ID E4WLZ9_9PHYC Unreviewed; 747 AA.
AC E4WLZ9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=OtV2_123 {ECO:0000313|EMBL:CBI70122.1};
OS Ostreococcus tauri virus 2.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Prasinovirus.
OX NCBI_TaxID=696472 {ECO:0000313|EMBL:CBI70122.1, ECO:0000313|Proteomes:UP000202189};
RN [1] {ECO:0000313|Proteomes:UP000202189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21289127; DOI=10.1128/JVI.02131-10;
RA Weynberg K.D., Allen M.J., Gilg I.C., Scanlan D.J., Wilson W.H.;
RT "Genome sequence of Ostreococcus tauri virus OtV-2 throws light on the role
RT of picoeukaryote niche separation in the ocean.";
RL J. Virol. 85:4520-4529(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; FN600414; CBI70122.1; -; Genomic_DNA.
DR RefSeq; YP_004063556.1; NC_014789.1.
DR GeneID; 10021105; -.
DR KEGG; vg:10021105; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000202189; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000202189}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 747 AA; 84423 MW; 26F50B433640FB7F CRC64;
MRVVKRSGRI EDMKFDNITN RIKNLTYGLS ENCDSSKVAQ QVASSLYDGI TVQEIDTLSA
EVCIGLITSD PDYEILATRI TASNIQKVCP NNFHIAMKKL AKAGIVTEEV ARIAGRVRDD
IDTKRDYDFG YFGLKTLEKS YLQRLDGILM ETPQYMFMRV AIGIHGEDID SVLETYDKMS
QGMFIHATPT LFNAGTPRPQ MSSCFLIANK EDSINGIYGT LTECAQISKW AGGIGMHIHD
VRANKSRIRG TNGQSDGIIP MLRVFNATAR YVNQAGRRKG SIAVYLEPWH ADIMEFLELR
LNQGDEEARC RDLFSSLWIP DLFMKRVEEG GQWSLFCPDK APGLSDAVGE EFEALYTKYE
AEGRANAIVP AADVWKAILK SQTETGTPYM LYKDACNKKS NQKNLGTIKS SNLCTEILEY
TDKDETAVCN LASIALPKYV NEETRTFDYE KLHEITKIVT KNLNRVIDRN FYPVETARKS
NMRHRPIGLG VQGLADVFIL CRYAFDSDEA KEMNARIFET MYHASLEASC ELAEAQGSYE
TFEGSPTSQG VLQFDMWEGE TKLNYDWDVL KERIKEKGLR NSLLMAPMPT ASTAQILGNN
ECFEPYTTNI YLRRTLAGEF VIVNKHLVND LKKIGLWSKD MKDLMVKAGG SIQNISDIPD
DIKNLYRTVW EIKMKDVIDM AAQRGRFIDQ SQSMNLFMES PTMSKLSSMH MYAWKQGLKT
GMYYLRSKAK ARPIQFSLEP ECVACSA
//
