ID RIR2_MACFA Reviewed; 389 AA. AC Q4R7Q7; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small chain; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=RRM2; ORFNames=QtsA-14617; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). Inhibits Wnt signaling CC (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 -!- SUBUNIT: Heterodimer of a large and a small subunit. Interacts (via Cy CC motif and when phosphorylated at Thr-33) with CCNF; the interaction CC occurs exclusively in G2 and early M (By similarity). CC {ECO:0000250|UniProtKB:P31350}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31350}. Nucleus CC {ECO:0000250|UniProtKB:P31350}. Note=Localized to the cytoplasm in S CC phase cells. May localize to the nucleus in G2 phase cells. CC {ECO:0000250|UniProtKB:P31350}. CC -!- PTM: Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt CC signaling (By similarity). Phosphorylated on Thr-33 by CDK1 and CDK2; CC predominantly in G2 and M phase (By similarity). CC {ECO:0000250|UniProtKB:P31350}. CC -!- PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase CC complex; leading to its degradation by the proteasome. CC {ECO:0000250|UniProtKB:P31350}. CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: the CC specificity site, which controls substrate specificity, and the CC activity site which regulates overall catalytic activity. A substrate- CC binding catalytic site, located on M1, is formed only in the presence CC of the second subunit M2 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB168758; BAE00865.1; -; mRNA. DR RefSeq; NP_001271095.1; NM_001284166.1. DR AlphaFoldDB; Q4R7Q7; -. DR SMR; Q4R7Q7; -. DR STRING; 9541.ENSMFAP00000003161; -. DR eggNOG; KOG1567; Eukaryota. DR OrthoDB; 5487627at2759; -. DR Proteomes; UP000233100; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB. 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:SF20; 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 2: Evidence at transcript level; KW Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..389 FT /note="Ribonucleoside-diphosphate reductase subunit M2" FT /id="PRO_0000190448" FT MOTIF 49..51 FT /note="Cy" FT /evidence="ECO:0000250|UniProtKB:P31350" FT ACT_SITE 176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 138 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" 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 169 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 232 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 BINDING 269 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11157" FT MOD_RES 33 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P11157" SQ SEQUENCE 389 AA; 44804 MW; 973BAF4471AF2039 CRC64; MLSVRIPLAP ITNPQQLQLS PLKGLSLVDK ENTPPALSGA RVLASKTARR IFQEPAEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM PCVEKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRVE QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF //