RIR2_SPISO
ID RIR2_SPISO Reviewed; 384 AA.
AC P07201;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
DE AltName: Full=p41;
OS Spisula solidissima (Atlantic surf-clam).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Venerida; Mactroidea; Mactridae; Spisula.
OX NCBI_TaxID=6584;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2148535; DOI=10.1101/gad.4.12a.2157;
RA Standart N.M., Dale M., Stewart E., Hunt T.;
RT "Maternal mRNA from clam oocytes can be specifically unmasked in vitro by
RT antisense RNA complementary to the 3'-untranslated region.";
RL Genes Dev. 4:2157-2168(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-384.
RX PubMed=2987274; DOI=10.1083/jcb.100.6.1968;
RA Standart N.M., Bray S.J., George E.L., Hunt T., Ruderman J.V.;
RT "The small subunit of ribonucleotide reductase is encoded by one of the
RT most abundant translationally regulated maternal RNAs in clam and sea
RT urchin eggs.";
RL J. Cell Biol. 100:1968-1976(1985).
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 -!- MISCELLANEOUS: There is no sign of synthesis of a corresponding large
CC subunit after fertilization. The authors suspect that the unfertilized
CC oocytes contain a stockpile of large subunits ready for combination
CC with newly made small subunits.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; X55125; CAA38919.1; -; mRNA.
DR EMBL; X02471; CAA26307.1; -; mRNA.
DR PIR; A22259; RDSS2R.
DR PIR; S24585; S24585.
DR AlphaFoldDB; P07201; -.
DR SMR; P07201; -.
DR PRIDE; P07201; -.
DR UniPathway; UPA00326; -.
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:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..384
FT /note="Ribonucleoside-diphosphate reductase small chain"
FT /id="PRO_0000190453"
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 384 AA; 44447 MW; 2F576F7BEA9297B0 CRC64;
MLSINTTRKE NELSGNLGKM KITEENKPKK VLGEITNFQR STQKTPLKQE IKPVVKKSQQ
VEPLLADNPR RFVVLPIQYH DIWKMYKKAE ASFWTAEEVD LSKDMAHWES LKKEEKHFIS
HVLAFFAASD GIVNENLVER FSKEVQVTEA RCFYGFQIAM ENIHSEMYSL LIDTYIKDPQ
ERDFLFNAIE TMPCVKEKAD WAMRWINDDS SSYAERVVAF AAVEGIFFSG SFASIFWLKK
RGIMPGLTFS NELISRDEGL HCDFACLMFS HLVNKPSQER IHQIIDEAVK IEQVFLTEAL
PCRLIGMNCD LMRQYIEFVA DRLLLELKCD KLYNKENPFD FMEHISLEGK TNFFEKRVGE
YQKMGVMSGG NTGDSHAFTL DADF
