ID   A0A023NGC2_9CAUD        Unreviewed;       875 AA.
AC   A0A023NGC2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=M316_0079 {ECO:0000313|EMBL:AHX01144.1};
OS   Nitrincola phage 1M3-16.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=1472912 {ECO:0000313|EMBL:AHX01144.1, ECO:0000313|Proteomes:UP000024336};
RN   [1] {ECO:0000313|EMBL:AHX01144.1, ECO:0000313|Proteomes:UP000024336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Movassaghi M., Lobo N., Moulton K.D., Mwaura F., Rothschild L.J.,
RA   Duboise S.M.;
RT   "Complete Genome Sequence of a Haloalkaliphilic Bacteriophage, Isolated
RT   from Lake Magadi in Kenya's Great Rift Valley.";
RL   Submitted (MAR-2014) 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; KJ534580; AHX01144.1; -; Genomic_DNA.
DR   RefSeq; YP_009037269.1; NC_024217.1.
DR   GeneID; 19527032; -.
DR   KEGG; vg:19527032; -.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000024336; 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; -; 2.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
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   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024336}.
FT   DOMAIN          3..89
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   875 AA;  99578 MW;  F8A871914F456981 CRC64;
     MINKVTKRDG TVEDFDVDNI NRWSDWASSE CGVDWSSIVF DAVRSLPEEC TTSELHQALI
     NACLSKRTEG HTKMAARLLV GQIYKEAYGC FSIPSLKDFY EEAVEEGRWV DMGYTDYELE
     QLDSVIDHTK DFTYTYATLK QMYDKYMLNF SGHPVESPQM TFMGIAMNQM RNEDDKLSKV
     ISAYQGLSNL NLNLPTPTLN GSRTSLESSP SCVVISGGDT VDSINAAINV AYTMTAQRAG
     IGIELTTRGP NDPVKGGLVR HGGKHSYYSH IDSAVKANSQ VTRGGSATVS YCVLDPEIEG
     LLTMKQQRTP ENYRIDTLDY SFKVNTSFLR RMAKNEDWML VSVYYAPTLW DLFYSGDVGA
     FEAEYQSVLS SFIPKKIVKA RDVMQAWISS RADTGRNYIT FIDNMNQHTP FNEPIRLSNL
     CVAGGTLILT DEGSLPIGQM EGQWVTVWNG SEWSEVQVVK TGIDQEMIRV YVENMETGQA
     DYLTCTPYHK WYLKDYTELR TFQLERGNEL LVWKDSEGVV TRHKVMGLLP VESQDSYCFN
     EPLRNMGVFN GILTGQCQEI ALPTKPFSSV ENLFKKHSDG TIALCFLGSI VLKDYTDEEY
     EELCYTLCKI IDNTIGDTKY PYASMEETAK GYRSIGVGMT NLAHYMASKG LAFDSEAGRN
     EIHKLAERHS YFLHKASVRL AKEKGVFKYI DRSKYKDGWI PLDTYKKEVD QFITVDNQYP
     WEELRQDILK HGVRFSVLEA QMPVESSSLV TNSTNAIYPV RNLELYKNSR KGSVYYRAPD
     MDTLHYQSAW DIPSQEMIKV YAIVQKWMGQ SISADFWHDY NKGDLKQADI IRDVLLSAKL
     GMKTWYYHNF KMKDNKRKEE TVTQIEESGC ESCSL
//