ID RIR2B_MACFA Reviewed; 351 AA. AC Q4R741; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B; DE EC=1.17.4.1; GN Name=RRM2B; ORFNames=QtsA-16381; 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: Plays a pivotal role in cell survival by repairing damaged CC DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for CC DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free CC radical center required for catalysis. Forms an active ribonucleotide CC reductase (RNR) complex with RRM1 which is expressed both in resting CC and proliferating cells in response to DNA damage (By similarity). CC {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: Heterotetramer with large (RRM1) subunit. Interacts with CC p53/TP53. Interacts with RRM1 in response to DNA damage. DNA damage (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Note=Translocates from cytoplasm to nucleus in response to DNA damage. CC {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; AB168988; BAE01083.1; -; mRNA. DR AlphaFoldDB; Q4R741; -. DR SMR; Q4R741; -. DR STRING; 9541.ENSMFAP00000024294; -. DR eggNOG; KOG1567; Eukaryota. 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; IEA:UniProtKB-EC. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; 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:SF19; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2 B; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR PIRSF; PIRSF000355; NrdB; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Deoxyribonucleotide synthesis; DNA damage; DNA repair; Iron; KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome. FT CHAIN 1..351 FT /note="Ribonucleoside-diphosphate reductase subunit M2 B" FT /id="PRO_0000228151" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 100 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 131 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 131 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 134 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 194 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 351 AA; 40763 MW; 9887F862C3FD498A CRC64; MGDPERPEAA GLDLDERSSS DTNDNEIKSN EEPLLRKSSR RFVIFPIQYP DIWKMYKQAQ ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGIFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEER VREIIVDAVQ IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F //