ID   A0A3T0II43_9CAUD        Unreviewed;       675 AA.
AC   A0A3T0II43;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=pW4_84 {ECO:0000313|EMBL:AZU99099.1};
OS   Bacillus phage pW4.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=2500560 {ECO:0000313|EMBL:AZU99099.1, ECO:0000313|Proteomes:UP000288674};
RN   [1] {ECO:0000313|EMBL:AZU99099.1, ECO:0000313|Proteomes:UP000288674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hu X., Wan X., Geng P., Yuan Z.;
RT   "Characterization of novel siphovirus infecting Emetic Bacillus cereus.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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; MK288022; AZU99099.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000288674; 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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288674}.
FT   DOMAIN          534..556
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   675 AA;  77457 MW;  37D30DB4F1A0B796 CRC64;
     MQKDKEAVRS YFMDYINENI RSFLDFEEKM NFMVNEKYYD KEVLDQYTPK QVEEIFNHAY
     SFDFRFPSFM SALKFFTDYA LMNRKGDRYL ERYEDRVAMT ALFLGQGSFK SAMNLCDRMM
     KQRYQPATPT FLNAGKYARG EMVSCFLLDV NDAMNDISFR IANSLELSKL GGGVALNLTG
     LRSKGDPIKG IDNRASGVVP VMKLLEDSFA YANQLGARKG SGVAYLNIFH WDIVDFLDTK
     KINTDEKTRI QSLSIGVSVP DKFLELAEND EEFYMFSPYD VKKEYGLAID EIDWDKMYDE
     VVNNHKVKKK KMSAAEMWTD YIMRVLFESG YPYIMFEGNV NNQHPLKYLG RVKKSNLCTE
     ILQYSSDTTK ADYGEEDDLG LDISCNLGAL NIVNVMEGKD LKGDTFAGMD ALTAVTDFSN
     IKNVPTIKKA NDLMKSVGLG FMNLHGYLAK NGIPYGSKAS IDFARTFFST INYYTLVRSN
     QIAIERESVF FGFDKSTYST GEYFESHIEE DYRPKLKKVQ KLFEGIEIPT QEDWMKLAYS
     VQQHGLYHSY RLASAPTGGI SYVQNATQGV LPIVNLIEAR TTNKFTVQYP APFMEEAEQY
     YESAYDIDPF KIVDVIAEIQ KHIDQGISFT LHYKGEPNTR LLGRIYAYAY KKKVKTIYYL
     RTKLTQVTEC EACSI
//