RIR2_CAEEL
ID RIR2_CAEEL Reviewed; 381 AA.
AC P42170;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=rnr-2; ORFNames=C03C10.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; Z35637; CAA84688.1; -; Genomic_DNA.
DR PIR; T18876; T18876.
DR RefSeq; NP_497821.1; NM_065420.5.
DR AlphaFoldDB; P42170; -.
DR SMR; P42170; -.
DR BioGRID; 40762; 11.
DR DIP; DIP-24490N; -.
DR IntAct; P42170; 1.
DR STRING; 6239.C03C10.3; -.
DR EPD; P42170; -.
DR PaxDb; P42170; -.
DR PeptideAtlas; P42170; -.
DR EnsemblMetazoa; C03C10.3.1; C03C10.3.1; WBGene00004392.
DR GeneID; 175525; -.
DR KEGG; cel:CELE_C03C10.3; -.
DR UCSC; C03C10.3.1; c. elegans.
DR CTD; 175525; -.
DR WormBase; C03C10.3; CE00874; WBGene00004392; rnr-2.
DR eggNOG; KOG1567; Eukaryota.
DR GeneTree; ENSGT00390000013305; -.
DR HOGENOM; CLU_035339_2_1_1; -.
DR InParanoid; P42170; -.
DR OMA; KVGEYQR; -.
DR OrthoDB; 680824at2759; -.
DR PhylomeDB; P42170; -.
DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00326; -.
DR PRO; PR:P42170; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004392; Expressed in germ line (C elegans) and 5 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
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;
KW Reference proteome.
FT CHAIN 1..381
FT /note="Ribonucleoside-diphosphate reductase small chain"
FT /id="PRO_0000190455"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 44289 MW; 75497147ABF36C59 CRC64;
MTLTEIQNVE KENAGASVPK HSSNKLKLEK ELEKLEIVDQ TKAASAEETN NESEVNELDA
DEPMLQDLDN RFVIFPLKHH DIWNFYKKAV ASFWTVEEVD LGKDMNDWEK MNGDEQYFIS
RILAFFAASD GIVNENLCER FSNEVQVSEA RFFYGFQIAI ENIHSEMYSK LIETYIRDET
ERNTLFNAVD EFEFIKKKAD WALRWISDKK ASFAERLIAF AAVEGIFFSG SFASIFWLKK
RGLMPGLTHS NELISRDEGL HRDFACLLYS KLQKKLTQQR IYDIIKDAVA IEQEFLTEAL
PVDMIGMNCR LMSQYIEFVA DHLLVELGCD KLYKSKNPFD FMENISIDGK TNFFEKRVSE
YQRPGVMVNE AERQFDLEAD F
