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P50642

- RIR1_EHV4

UniProt

P50642 - RIR1_EHV4

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene
N/A
Organism
Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.By similarity

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071SubstrateBy similarity
    Sitei223 – 2231Important for hydrogen atom transferBy similarity
    Binding sitei253 – 2531Substrate; via amide nitrogenBy similarity
    Active sitei435 – 4351Proton acceptorBy similarity
    Active sitei437 – 4371Cysteine radical intermediateBy similarity
    Active sitei439 – 4391Proton acceptorBy similarity
    Sitei452 – 4521Important for hydrogen atom transferBy similarity
    Sitei764 – 7641Important for electron transferBy similarity
    Sitei765 – 7651Important for electron transferBy similarity
    Sitei784 – 7841Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei787 – 7871Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiEquine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
    Taxonomic identifieri10333 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
    Virus hostiEquus caballus (Horse) [TaxID: 9796]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 789789Ribonucleoside-diphosphate reductase large subunitPRO_0000187242Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi223 ↔ 452Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Keywords - Developmental stagei

    Early protein

    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

    Protein-protein interaction databases

    IntActiP50642. 2 interactions.
    MINTiMINT-6732615.

    Structurei

    3D structure databases

    ProteinModelPortaliP50642.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni222 – 2232Substrate bindingBy similarity
    Regioni435 – 4395Substrate bindingBy similarity
    Regioni620 – 6245Substrate bindingBy similarity

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50642-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALDFLSTDC PLGIVSDIIS NVNTIKEYGY SSELSTTLAP RPSREQVLEY    50
    ITRVVDKLKP LCRVDERLYI ACGELVHLRI KARNTDLKYW LKSSEIDLSD 100
    VVEQAILEHI DFVQKTLNSF ETSEYRDLCS LGLQSALKYE EMYLAKMRGG 150
    RLESMGQFFL RLATTATHYT MEQPAMARVL VSGEVGWTYI FRAFFTALAG 200
    QVVIPATPIM LFGGRDCGSM ASCYLLNPRV TDMNSAIPAL MEEVGPILCN 250
    RGGIGLSLQR FNTPPTEGCS RGVMALLKLL DSMTMAINSD GERPTGVCVY 300
    FEPWHADIRA ILNMRGMLAR DETVRCDNIF ACMWTPDLFF DRYQRYVDGE 350
    SGIMWTLFDD TASHLCHMYG NDFTREYERL ERCGFGIDAI PIQDMAFIIV 400
    RSAVMTGSPF LMFKDACNRH YHFDMRQRGA IMGSNLCTEI IQHADETQNG 450
    VCNLASINLP KCLALPPPNI AGVPYFDFAA LGRAAATATI FVNAMMCAST 500
    YPTVKSQKGV EENRSLGLGI QGLHTTFLML DLDMASPEAH QLNKQIAERL 550
    LLNSMKASAT LCKLGMQPFK GFEDSKYSRG ELPFDAYPNV TLTNRNAWRR 600
    LRTDIKQYGL YNSQFVAYMP TVSSSQVTES SEGFSPVYTN LFSKVTATGE 650
    VLRPNVLLMR TIRSIFPQEC ARLQALSTLE AAKWSVVGAF GDLPVGHPLS 700
    KFKTAFEYDQ TMLINMCADR AAFVDQSQSM SLFITEPADG KLPASRIMNL 750
    LVHAYKRGLK TGMYYCKIKK ATNNGVFVGG DLVCTSCSL 789
    Length:789
    Mass (Da):88,047
    Last modified:October 1, 1996 - v1
    Checksum:i7CD9A24F3147988B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75354 Genomic DNA. Translation: CAA53100.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75354 Genomic DNA. Translation: CAA53100.1 .

    3D structure databases

    ProteinModelPortali P50642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P50642. 2 interactions.
    MINTi MINT-6732615.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    [Graphical view ]
    Pfami PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences of the ribonucleotide reductase-encoding genes of equine herpesvirus 4."
      Riggio M.P., Onions D.E.
      Gene 143:217-222(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Tinkering with a viral ribonucleotide reductase."
      Lembo D., Brune W.
      Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiRIR1_EHV4
    AccessioniPrimary (citable) accession number: P50642
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3