQ RVERNEQWTF 350
    FCPNEAPGLA DVWGDEFVAL YEKYEKENRG RRSLPAQKVW YAILQSQVET 400
    GNPFMLYKDS CNRKSNQKNV GTIRCSNLCT EIVEYSSPDE VAVCNLASVA 450
    LPTFIKDGKY NFQKLHDVVK VVTRNLNKII DVNYYPVPEA RRSNMRHRPV 500
    GLGVQGLADA FFALRLPFES AGAKKLNIQI FETIYHAALE ASCEIAQVEG 550
    TYESYEGSPA SQGILQYDMW NVNPTDLWDW AELKEKIAKH GIRNSLLVAP 600
    MPTASTSQIL GFNECFEPYT SNMYQRRVLS GEFQIVNPWL LKDLVERDLW 650
    NEDMKNKLVM LDGSIQAIPE IPQDLKDLYK TVWEISQKTV IDYAADRGPF 700
    IDQSQSLNIH LKDPSYGKIT SMHFYGWKKG LKTGMYYLRT MAASAAIKFT 750
    VDPVALRARN EESNEENKKP VIKNGKAEIS AEPTKEEIDI YNEKVLACSI 800
    KNPEACEMCS A 811
    Length:811
    Mass (Da):91,999
    Last modified:February 1, 1996 - v2
    Checksum:i6650E0EE4C2E8DF6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511N → Y in CAA46232. (PubMed:8479429)Curated
    Sequence conflicti327 – 3271E → Q in CAA46232. (PubMed:8479429)Curated
    Sequence conflicti425 – 4251C → S in CAA46232. (PubMed:8479429)Curated
    Sequence conflicti560 – 5612AS → CI in CAA46232. (PubMed:8479429)Curated
    Sequence conflicti583 – 5831L → F in CAA46232. (PubMed:8479429)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65116 Genomic DNA. Translation: CAA46232.1.
    CU329670 Genomic DNA. Translation: CAA91952.1.
    PIRiS34807.
    S62577.
    RefSeqiNP_594491.1. NM_001019920.2.

    Genome annotation databases

    EnsemblFungiiSPAC1F7.05.1; SPAC1F7.05.1:pep; SPAC1F7.05.
    GeneIDi2541695.
    KEGGispo:SPAC1F7.05.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65116 Genomic DNA. Translation: CAA46232.1 .
    CU329670 Genomic DNA. Translation: CAA91952.1 .
    PIRi S34807.
    S62577.
    RefSeqi NP_594491.1. NM_001019920.2.

    3D structure databases

    ProteinModelPortali P36602.
    SMRi P36602. Positions 15-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278191. 25 interactions.
    IntActi P36602. 1 interaction.
    MINTi MINT-4688885.
    STRINGi 4896.SPAC1F7.05-1.

    Proteomic databases

    MaxQBi P36602.
    PaxDbi P36602.
    PRIDEi P36602.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC1F7.05.1 ; SPAC1F7.05.1:pep ; SPAC1F7.05 .
    GeneIDi 2541695.
    KEGGi spo:SPAC1F7.05.

    Organism-specific databases

    PomBasei SPAC1F7.05.

    Phylogenomic databases

    eggNOGi COG0209.
    HOGENOMi HOG000057035.
    KOi K10807.
    OMAi ANGSIQH.
    OrthoDBi EOG7C5MHR.
    PhylomeDBi P36602.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Miscellaneous databases

    NextBioi 20802788.
    PROi P36602.

    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. "The cell cycle genes cdc22+ and suc22+ of the fission yeast Schizosaccharomyces pombe encode the large and small subunits of ribonucleotide reductase."
      Fernandez-Sarabia M.J., McInerny C., Harris P., Gordon C., Fantes P.
      Mol. Gen. Genet. 238:241-251(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "A novel S phase inhibitor in fission yeast."
      Woollard A., Basi G., Nurse P.
      EMBO J. 15:4603-4612(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPD1.
    4. "The Schizosaccharomyces pombe replication inhibitor Spd1 regulates ribonucleotide reductase activity and dNTPs by binding to the large Cdc22 subunit."
      Hakansson P., Dahl L., Chilkova O., Domkin V., Thelander L.
      J. Biol. Chem. 281:1778-1783(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC22.

    Entry informationi

    Entry nameiRIR1_SCHPO
    AccessioniPrimary (citable) accession number: P36602
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3