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Database: UniProt
Entry: F0YEY7_AURAN
LinkDB: F0YEY7_AURAN
Original site: F0YEY7_AURAN 
ID   F0YEY7_AURAN            Unreviewed;       555 AA.
AC   F0YEY7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   Name=RRL5 {ECO:0000313|EMBL:EGB06334.1};
GN   ORFNames=AURANDRAFT_54285 {ECO:0000313|EMBL:EGB06334.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB06334.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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; GL833135; EGB06334.1; -; Genomic_DNA.
DR   RefSeq; XP_009038913.1; XM_009040665.1.
DR   AlphaFoldDB; F0YEY7; -.
DR   EnsemblProtists; EGB06334; EGB06334; AURANDRAFT_54285.
DR   GeneID; 20222377; -.
DR   KEGG; aaf:AURANDRAFT_54285; -.
DR   eggNOG; KOG1112; Eukaryota.
DR   InParanoid; F0YEY7; -.
DR   OrthoDB; 5472715at2759; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
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; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729}.
FT   DOMAIN          7..98
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   555 AA;  61980 MW;  A24A338F0116C6AD CRC64;
     MFADDDMQVV KRNGKKETVR YDKITSRIKK LCYGFDAKYI KPNQITQKVI QGVYDGVTTH
     ELDELAAQTT AYMATQHPDF SVLAARISVS NLHKSTDKTF SDVVEKLHKH VHPKTKKPAA
     LISDETYATV QKHKDAINAA IVYDRDFEYD YFGFKTLERS YLMRLDGAIA ERPQHMIMRV
     ALGIHGDDLA GAFETYEMMS QKMFTHATPT LFNAGTPRPQ LSSCFLLAMK EDSIEGIYDT
     LKRCAAISKY AGGIGLSVHN IRATDSYICG SNGTSNGIVP MLRVYNDTAR YVDQGGRRRK
     GSFAIYLEPW HADIEMWLDL KKNHGNELER ARDLFYGLWI PDLFMKRVEA NGFWSLMCPN
     ECPGLADCHG AKFEALYERY EAEGCARKAI PAQQLWFAIL DSQVETGTPY MLYKDACNGK
     SNQKHLGTIK SSNLCTEIVE YTAPDEIAVC NLASINLGSE VSGATHNSKR LGRRRFEVSG
     ATHNSKRLGR RRFDYSRGPV RGDTRRPVTG GASGWGALIR GPSLGPVRVA ETCGRAEACD
     AYLVGASWCS KVSRA
//
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