RIR1_VZVO
ID RIR1_VZVO Reviewed; 775 AA.
AC Q4JQV6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026};
DE Short=R1 {ECO:0000255|HAMAP-Rule:MF_04026};
DE EC=1.17.4.1 {ECO:0000255|HAMAP-Rule:MF_04026};
DE AltName: Full=Ribonucleotide reductase large subunit {ECO:0000255|HAMAP-Rule:MF_04026};
GN Name=RIR1 {ECO:0000255|HAMAP-Rule:MF_04026}; ORFNames=ORF19;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
RN [3]
RP REVIEW.
RX PubMed=18990579; DOI=10.1016/j.tibs.2008.09.008;
RA Lembo D., Brune W.;
RT "Tinkering with a viral ribonucleotide reductase.";
RL Trends Biochem. Sci. 34:25-32(2009).
CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the
CC precursors necessary for viral DNA synthesis. Allows virus growth in
CC non-dividing cells, as well as reactivation from latency in infected
CC hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000255|HAMAP-Rule:MF_04026}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04026};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_04026}.
CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit
CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit
CC protein complex are also active, composed of (R1)n(R2)n.
CC {ECO:0000255|HAMAP-Rule:MF_04026}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000255|HAMAP-Rule:MF_04026}.
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DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57685.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57756.1; -; Genomic_DNA.
DR RefSeq; NP_040142.1; NC_001348.1.
DR SMR; Q4JQV6; -.
DR IntAct; Q4JQV6; 20.
DR GeneID; 1487716; -.
DR KEGG; vg:1487716; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0019046; P:release from viral latency; IEA:UniProtKB-KW.
DR HAMAP; MF_04026; HSV_RIR1; 1.
DR InterPro; IPR034717; HSV_RIR1.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; DNA replication; Early protein;
KW Nucleotide-binding; Oxidoreductase; Viral latency;
KW Viral reactivation from latency.
FT CHAIN 1..775
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000385163"
FT ACT_SITE 427
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 429
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 427..431
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT BINDING 606..610
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 216
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 444
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 750
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 751
FT /note="Important for electron transfer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 770
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT SITE 773
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
FT DISULFID 216..444
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04026"
SQ SEQUENCE 775 AA; 86828 MW; 187695A65EB91B9D CRC64;
MEFKRIFNTV HDIINRLCQH GYKEYIIPPE STTPVELMEY ISTIVSKLKA VTRQDERVYR
CCGELIHCRI NLRSVSMETW LTSPILCLTP RVRQAIEGRR DEIRRAILEP FLKDQYPALA
TLGLQSALKY EDFYLTKLEE GKLESLCQFF LRLAATVTTE IVNLPKIATL IPGINDGYTW
TDVCRVFFTA LACQKIVPAT PVMMFLGRET GATASCYLMD PESITVGRAV RAITGDVGTV
LQSRGGVGIS LQSLNLIPTE NQTKGLLAVL KLLDCMVMAI NSDCERPTGV CVYIEPWHVD
LQTVLATRGM LVRDEIFRCD NIFCCLWTPD LFFERYLSYL KGASNVQWTL FDNRADILRT
LHGEAFTSTY LRLEREGLGV SSVPIQDIAF TIIRSAAVTG SPFLMFKDAC NRNYHMNTQG
NAITGSNLCT EIVQKADAHQ HGVCNLASIN LTTCLSKGPV SFNLNDLQLT ARTTVIFLNG
VLAAGNFPCK KSCKGVKNNR SLGIGIQGLH TTCLRLGFDL TSQPARRLNV QIAELMLYET
MKTSMEMCKI GGLAPFKGFT ESKYAKGWLH QDGFSTISYL DLPWCTLRDD ICAYGLYNSQ
FLALMPTVSS AQVTECSEGF SPIYNNMFSK VTTSGELLRP NLDLMDELRD MYSCEEKRLE
VINILEKNQW SVIRSFGCLS NSHPLLKYKT AFEYEQEDLV DMCAERAPFI DQSQSMTLFI
EERPDGTIPA SKIMNLLIRA YKAGLKTGMY YCKIRKATNS GLFAGGELTC TSCAL
