Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O61065

- RIR1_CRYPV

UniProt

O61065 - RIR1_CRYPV

Protein

Ribonucleoside-diphosphate reductase large chain

Gene

RNR1

Organism
Cryptosporidium parvum
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    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 sitei52 – 521Allosteric activatorBy similarity
    Binding sitei87 – 871Allosteric activatorBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Sitei216 – 2161Important for hydrogen atom transferBy similarity
    Sitei224 – 2241Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
    Sitei254 – 2541Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei425 – 4251Proton acceptorBy similarity
    Active sitei427 – 4271Cysteine radical intermediateBy similarity
    Active sitei429 – 4291Proton acceptorBy similarity
    Sitei442 – 4421Important for hydrogen atom transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei798 – 7981Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei801 – 8011Interacts 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 R1 subunit
    Gene namesi
    Name:RNR1
    OrganismiCryptosporidium parvum
    Taxonomic identifieri5807 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaCryptosporidiidaeCryptosporidium

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 803803Ribonucleoside-diphosphate reductase large chainPRO_0000187196Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi216 ↔ 442Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Structurei

    3D structure databases

    ProteinModelPortaliO61065.
    SMRiO61065. Positions 15-789.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9191ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni215 – 2162Substrate bindingBy similarity
    Regioni283 – 2864Allosteric effector binding, determines substrate specificityBy similarity
    Regioni425 – 4295Substrate bindingBy similarity
    Regioni603 – 6075Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.

    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.

    O61065-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYVVNRKGEE EPVSFDQILS RITKLSYGLH PLVDPARVTQ AVINGLYSGI    50
    KTSELDELAS QTCAYMAATH NDFSKLAARI STSNLHKNTS SDIGDVASQL 100
    YNFKDNQGCP APLISKPVYD FIMENRERIN SKIDFSKDFE YDYFAFKTLE 150
    RSYLLKIDNK VVERPQHLLM RVSCGIHCGD IEAALETYEL LSQKYFTHAT 200
    PTLFNSGTPR PQMSSCFLLR IPEDSINGIF DTLTKCANIS KTAGGLGVAV 250
    SNIRGTGSYI RGTNGRSNGL IPMLRVYNDT ARYIDQGGGK RKGAIAIYLE 300
    PWHVDVVEFI EIRKNHGKEE MRCRDLFPAL WVPDLFMERV EKDQDWTLMC 350
    PDECRGLQDV WGDDFKKLYE EYEKQGRGRK TMKAQKLWFL ILQAQIETGT 400
    PFICYKDAAN SKSNQKNLGT IVSSNLCTEI IEYTSTDEVA VCNLASIGLP 450
    KFVDKNNKTF DFDKLKEVTK VITRNLNKLI DVGYYSLKEC KKSNLRHRPL 500
    GIGIQGLADC FMMLRMPYES EGAKKLNKQI FEVIYYAALD ASCELAEKYG 550
    PYETYSGSPA SKGILQFDMW GVTPDSGLCD WDLLKDRISK HGIRNSLLIS 600
    PMPTASTSQI LGNNESFEPF TSNIYHRRVL SGEFFVVNPH LLNDLLELGL 650
    WDDRLKQNII ANNGSIQNIL TIPEDIRELY KTVWEIKQKT VIDMAADRGP 700
    YVCQSQSLNI HMENANFAKL SSMHFYGWKK GLKTGIYYLR TQSATRPIQF 750
    TVDQQLLKSE TKEKDSLETN KRQALEPEAQ KLIACPLRPT NMKDDEECMM 800
    CSG 803
    Length:803
    Mass (Da):91,123
    Last modified:August 14, 2001 - v2
    Checksum:i9DBE7F2AC337F97F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043243 Genomic DNA. Translation: AAC12280.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043243 Genomic DNA. Translation: AAC12280.2 .

    3D structure databases

    ProteinModelPortali O61065.
    SMRi O61065. Positions 15-789.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0209.

    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. "Molecular characterization of ribonucleotide reductase from Cryptosporidium parvum."
      Akiyoshi D.E., Balakrishnan R., Huettinger C., Widmer G., Tzipori S.
      DNA Seq. 13:167-172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GCH1.

    Entry informationi

    Entry nameiRIR1_CRYPV
    AccessioniPrimary (citable) accession number: O61065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3