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)

Q196Z5

- RIR1_IIV3

UniProt

Q196Z5 - RIR1_IIV3

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

IIV3-065R

Organism
Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (11 Jul 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei67 – 671SubstrateBy similarity
    Sitei83 – 831Important for hydrogen atom transferBy similarity
    Sitei90 – 901Allosteric effector bindingBy similarity
    Binding sitei111 – 1111Substrate; via amide nitrogenBy similarity
    Sitei119 – 1191Allosteric effector bindingBy similarity
    Active sitei317 – 3171Proton acceptorBy similarity
    Active sitei319 – 3191Cysteine radical intermediateBy similarity
    Active sitei321 – 3211Proton acceptorBy similarity
    Sitei334 – 3341Important for hydrogen atom transferBy similarity
    Sitei597 – 5971Important for electron transferBy similarity
    Sitei598 – 5981Important for electron transferBy similarity
    Sitei625 – 6251Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei628 – 6281Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    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

    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
    ORF Names:IIV3-065R
    OrganismiInvertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus)
    Taxonomic identifieri345201 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageIridoviridaeChloriridovirus
    Virus hostiAedes vexans (Inland floodwater mosquito) (Culex vexans) [TaxID: 7163]
    Culex territans [TaxID: 42431]
    Culiseta annulata [TaxID: 332058]
    Ochlerotatus sollicitans (eastern saltmarsh mosquito) [TaxID: 310513]
    Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus) [TaxID: 329105]
    Psorophora ferox [TaxID: 7183]
    ProteomesiUP000001358: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630Ribonucleoside-diphosphate reductase large subunitPRO_0000376950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi83 ↔ 334Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    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
    Regioni82 – 832Substrate bindingBy similarity
    Regioni317 – 3215Substrate bindingBy similarity
    Regioni459 – 4635Substrate bindingBy similarity

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 2 hits.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q196Z5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITIDESRNN LFDALGLQRL KDSYMKEDES SPQERFAFIA RQFCADDEPL    50
    AQRLYDYMSQ HWLSPSSPQL SFGRTKQGLP IACFLPYLHD TARGLIDTWA 100
    EVSELSMIGG GIGLGVGIRQ PDEKSVGIIP HLRTYDASCT AYKQGQTRRG 150
    SYAAYLDISH PEILSFLNTR RVGGDHNYKL LNLHNGVNVP DSFMKKIWIL 200
    STLAPFVKMD PCPTTETLFK KAVTTLKDSR YFGADDRWLG EVSFAALAEQ 250
    LDVVNRWDLI DPHTGKVKET IKATELWERI ILTRAETGEP YIHWIDTSNR 300
    ALPQFQKNLG LSIRQSNLCS EVVLPTDETR TAVCCLASLN LDYFDKWCNN 350
    EQFYLDVATY LDNVLQYFID HAPPTLKRAV HSARSERAIG IGALGFHSYL 400
    QSKMVDIESL PAYLINKKIF KTISSHLERV NLELGELRGE APDCVGTGRR 450
    FSHMTAIAPN ATSSIIMGNT SPSCEPFRAN IYKQDTISGS FVTYNKHLKR 500
    LLEERIPDNQ ARERVWSSIK MHDGSVQHLN QLTVQEKKVF KTWPEINQLS 550
    LVMLAADRQK WIDQSQSTSL FFNPDERISY VHKIHLKAWL HGLKTLYYFR 600
    SRKILTVDKV HHTTTTADPK TENDCTFCEG 630
    Length:630
    Mass (Da):71,757
    Last modified:July 11, 2006 - v1
    Checksum:iB4F309D57AD92677
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ643392 Genomic DNA. Translation: ABF82095.1.
    RefSeqiYP_654637.1. NC_008187.1.

    Genome annotation databases

    GeneIDi4156315.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ643392 Genomic DNA. Translation: ABF82095.1 .
    RefSeqi YP_654637.1. NC_008187.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4156315.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF02867. Ribonuc_red_lgC. 2 hits.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome of invertebrate iridescent virus type 3 (mosquito iridescent virus)."
      Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A., Kutish G.F., Rock D.L.
      J. Virol. 80:8439-8449(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_IIV3
    AccessioniPrimary (citable) accession number: Q196Z5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 44 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

    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