ID   RIR2_SWPVK              Reviewed;         274 AA.
AC   P32209;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   ORFNames=C14L;
OS   Swinepox virus (strain Kasza) (SWPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus;
OC   Suipoxvirus swinepox; Swinepox virus.
OX   NCBI_TaxID=10277;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA   Massung R.F., Jayarama V., Moyer R.W.;
RT   "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT   identification of genetic elements supporting phenotypic observations
RT   including a novel G protein-coupled receptor homologue.";
RL   Virology 197:511-528(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=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]-
CC         disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]-
CC         dithiol; 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   -!- SUBUNIT: Heterodimer of a large and a small chain.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; L22013; AAC37857.1; -; Unassigned_RNA.
DR   AlphaFoldDB; P32209; -.
DR   SMR; P32209; -.
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:UniProtKB-KW.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..274
FT                   /note="Ribonucleoside-diphosphate reductase small chain"
FT                   /id="PRO_0000190500"
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   274 AA;  31753 MW;  F6F1A309EC75F411 CRC64;
     MEPILQESDS RFVIFPIKYH DIWKMYKQSV ASFWTVEEVD LSKDLDDWDK LTKDEKYFIK
     HILAFFASSD GIVNENLAER FYVDVQCSEA RCFYGFQIAM ENIHSEMYSL LIDTYVRDNI
     EKMHLFNAIE TMECVKKKAD WARKWISSNK VYGERVVAFA AVEGIFFSGS FAAIFWIKKR
     GLMPGLTFSN ELISRDEGLH CDFACLMFKH LLHPPSKEVI TSIIIDAVNI EKEFLTVAIP
     VDLIGMNCCL MSQYIEFVAD RLLTELGCEK SQCI
//