RIR2_VAR67
ID RIR2_VAR67 Reviewed; 319 AA.
AC P0DSS7; P33799;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN ORFNames=C8L, F4L;
OS Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=587200;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8109158; DOI=10.1016/0168-1702(93)90093-3;
RA Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V.,
RA Sandakhchiev L.S.;
RT "Analysis of the nucleotide sequence of a 43 kbp segment of the genome of
RT variola virus India-1967 strain.";
RL Virus Res. 30:239-258(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT "Genes of variola and vaccinia viruses necessary to overcome the host
RT protective mechanisms.";
RL FEBS Lett. 319:80-83(1993).
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 -!- 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 -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48969.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X69198; CAA48969.1; ALT_INIT; Genomic_DNA.
DR PIR; H36839; H36839.
DR RefSeq; NP_042072.2; NC_001611.1.
DR SMR; P0DSS7; -.
DR GeneID; 1486388; -.
DR KEGG; vg:1486388; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002060; 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_0000190499"
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; 37031 MW; E0D62D56C4894928 CRC64;
MEPILAKNPN RFVIFPIQYH DIWNMYKKAE ASFWTVEEVD ISKDINDWNK LTPDEKYFIK
HVLAFFAASD GIVNENLAER FCIEVQITEA RCFYGFQMAI ENIHSEMYSL LIDTYVKDSN
EKNYLFNAIE TMPCVKKKAD WAQKWIHDSA GYGERLIAFA AVEGIFFSGS FASIFWLKKR
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LLYPPSEETV RSIITDAVSI EQEFLTVALP
VKLIGMNCEM MKTYMEFVAD RLISELGFKR IYNVTNPSDF MENISLEGKT NFFEKRVGEY
QKMGVMSQED NHFSLDVDF
