ID   A0A0P0YN52_9PHYC        Unreviewed;       758 AA.
AC   A0A0P0YN52;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS   Yellowstone lake phycodnavirus 3.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Prasinovirus.
OX   NCBI_TaxID=1586715 {ECO:0000313|EMBL:BAT22531.1};
RN   [1] {ECO:0000313|EMBL:BAT22531.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3 {ECO:0000313|EMBL:BAT22531.1};
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAT22531.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3 {ECO:0000313|EMBL:BAT22531.1};
RX   PubMed=26459929; DOI=10.1038/srep15131;
RA   Zhang W., Zhou J., Liu T., Yu Y., Pan Y., Yan S., Wang Y.;
RT   "Four novel algal virus genomes discovered from Yellowstone Lake
RT   metagenomes.";
RL   Sci. Rep. 5:15131-15131(2015).
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; LC015649; BAT22531.1; -; Genomic_DNA.
DR   RefSeq; YP_009174249.1; NC_028108.1.
DR   GeneID; 26100772; -.
DR   KEGG; vg:26100772; -.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000203025; 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   Early protein {ECO:0000256|ARBA:ARBA00022518};
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:UP000203025}.
FT   DOMAIN          1..94
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   758 AA;  85261 MW;  9FBAF7CB01CB04C5 CRC64;
     MKVHKRSGDA VPMLFDKVTK RISKLNEAPE FAPLKVQPDK VAQKVFTSMY DGISTTEIDN
     LTAEVAVGMI TEDPDYETLA MRVTVSNLQK TSPKTFSDAM VALHVKGIVS DHFMKCVALE
     IDSWIQPKRD YLFGYFGIRT LQKGYLNEGE TPQYLFMRVA VGIHGDDLPR VRETYDLMSQ
     KFFTHATPTL FNAGTNNPQM SSCFLVAMKD DSIEGIYETL KECAHISKWS GGIGIHCSNI
     RSSGTRINGT NGVADGIVPM LRVFNNTARY VNQGGGKRKG SFAIYLEPWH ADVMDFLELR
     LNQGDEEMRC RDLFTALWIP DLFMEKVEKD EEWHLMCPHE CPGLPDVYGE AFNELYRTYV
     AQGRFKKVVR ARDVWDRVLK SQVETGTPYM CYKDAANAKS NQKNIGAIKS SNLCTEIMEV
     SKPDETAVCN LASLCLPTFV KASSFDFAKL YEVTRVVTRN LNRVIDRNFY PTEAARKSNM
     RHRPIAIGVQ GLADVFMMLG LSFDDPKARE LNKGIFEAVY HAALLESCEL AKEDGPYETF
     KGSPASEGIL QPDMWGVTEN EFWSALKVEI KTHGLRNSLL VAPMPTASTA QIMGNNEAFE
     PYTTNIYLRR TLAGEFVMVN KHLVRDLQKI DMWSPKIKNE IVRAGGSVQA LDIPQNLKDI
     YRTVWEIPQK SIIDMAADRG AYIDQSQSLN VFMENPSLAK LSSMHMYGWH KGLKTGMYYL
     RTRAKAKAQQ VTVPVAPTPE QILACSRENP ESCAMCSG
//