ID   A0A0P0YNQ3_9PHYC        Unreviewed;       761 AA.
AC   A0A0P0YNQ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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:BAT22615.1};
RN   [1] {ECO:0000313|EMBL:BAT22615.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3 {ECO:0000313|EMBL:BAT22615.1};
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAT22615.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3 {ECO:0000313|EMBL:BAT22615.1};
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}.
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DR   EMBL; LC015649; BAT22615.1; -; Genomic_DNA.
DR   RefSeq; YP_009174333.1; NC_028108.1.
DR   GeneID; 26100856; -.
DR   KEGG; vg:26100856; -.
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   761 AA;  85677 MW;  18048E0AB0A156A8 CRC64;
     MKVYKRSGDE VPMLFDKVTK RISKLNEAPE FEPLKVQPDK VAQKVFTSMY DGISTTEIDN
     LTAEVAVGMI TEDPDYETLA MRVTVSNMQK TSPKTFSDAM VALHVKGIVS DHFMKCVALE
     LDAVIQPKRD YLFGYFGIKT LQKGYLNVGE TPQYLFMRVA VGIHGDDLPR VKETYDLMSQ
     KFFTHATPTL FNAGTNNPQM SSCFLVAMKD DSIEGIYETL KECAHISKWS GGIGIHCSNI
     RASGTRINGT NGVADGIVPM LRVFNNTARY VNQGGGKRKG SFAIYLEPWH ADIMDFLELR
     LNQGDEEMRC RDLFTALWIP DLFMEKVEKD EDWHLMCPHE CPGLPDVYGE AFNELYRTYV
     AQGRYKKVVR ARDIWDGVLK SQVETGTPYM CYKDACNEKS NQKNIGTIKS SNLCTEIIEV
     SSPDETAVCN LASLCLPTFI KGNHFDFAKL YEVTRVVTRN LNRVIDRNFY PTEAARKSNM
     RHRPIAIGVQ GLADVFMMLG LSFDETKARE LNKGIFEAVY HAALLESCEL AKEEGSYETF
     KGSPASEGIL QPDMWGIAAN EFWDGLKVEI KTHGLRNSLL VAPMPTASTA QIMGNNEAFE
     PYTTNIYLRR TLAGEFVMIN RHLVRDLQKI NRWNPQIKNE IVRAGGSVQA LDIQEELKAI
     YRTIWEIPQK SVIDMAADRG AYIDQSQSLN IFMENPSLAK LSSMHLYGWK KGLKTGMYYL
     RTRAKARAQQ VTVPVATAKP TEEDILACSR ENPESCAMCS G
//