RIR2_OSHVF
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 03-AUG-2022, entry version 84.
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.
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 -!- PATHWAY: Genetic information processing; DNA replication.
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}.
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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 UniPathway; UPA00326; -.
DR Proteomes; UP000007021; Genome.
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; 1.10.3290.10; -; 1.
DR Gene3D; 1.10.620.20; -; 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; PTHR23409; 1.
DR Pfam; PF02661; Fic; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR SUPFAM; SSF47240; SSF47240; 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
