ID Q77SA7_9ABAC Unreviewed; 760 AA.
AC Q77SA7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
OS Ectropis obliqua nucleopolyhedrovirus.
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC Alphabaculovirus ecobliquae.
OX NCBI_TaxID=59376 {ECO:0000313|EMBL:AAQ88175.1, ECO:0000313|Proteomes:UP000214344};
RN [1] {ECO:0000313|EMBL:AAQ88175.1, ECO:0000313|Proteomes:UP000214344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:AAQ88175.1,
RC ECO:0000313|Proteomes:UP000214344};
RX PubMed=16554721;
RA Ma X.C., Xu H.J., Tang M.J., Xiao Q., Hong J., Zhang C.X.;
RT "Morphological, phylogenetic and biological characteristics of Ectropis
RT obliqua single-nucleocapsid nucleopolyhedrovirus.";
RL J. Microbiol. 44:77-82(2006).
RN [2] {ECO:0000313|EMBL:AAQ88175.1, ECO:0000313|Proteomes:UP000214344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:AAQ88175.1,
RC ECO:0000313|Proteomes:UP000214344};
RX PubMed=17097707; DOI=10.1016/j.virol.2006.10.024;
RA Ma X.C., Shang J.Y., Yang Z.N., Bao Y.Y., Xiao Q., Zhang C.X.;
RT "Genome sequence and organization of a nucleopolyhedrovirus that infects
RT the tea looper caterpillar, Ectropis obliqua.";
RL Virology 360:235-246(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; DQ837165; AAQ88175.1; -; Genomic_DNA.
DR RefSeq; YP_874319.1; NC_008586.1.
DR GeneID; 5176469; -.
DR KEGG; vg:5176469; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000214344; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 2..93
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 760 AA; 86259 MW; 72F4235B1F11E646 CRC64;
MFSVTKRDNA KQCFDQKKIV KTLQNLSVDL NKNLIDCEAL VAQLKKTLVS NVSTSQLCVL
LARESASMAY IHDEYAMLAG RLMVIDNHKQ VSDDYAVVVD NLYNQNLVSA QFYKSAIANM
HTINATLNYN LDYDYKYFGF KTLENGYLKT IEGKVAERIQ HMYMRVALTI HGNDTDDCIE
NVFETYNLMA HKMYTHASPT LFASGSCYAQ LASCFLLNIK EDSIVGIYET LRDCALISKF
GGGIGLSVHN VRARGSFIES TNGTANGLEA MLRVYNNAVR HVDQGGKRKG AMAIYVEPWH
ADIYDFLELK RNMGAEDRKA RDLLYALWVP DLFMKRVEAD GMWSLMCPRE SPLLDTVHGS
EFEQLYVAYE KCGKFVRQIK ARDLFRTIVE TQVETGTPYM MYKDACNMKS NQKHLGTIKN
SNLCAEIVEY SDKNESAVCN LASICVNQFV DIDVGEYNFE MLKYVTKIVV KNLNKIIDIN
YYPLLSAQKS NRKHRPIGVG IQGLADTFAM LRMPYESDQA KVLNTKIAET IYFGALEASC
ELAKAYGVHD SYFSSPASLG ILQYDLWNHT PTSMWDWTQL KKDIKQHGLR NSLCVAYMPT
ATTAQILGNN ESFEPFTNNI YVRRVLAGDF QVINKYLTDD LIKLNLYNEQ MRNKIIANNG
SVQNIEEIPK HVRELYKTVW EMKVKNLIGM AADRGPFIDQ SQSFNIFLSQ PTYALLTTIH
MHTWKSGLKT GMYYLRTKPA ADAIKFTVDK SQIVCNACSS
//
