RIR1_OSHVF
ID RIR1_OSHVF Reviewed; 835 AA.
AC Q6R7H4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
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 -!- 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 large
CC chain family. {ECO:0000305}.
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DR EMBL; AY509253; AAS00941.1; -; Genomic_DNA.
DR RefSeq; YP_024594.1; NC_005881.2.
DR SMR; Q6R7H4; -.
DR GeneID; 2948194; -.
DR KEGG; vg:2948194; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000007021; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Disulfide bond; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..835
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000385023"
FT ACT_SITE 447
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 449
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 447..451
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 660..664
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 464
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 797
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 798
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 830
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 833
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 238..464
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 835 AA; 93356 MW; 4C5813635B9E5F47 CRC64;
MACSMANAVR PGLSDLPEGV DLSNPKEVRS LLIKLTHARK STVYDTKIRR LHGVIVNSIM
ENYNSAEGEL DMAITPLIPS HPDYAFLAGR VSAYMTQINT PKTFTDAVYG IQMAVGETNG
FRSPMKPVKG GLSDEIVDFV NEHGARLDGM IDDVRDYSHN YMGITGLLNG VAIKVNKKLY
ERPQYVFMRV AMAMTDLSSE TALEDIWQTY MLISGQCLSM ASPVLFNGGT SSSNTASCFL
LDMGDNMVSI TKKVAQTMTL IAKNGGIGIN FSKLRATGSK IGMAGKSSGI GGKLNLFDRV
AQSVDQGENK RPGAIAGYLT DWHADMYDWL YSRYSGSGNE VNKRHVLNMG LVMSDLFMER
VENDKEWSLF SPNDVVGLEE LYGEKFVRAY RAHEANPKIK RTTVSARKLF SDIANMMWST
GEPYILFKDA VNERSNHKHL GTIKNSNLCC EIVQYCDTNE IAVCNLATIC VSNFVNVETG
EIDFEGIADA AGVACKGINN LIDKQNYDLG NEQLMRLADE RTEEVVEVNG IKFDAKYNLV
SYSNLKHRPQ GIGMQGLHDV FMKLKIPYDS EMAFRLAALI QEAIYYGAVR ESVKIAEEKG
PYPSYYWDNN THREGKLQFD FLEGFDRDRD LTHELFNWRE VLKKFEKFGI NNSVVTAQPP
SASSSQLNDN VESIEAITSN RFTKGIKDGK FIIINKHLQK DLEDLGMWDA QMVGDIEAND
GSIQNIERIP KNIREIYKTA REIDHKAVVK ICAAIQPFID QTISKNMFVP KNVDNPVQLI
MENVILGHKM KLKTGMYYTR GIPAMKQQNF GKMNFQDKDI GKPVPELVDC EACSA
