RIR2_VACCW
ID RIR2_VACCW Reviewed; 319 AA.
AC P11158; Q76ZX1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN OrderedLocusNames=VACWR043; ORFNames=F4L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=2219701; DOI=10.1016/0042-6822(90)90338-r;
RA Roseman N.A., Slabaugh M.B.;
RT "The vaccinia virus HindIII F fragment: nucleotide sequence of the left 6.2
RT kb.";
RL Virology 178:410-418(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2826813; DOI=10.1128/jvi.62.2.519-527.1988;
RA Slabaugh M., Roseman N., Davis R., Mathews C.;
RT "Vaccinia virus-encoded ribonucleotide reductase: sequence conservation of
RT the gene for the small subunit and its amplification in hydroxyurea-
RT resistant mutants.";
RL J. Virol. 62:519-527(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ENZYME ACTIVITY, AND INDUCTION.
RX PubMed=3534300; DOI=10.1128/jvi.60.2.506-514.1986;
RA Slabaugh M.B., Mathews C.K.;
RT "Hydroxyurea-resistant vaccinia virus: overproduction of ribonucleotide
RT reductase.";
RL J. Virol. 60:506-514(1986).
CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the
CC precursors necessary for viral DNA synthesis. Allows virus growth in
CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides
CC from the corresponding ribonucleotides (By similarity). {ECO:0000250}.
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|PROSITE-ProRule:PRU10014,
CC ECO:0000269|PubMed:3534300};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
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 (By
CC similarity). {ECO:0000250}.
CC -!- INDUCTION: Expressed early in the viral replicative cycle.
CC {ECO:0000269|PubMed:2219701, ECO:0000269|PubMed:3534300}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; M34368; AAA48244.1; -; mRNA.
DR EMBL; M19117; AAA88680.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89322.1; -; Genomic_DNA.
DR PIR; A29892; RDVZVV.
DR RefSeq; YP_232925.1; NC_006998.1.
DR SMR; P11158; -.
DR DIP; DIP-2157N; -.
DR IntAct; P11158; 1.
DR MINT; P11158; -.
DR DNASU; 3707500; -.
DR GeneID; 3707500; -.
DR KEGG; vg:3707500; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 2: Evidence at transcript level;
KW Deoxyribonucleotide synthesis; Early protein; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..319
FT /note="Ribonucleoside-diphosphate reductase small chain"
FT /id="PRO_0000190498"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 70
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 319 AA; 36973 MW; 8E296CCC5AB4F949 CRC64;
MEPILAPNPN RFVIFPIQYY DIWNMYKKAE ASFWTVEEVD ISKDINDWNK LTPDEKYFIK
HVLAFFAASD GIVNENLAER FCTEVQITEA RCFYGFQMAI ENIHSEMYSL LIDTYVKDSN
EKNYLFNAIE TMPCVKKKAD WAQKWIHDSA GYGERLIAFA AVEGIFFSGS FASIFWLKKR
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LLHPPSEETV RSIITDAVSI EQEFLTAALP
VKLIGMNCEM MKTYIEFVAD RLISELGFKK IYNVTNPFDF MENISLEGKT NFFEKRVGEY
QKMGVMSQED NHFSLDVDF
