ID   A0A2I7R1D1_9CAUD        Unreviewed;       762 AA.
AC   A0A2I7R1D1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=NVP1101O_040 {ECO:0000313|EMBL:AUR87451.1};
OS   Vibrio phage 1.101.O._10N.261.45.C6.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=2070725 {ECO:0000313|EMBL:AUR87451.1, ECO:0000313|Proteomes:UP000273409};
RN   [1] {ECO:0000313|EMBL:AUR87451.1, ECO:0000313|Proteomes:UP000273409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kauffman K.M., Hussain F.A., Yang J., Arevalo P., Brown J.M., Chang W.K.,
RA   VanInsberghe D., Elsherbini J., Cutler M.B., Kelly L., Polz M.F.;
RT   "A major lineage of nontailed dsDNA viruses as unrecognized killers of
RT   marine bacteria.";
RL   Submitted (NOV-2017) 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; MG592473; AUR87451.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000273409; 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   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; 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.
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          3..88
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   762 AA;  87276 MW;  4CAD91311C5FD918 CRC64;
     MINSVIKVNG IKEEFKAEKL NRWGEWAAKN DVAWSDIVMR TLDQLFDGCT TKDIHQAMIN
     VCVDKKDEKH LAFAARLLRG SIYKDVYNGA PVSFRESYNN LVEQGFWQDF HLSDESLDKI
     EEVFDPQFDK TYEYTSLLQF VDKYSMRKFT DSGYQLVETP QLMLMGIALA LFQNDSLEHV
     LNFYRIIRER KLNIATPIMA AARSGENEFT SCFLASSKDT LDSIAASTQL CYTMTANRAG
     VGMEYDVRSF GDVVGNNKCK HGGKLPQYNM LLNTIKSVTQ GVRGGAATVT FNVLDPEIDD
     LLRLKNPVTP LAKRIELMDY SLAWNNEFIR RVAKNEDWLL VSKKECPELH KAFYEERDKF
     PSLMEEMINK YSGKNNVANF LDPNYTPEKP KKFNGKIVKA RDIMKTFITQ RQETGQIYCI
     NIDTSNDHSS FKQDIIRQSN LCQEVCLPTK GFDSVLSLYN DANPDKDGIV GLCFLLATDV
     GKCSYEELDE VNYYACRALD NILTLTKYPF KALEDIGKKY RSIGVGVTNL AYFMAKNGVK
     YSSEEGRNLV HKLMEKQQFS LIRSSIELAK ERGKFEWYSR TKYPEGSLCI DTYTKEIDNH
     HSQPLELDWE ELKRKQLRHG MRFVTVSAHM PCESSSAWGF STNGLYPIRQ GTVMKSRPEG
     LVPFTAPDYE NLKDTYEAAW DVEPQDMYKI YGIVQKFTCM AISADSYLDF SKQDGKVSVS
     QMMKDMIFSQ KVGMKTHYYL NSRTENKHIQ SSEDDGCSSC KL
//