ID   RIR2_RSIV               Reviewed;         312 AA.
AC   Q9QTF2;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   Name=RR-2;
OS   Red sea bream iridovirus (RSIV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Alphairidovirinae; Megalocytivirus;
OC   Infectious spleen and kidney necrosis virus.
OX   NCBI_TaxID=65424;
OH   NCBI_TaxID=94231; Epinephelus.
OH   NCBI_TaxID=8163; Lateolabrax.
OH   NCBI_TaxID=8160; Seriola.
OH   NCBI_TaxID=8237; Thunnus thynnus (Atlantic bluefin tuna) (Scomber thynnus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ehime-1;
RA   Kurita J., Nakajima K., Hirono I., Aoki T.;
RT   "7.1kbp DNA sequence of red sea bream iridovirus (RSIV) containing largest
RT   subunit of the DNA-dependent RNA polymerase (RPO-1) gene, RAD2 homolog gene
RT   and ribonucleotide reductase small subunit (RR-2) gene.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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: Heterodimer of a large and a small chain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; AB018418; BAA82755.1; -; Genomic_DNA.
DR   SMR; Q9QTF2; -.
DR   UniPathway; UPA00326; -.
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   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..312
FT                   /note="Ribonucleoside-diphosphate reductase small chain"
FT                   /id="PRO_0000190493"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         62
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         156
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35653 MW;  7D3E43D5F4F48B0B CRC64;
     MDRYVLRPND PHLWAMYKKA VASFWTVEEV DLSTDVRHWT DKLTEAERRF MSHILAFFAM
     ADGIVGDNLV CNFAKELDHI PEARAFYGFQ VAIENIHAEM YTQLIITLVA KENQAALFSA
     AEDMPCVKAK AQWAAQWLNA THKPIATRLL AFAAVEGVMF SGSFAAIFWL KKRSLMPGLA
     FSNELISRDE GLHCDFACML FRQMANKPCQ DDAHQIISDA VDIETAFFRE ALKTPLLGMN
     SDSMKLYIQF VADRLLDALG YAKMYNVSNP FDFMDNISIE GKTNFFERRV SEYQRMGVFT
     PSSMEFTMNE EF