ID M1JTB5_NPVSL Unreviewed; 828 AA.
AC M1JTB5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
GN ORFNames=SlsnVgp020 {ECO:0000313|EMBL:AGE89875.1};
OS Spodoptera littoralis nuclear polyhedrosis virus (SlNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC Alphabaculovirus splittoralis.
OX NCBI_TaxID=10456 {ECO:0000313|EMBL:AGE89875.1, ECO:0000313|Proteomes:UP000232896};
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1] {ECO:0000313|EMBL:AGE89875.1, ECO:0000313|Proteomes:UP000232896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AN1956 {ECO:0000313|EMBL:AGE89875.1};
RX PubMed=23219924; DOI=10.1016/j.virusres.2012.11.016;
RA Breitenbach J.E., El-Sheikh el.-S.A., Harrison R.L., Rowley D.L.,
RA Sparks M.E., Gundersen-Rindal D.E., Popham H.J.;
RT "Determination and analysis of the genome sequence of Spodoptera littoralis
RT multiple nucleopolyhedrovirus.";
RL Virus Res. 171:194-208(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX454574; AGE89875.1; -; Genomic_DNA.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000232896; Chromosome.
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 47..138
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 828 AA; 93045 MW; 52835DFBE132D72E CRC64;
MLSQDVGYAL SQDMCYLCVR DTVHVKFTIN TFQYFNLELN SIMLSSDYVT KRDGRKEDVS
VRKIKYRIEK QCYGLDMYFV NPASLTRRVV QGIYPGVTTV ELDNLIAETA ASMTIDHSDY
SLLAARLAVS NLHKETKDLF FNVIVDMYEA IDQKTGAATP MISDFHYGII AANADRLNSA
IMHDRDFNYD YFGFKTMQRS YLFKINGITV ERPQYMMMRV AIGIHGRDID AAIETYNLMS
NGYFTHASPT LFSAATPKAQ MSSCFLVAIK EDSIEGIYDT LKQCAMISKS GGGIGFHVHN
VRAKGSSVAG VDGAANGLVP MLRVYNNTAR YVNQGGNKRP GAFAVYVEPW HADVFDFLDL
KKNTGKEEVR ARELFYALWI PDLFMRRVET DAMWSLMCPM QSPGLADCHG VEFEALYEKY
EKQGRYVKRV SAQTLWRAII EAQVETGTPY MLYKDSCNRK SNQSNLGTIK CSNLCTEIVE
YTSKDEVAVC NLASIAVNKF VAPQPGVYDF ERLKEITKIV TRNLNRIIDA NQCPLREAER
SNQRNRPIGI GVQGMADAFV TMRMPYESDA AAELNKKIFE TIYYGALEAS CELAAKDGPY
ETYKGSPASR GELQYDMWNG ATPSNLWDWS LLKSKISKYG LRNSLLLAPM PTASTAQILG
NNESFEPFTS NIYQRRVLSG EFQVVNRHLV KDLAAIGLWN DTMKNLIMYN NGSVQNIESI
PFEIRQLYKT VWEMSMRTMI RMAADRGAFI DQSQSFNVYM AEPSYGKLTS IHFYAWKMGL
KTGMYYLRTK PAVNAIQFTV DKNAATAAAA TAAAAFAVSS SDCTSCSS
//
