ID RIR2_OSHVF Reviewed; 579 AA. AC Q6R7K3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Ribonucleoside-diphosphate reductase small chain; DE EC=1.17.4.1; GN ORFNames=ORF20; OS Ostreid herpesvirus 1 (isolate France) (OsHV-1) (Pacific oyster OS herpesvirus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Malacoherpesviridae; Ostreavirus; OC Ostreavirus ostreidmalaco1; Ostreid herpesvirus 1. OX NCBI_TaxID=654903; OH NCBI_TaxID=29159; Crassostrea gigas (Pacific oyster) (Crassostrea angulata). OH NCBI_TaxID=6579; Pecten maximus (King scallop) (Pilgrim's clam). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15604430; DOI=10.1099/vir.0.80382-0; RA Davison A.J., Trus B.L., Cheng N., Steven A.C., Watson M.S., Cunningham C., RA Le Deuff R.M., Renault T.; RT "A novel class of herpesvirus with bivalve hosts."; RL J. Gen. Virol. 86:41-53(2005). RN [2] RP REVIEW. RX PubMed=18990579; DOI=10.1016/j.tibs.2008.09.008; RA Lembo D., Brune W.; RT "Tinkering with a viral ribonucleotide reductase."; RL Trends Biochem. Sci. 34:25-32(2009). CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the CC precursors necessary for viral DNA synthesis. Allows virus growth in CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides CC from the corresponding ribonucleotides (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 -!- 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 composed of a homodimer of the large subunit CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit CC protein complex are also active, composed of (R1)n(R2)n (By CC 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; AY509253; AAS00912.1; -; Genomic_DNA. DR RefSeq; YP_024565.1; NC_005881.2. DR SMR; Q6R7K3; -. DR GeneID; 2948202; -. DR KEGG; vg:2948202; -. DR Proteomes; UP000007021; Segment. 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 CDD; cd01049; RNRR2; 1. DR Gene3D; 1.10.3290.10; Fido-like domain; 1. DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR003812; Fido. DR InterPro; IPR036597; Fido-like_dom_sf. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR000358; RNR_small_fam. DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1. DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1. DR Pfam; PF02661; Fic; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR SUPFAM; SSF140931; Fic-like; 1. DR PROSITE; PS51459; FIDO; 1. PE 3: Inferred from homology; KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..579 FT /note="Ribonucleoside-diphosphate reductase small chain" FT /id="PRO_0000385024" FT DOMAIN 435..579 FT /note="Fido" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791" FT ACT_SITE 167 FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 160 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 160 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 225 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 579 AA; 66994 MW; E7B90F9E49DF0791 CRC64; MSQSTIKFDL GELTTTQCAR LLSKFIRKAT LTPEQFEILN TSYDELTEFD DHPLYGGATD HHKDIVGKYD HALLKPAVYQ QLRDFATKME SSSWQQTEID AESDIPTWEQ ISENERDCVR KVLAFFAVGD TLVKDRIAIF ADEFPLPECK DFIDWQTVNE GVHQRVYNNY LDALVKDKIY LADLVNAYKD PEFAPIKKKV DWLGKIISVE NDSRGEMVVG QVCTEAIMFA ASFAILLKFR APYMRALVLG NEFIRRDETL HFRFYAELLR LMPDRPSDER IAELLTEATE IELEFAEYVV PEGVKYITKD RLIQHVKANT NQVCEMLDIN PIYFDQKGNV LLSPLLYMNT LESEQKINFF EGKATEYNTK QYKVDFNNLF PPVKKMIEFA DEEEFIAAIV EGEGLSKDRN KDIVKQQLCL AWDHLSSHDM EGLVDMTWTL KDVHRIAMNH VIFNNGEFSN GYKFTVIDSG KVMYPTYETV EILESAVQGL IDDYNRDFSA LDKGVEKFDK DKIRVAARFI LDLLYIHPFS DGNGRTARLI MAHLIGKMTT PINREEYLKS IYHYRQTGDV SVFVDQFYR //