RIR2_SCHPO
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 03-AUG-2022, entry version 168.
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 -!- PATHWAY: Genetic information processing; DNA replication.
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; 4896.SPBC25D12.04.1; -.
DR iPTMnet; P36603; -.
DR SwissPalm; P36603; -.
DR MaxQB; P36603; -.
DR PaxDb; P36603; -.
DR PRIDE; P36603; -.
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 Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00326; -.
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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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; -; 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 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
