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Q6GZT8

- RIR1_FRG3G

UniProt

Q6GZT8 - RIR1_FRG3G

Protein

Putative ribonucleoside-diphosphate reductase large subunit

Gene

FV3-038R

Organism
Frog virus 3 (isolate Goorha) (FV-3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    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 sitei60 – 601SubstrateBy similarity
    Sitei75 – 751Important for hydrogen atom transferBy similarity
    Sitei82 – 821Allosteric effector bindingBy similarity
    Binding sitei103 – 1031Substrate; via amide nitrogenBy similarity
    Sitei112 – 1121Allosteric effector bindingBy similarity
    Active sitei256 – 2561Proton acceptorBy similarity
    Active sitei258 – 2581Cysteine radical intermediateBy similarity
    Active sitei260 – 2601Proton acceptorBy similarity
    Sitei273 – 2731Important for hydrogen atom transferBy similarity
    Sitei534 – 5341Important for electron transferBy similarity
    Sitei535 – 5351Important for electron transferBy similarity
    Sitei560 – 5601Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei563 – 5631Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. 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:
    Putative ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase large subunit
    Gene namesi
    ORF Names:FV3-038R
    OrganismiFrog virus 3 (isolate Goorha) (FV-3)
    Taxonomic identifieri654924 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageIridoviridaeRanavirus
    Virus hostiAmbystoma (mole salamanders) [TaxID: 8295]
    Hyla versicolor (chameleon treefrog) [TaxID: 30343]
    Lithobates pipiens (Northern leopard frog) (Rana pipiens) [TaxID: 8404]
    Notophthalmus viridescens (Eastern newt) (Triturus viridescens) [TaxID: 8316]
    Rana sylvatica (Wood frog) [TaxID: 45438]
    ProteomesiUP000008770: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 565565Putative ribonucleoside-diphosphate reductase large subunitPRO_0000410591Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi75 ↔ 273Redox-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

    Structurei

    3D structure databases

    ProteinModelPortaliQ6GZT8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni74 – 752Substrate bindingBy similarity
    Regioni256 – 2605Substrate bindingBy similarity
    Regioni400 – 4045Substrate bindingBy similarity

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR000788. RNR_lg_C.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.

    Sequencei

    Sequence statusi: Complete.

    Q6GZT8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSAVSFPIT SQASDMLSKF YGSDLGSLYG TLAEKYSGGK PELAEKLRDY    50
    ACKGWFGYSS PILTSVTGSG LPISCFLLYV PDTIEGLVDH TSELRWLSVM 100
    GGGVAGHWDD VRGPSAKSCG TIPFLHTVDA DMSAYWQGKV RRGSYAAYMS 150
    ISHPDLIEFI TMRTPTGDVN RKNLNLHHGV NITDTFMRCV ERGENWDLVD 200
    PKSGAVAHTV SARELWERIL ETRFRTGEPY LNFIDTANRG LHPALKRKGL 250
    KIRGSNLCNE IHLPTAADRT AVCCLSSVNL ERYDEWRETD LVECLVEMLD 300
    NVIQTFVDEA PLKTPHTARA VRSAAGERSI GLGAMGWARY LQKHRIPFDS 350
    EEAVRLTGII FRGIKSAAVR ATRALAKERG EAPDLTGYGV RNAHLLAVAP 400
    NANSALLLGT SPSVEPEIGA AYVHRTRVGS HQAVNPYLKR DLESLGLDTE 450
    EVWDSIVSNK GSVQHIAALP DSLKKVYKTS FEMDQRVIVR QAAERQRHLC 500
    QGQSLNLFFP IGADKTNLSD VHRLAWKSGC KGLYYLRTCA GRTGHKIFEA 550
    KKNPEKTEEC TACQG 565
    Length:565
    Mass (Da):62,363
    Last modified:July 19, 2004 - v1
    Checksum:i790187621FAFC2E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY548484 Genomic DNA. Translation: AAT09697.1.
    RefSeqiYP_031616.1. NC_005946.1.

    Genome annotation databases

    GeneIDi2947817.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY548484 Genomic DNA. Translation: AAT09697.1 .
    RefSeqi YP_031616.1. NC_005946.1.

    3D structure databases

    ProteinModelPortali Q6GZT8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2947817.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR000788. RNR_lg_C.
    [Graphical view ]
    Pfami PF02867. Ribonuc_red_lgC. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae)."
      Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.
      Virology 323:70-84(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_FRG3G
    AccessioniPrimary (citable) accession number: Q6GZT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 41 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