ID   RIR2_SCHPO              Reviewed;         391 AA.
AC   P36603; O74355;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   Name=suc22; ORFNames=SPBC25D12.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8479429; DOI=10.1007/bf00279553;
RA   Fernandez-Sarabia M.J., McInerny C., Harris P., Gordon C., Fantes P.;
RT   "The cell cycle genes cdc22+ and suc22+ of the fission yeast
RT   Schizosaccharomyces pombe encode the large and small subunits of
RT   ribonucleotide reductase.";
RL   Mol. Gen. Genet. 238:241-251(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12695334; DOI=10.1101/gad.1090803;
RA   Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.;
RT   "Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by
RT   both checkpoint-dependent and -independent mechanisms.";
RL   Genes Dev. 17:1130-1140(2003).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides.
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   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12695334}. Cytoplasm
CC       {ECO:0000269|PubMed:12695334}. Note=Localization to the cytoplasm is
CC       CSN- and checkpoint-dependent and is required for an efficient DNA
CC       damage response.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; X65115; CAA46231.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA20100.1; -; Genomic_DNA.
DR   PIR; S34808; S34808.
DR   PIR; T39992; T39992.
DR   RefSeq; NP_596546.1; NM_001022467.2.
DR   AlphaFoldDB; P36603; -.
DR   SMR; P36603; -.
DR   BioGRID; 276910; 9.
DR   STRING; 284812.P36603; -.
DR   iPTMnet; P36603; -.
DR   SwissPalm; P36603; -.
DR   MaxQB; P36603; -.
DR   PaxDb; 4896-SPBC25D12-04-1; -.
DR   EnsemblFungi; SPBC25D12.04.1; SPBC25D12.04.1:pep; SPBC25D12.04.
DR   GeneID; 2540381; -.
DR   KEGG; spo:SPBC25D12.04; -.
DR   PomBase; SPBC25D12.04; suc22.
DR   VEuPathDB; FungiDB:SPBC25D12.04; -.
DR   eggNOG; KOG1567; Eukaryota.
DR   HOGENOM; CLU_035339_2_1_1; -.
DR   InParanoid; P36603; -.
DR   OMA; KVGEYQR; -.
DR   PhylomeDB; P36603; -.
DR   PRO; PR:P36603; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IPI:PomBase.
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:0046704; P:CDP metabolic process; IDA:PomBase.
DR   GO; GO:0006240; P:dCDP biosynthetic process; IDA:PomBase.
DR   GO; GO:0009216; P:purine deoxyribonucleoside triphosphate biosynthetic process; IC:PomBase.
DR   GO; GO:0042278; P:purine nucleoside metabolic process; IC:PomBase.
DR   GO; GO:0009212; P:pyrimidine deoxyribonucleoside triphosphate biosynthetic process; IC:PomBase.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IC:PomBase.
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   Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..391
FT                   /note="Ribonucleoside-diphosphate reductase small chain"
FT                   /id="PRO_0000190463"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         229
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        285..288
FT                   /note="VVEA -> LLKP (in Ref. 1; CAA46231)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   391 AA;  45405 MW;  740ECDBECC8D0170 CRC64;
     MGLEHLEEFS YPKEHGEEVE YDSEQGVRKI YVKSIKETFN FDNVSEEEKQ EGGDYYLGKK
     EDELDEVVLR PNPHRFVLFP IKYHEIWQFY KKAEASFWTA EEIDLSKDLV DWDNKLNADE
     RYFISTVLAY FAASDGIVNE NLLERFSSEV QIPEARCVYG FQIMIENIHS ETYSLLLDTY
     IREPKEKQRH FDAILTMGSI KAKAKWALRW INDEDSTYAI RLVAFAAVEG IFFSGSFASI
     FWLKKRGLMP GLTFSNELIC RDEGLHTDFA CLMFSHLKHR PGRKVVEAII VEAVDIEKEY
     FTDALPVSLL GMNKDLMCQY IEFVADRLLV ALGNDKYYNV TNPFDFMENI SLAGKTNFFE
     KKVSDYQIAG VMSGTKRAEK DDHTFTIDED F
//