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P28846

- RIR1_EHV1B

UniProt

P28846 - RIR1_EHV1B

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

21

Organism
Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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 sitei208 – 2081SubstrateBy similarity
    Sitei224 – 2241Important for hydrogen atom transferBy similarity
    Binding sitei254 – 2541Substrate; via amide nitrogenBy similarity
    Active sitei436 – 4361Proton acceptorBy similarity
    Active sitei438 – 4381Cysteine radical intermediateBy similarity
    Active sitei440 – 4401Proton acceptorBy similarity
    Sitei453 – 4531Important for hydrogen atom transferBy similarity
    Sitei765 – 7651Important for electron transferBy similarity
    Sitei766 – 7661Important for electron transferBy similarity
    Sitei785 – 7851Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei788 – 7881Interacts 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
    Gene namesi
    Name:21
    OrganismiEquine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus)
    Taxonomic identifieri31520 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
    Virus hostiEquus caballus (Horse) [TaxID: 9796]
    ProteomesiUP000001189: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 790790Ribonucleoside-diphosphate reductase large subunitPRO_0000187241Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi224 ↔ 453Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP28846.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP28846.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni223 – 2242Substrate bindingBy similarity
    Regioni436 – 4405Substrate bindingBy similarity
    Regioni621 – 6255Substrate 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.

    P28846-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALNFLQSDC PLAIIQDVIS RVDAISDYGY ANELSTTLPP RPSRSQVLEY    50
    ITRVVDTLKP RCRVDERLYV VCGELVHLRI RTRNVEDLKY WLNSTEIALN 100
    EIVEKDILDH LDFIQRTLHA FESSEYRELC ALGLQSALKY EEMYLAKMRG 150
    GRIESMGQFF LRLATTATHY TMEEPAMARV LVSGEVGWTY IFKAYFTALA 200
    GQVLIPATPI MLFGGRDCGS LASCYLLNPR VTDMNSAMLA LMEEAGPILC 250
    NRGGIGLSLQ RFNTPPKEGC SRGVMALLKL IDSMTMAINS DGERPTGVCV 300
    YFEPWHADIR AILNMRGMLA RDETVRCDNI FACMWTPDLF FDRYQRYLDG 350
    ESGVMWTLFD DTASHLCHMY GKEFEEEYER LEQCGFGVDS IPIQDMAFII 400
    VRSAVMTGSP FLMFKDACNK HYHFDLRRKG AIMGSNLCTE IIQHADETQN 450
    GVCNLASINL PKCLAIPPPH TAGVPYFDFA ALGRAAATAT IFVNSMMRAG 500
    TYPTVKSQRG VDENRSLGLG IQGLHTAFLM LDLDMASPEA RQLNKQIAER 550
    LLLNSMKASA TLCRLGMKPF KGFEDSKYSL GELPFDSYPG VTLANRNAWR 600
    RLRTEIKQHG LYNSQFVAYM PTVSSSQVTE SSEGFSPVYT NLFSKVTATG 650
    EVLRPNLLLM RTIRSIFPRE CARLQALSTL EMAQWSVVGA FGDLPVGHPL 700
    SKFKTAFEYD QRTLIDMCAD RAPFVDQSQS MSLFITEPAD GKLPASKIMS 750
    LLVHAYKRGL KTGMYYCKIK KATNNGVFVG GDLVCTSCSL 790
    Length:790
    Mass (Da):88,399
    Last modified:December 1, 1992 - v1
    Checksum:iD8A21677716F5844
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY665713 Genomic DNA. Translation: AAT67278.1.
    PIRiD36797. WMBEA2.
    RefSeqiYP_053066.1. NC_001491.2.

    Genome annotation databases

    GeneIDi1487540.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY665713 Genomic DNA. Translation: AAT67278.1 .
    PIRi D36797. WMBEA2.
    RefSeqi YP_053066.1. NC_001491.2.

    3D structure databases

    ProteinModelPortali P28846.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P28846.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1487540.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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_EHV1B
    AccessioniPrimary (citable) accession number: P28846
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 73 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

    Documents

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

    External Data

    Dasty 3