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Q9UW15

- RIR1_NEUCR

UniProt

Q9UW15 - RIR1_NEUCR

Protein

Ribonucleoside-diphosphate reductase large chain

Gene

rnr-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      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.1 Publication

    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
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei739 – 7391Important for electron transferBy similarity
    Sitei924 – 9241Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei927 – 9271Interacts 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 large subunit
    Gene namesi
    Name:rnr-1
    ORF Names:B2A19.30, NCU03539
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 6, Linkage Group II

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261C → Y in un-24; temperature-sensitive mutant. 1 Publication
    Mutagenesisi124 – 1241V → I in un-24; temperature-sensitive mutant. 1 Publication
    Mutagenesisi125 – 1251M → I in un-24; temperature-sensitive mutant. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 929929Ribonucleoside-diphosphate reductase large chainPRO_0000187202Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    BioGridi1974838. 3 interactions.
    STRINGi5141.NCU03539.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UW15.
    SMRiQ9UW15. Positions 15-769.
    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
    Regioni604 – 6085Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000057035.
    KOiK10807.
    OMAiNKVSMKQ.
    OrthoDBiEOG7C5MHR.

    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.

    Q9UW15-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYVKKRDGRQ ERVQFDKITA RVSRLCYGLD MNHVDPVAIT QKVISGVYGG    50
    VTTAQLDDLA AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQWSLVISE 100
    LYNYVNPRTG KHSPMIAKDV YECVMRHKDE FDSAIVYDRD FNYQYFGFKT 150
    LERSYLLKLD GQIAERPQHM IMRVAVGIWG DDVERVIETY NLMSLKTFTH 200
    ASPTLFNAGT PQPQLSSCFL VDMKEDSIEG IYDTLKTCAM ISKMAGGIGL 250
    NIHRIRATGS YIAGTNGTSN GIVPMLRVFN NTARYVDQGG NKRPGAFAIY 300
    LEPWHADVFE FLDLRKNHGK EEVRARDLFL ALWIPDLFMK RVEQNGQWTL 350
    MCPHECPGLA DVYGDEFEAL YEKYEKEGKG RKTVKAQKLW YAILEAQTET 400
    GNPFMLYKDA CNRKSNQKNL GTIRSSNLCT EIIEYSAPDE VAVCNLASLA 450
    LSAFIDYENA SYDFKKLHEV TQVVVRNLNK IIDINHYPVK EAHNSNMRHR 500
    PIGVGVQGLA DAFLALRMPF DSDAASKLNI QIFETIYHAA LTASCQLAKE 550
    QGPYATYEGS PVSQGILQYD MWNVTPTNLW DWTALKADIK KYGVRNSLLL 600
    APMPTASTSQ ILGNNECFEP YTSNIYQRRV LAGEFQVVNP WLLRDLVEMG 650
    LWSDAMKNRI IAEGGSIQNI QSIPNDIKAL YKTVWEISQR TIVKMAADRG 700
    AFIDQSQSLN IHMREPTMGK ITSMHFAGWK MGLKTGMYYL RTQAAAQPIQ 750
    FTVDQEALRA TDDRVAPAHS GLKKRSPPAG TYTSIVLREN TSGPRPYAQT 800
    GVSGTSTPIG TRDVPTPAST PPPTEVPETL VQSDNRPRPL VSPAKSAGFK 850
    ADLPEPESPK ALATDPIVKT EDIGSPLLER KEGQNEDVDE DSQERDENIY 900
    SNAPLSEQQV AACAWNPGAD PSSCEMCSG 929
    Length:929
    Mass (Da):103,804
    Last modified:April 30, 2003 - v2
    Checksum:i68C47E8B21C047B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti912 – 9121A → R in AAD49743. (PubMed:10660063)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171697 Genomic DNA. Translation: AAD49743.1.
    AL390092 Genomic DNA. Translation: CAB98233.1.
    CM002237 Genomic DNA. Translation: EAA27582.1.
    PIRiT43711.
    RefSeqiXP_956818.1. XM_951725.2.
    UniGeneiNcr.20426.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000002608; EFNCRP00000002608; EFNCRG00000002605.
    GeneIDi3872956.
    KEGGincr:NCU03539.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171697 Genomic DNA. Translation: AAD49743.1 .
    AL390092 Genomic DNA. Translation: CAB98233.1 .
    CM002237 Genomic DNA. Translation: EAA27582.1 .
    PIRi T43711.
    RefSeqi XP_956818.1. XM_951725.2.
    UniGenei Ncr.20426.

    3D structure databases

    ProteinModelPortali Q9UW15.
    SMRi Q9UW15. Positions 15-769.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1974838. 3 interactions.
    STRINGi 5141.NCU03539.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000002608 ; EFNCRP00000002608 ; EFNCRG00000002605 .
    GeneIDi 3872956.
    KEGGi ncr:NCU03539.

    Phylogenomic databases

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

    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. "An osmotic-remedial, temperature-sensitive mutation in the allosteric activity site of ribonucleotide reductase in Neurospora crassa."
      Smith M.L., Hubbard S.P., Jacobson D.J., Micali O.C., Glass N.L.
      Mol. Gen. Genet. 262:1022-1035(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF CYS-26; VAL-124 AND MET-125.
      Strain: Oak Ridge.
    2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    3. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiRIR1_NEUCR
    AccessioniPrimary (citable) accession number: Q9UW15
    Secondary accession number(s): Q7RXZ9, Q9P3G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 110 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3