ID A7RCK1_PBCVA Unreviewed; 767 AA.
AC A7RCK1;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=C748R {ECO:0000313|EMBL:ABU44293.1};
GN ORFNames=AR158_C748R {ECO:0000313|EMBL:ABU44293.1};
OS Paramecium bursaria Chlorella virus AR158 (PBCV-AR158).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=380598 {ECO:0000313|EMBL:ABU44293.1, ECO:0000313|Proteomes:UP000203485};
OH NCBI_TaxID=74790; Paramecium bursaria.
RN [1] {ECO:0000313|EMBL:ABU44293.1, ECO:0000313|Proteomes:UP000203485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR158 {ECO:0000313|EMBL:ABU44293.1,
RC ECO:0000313|Proteomes:UP000203485};
RX PubMed=17027058; DOI=10.1016/j.virol.2006.08.033;
RA Fitzgerald L.A., Graves M.V., Li X., Feldblyum T., Nierman W.C.,
RA Van Etten J.L.;
RT "Sequence and annotation of the 369-kb NY-2A and the 345-kb AR158 viruses
RT that infect Chlorella NC64A.";
RL Virology 358:472-484(2007).
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; DQ491003; ABU44293.1; -; Genomic_DNA.
DR RefSeq; YP_001498829.1; NC_009899.1.
DR GeneID; 5659976; -.
DR KEGG; vg:5659976; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000203485; 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:UP000203485}.
FT DOMAIN 10..113
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 767 AA; 86004 MW; BED804E212D88F48 CRC64;
MVGRPMNRLM VVLKRDGSKE NISFDKILQR IQRLCWPIDS KPVYKGSRAM TGLSVDVSKI
VASVCASIVD GISTVQLDEL TADKSASMTT EHPDYGILAA RISVSNLQKQ THDKITDAYA
EIAHLLSDDF KENIEKHADE YQSFIDYDRD YDFDYFGFKT MERLYLTKVN NKIVERPQHV
YLRVAIGLWG SDIARVKETY DALSCRKFTH ASPTLFNAGF KKAQLASCFL VTVEDSLGDI
YKVLGDCAQL SKHGGGLGIN ISEIRGRGSR INGTNGESDG IVPMLKVFDT TSAYANQGGR
RKGSFAIYLE PHHPDVMDFL LMKRNQGEES LRARNLFYAV WLNDLFMKRV ETDAQWSLFD
PSECPGLTDA FGDEYAELYE RYEAEGKAKN VVKARDVWNT MVTTIIETGQ PYVSNKDAVN
KKNMQMNAGT IRGSNLCNEI VEYTSKEETA VCVIGSVVLK NYVKNDKFDF DDLRKNVKIL
AKNLDRSIDV MSYPIKEAET SNKLRRPIGV GVQGLQDVFF KLKLPFDSSE ARDLNREIFE
HIYYAAVEAS IELAEIHGPY PTFEGSPASK GILQYHLWDV TPKSNLDWRG LEERVKKGVR
NSLVTALMPT ASTAQICGSI EAFEPITSNL YSRRTLAGEF PVVNSYLVRE LIERGTWSES
MKNQIIANGG SIQKVIGIHP SVKAVYKTAW DLSMKSVIDM AADRGPFVDQ TQSMNLFLAQ
PTLKNVTSML FYGWKSGLKT LQYYLRSKPS SSAIAVTIDN DCLVCSA
//
