ID   D6PL20_9ZZZZ            Unreviewed;       431 AA.
AC   D6PL20;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
OS   uncultured organism MedDCM-OCT-S09-C426.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=743650 {ECO:0000313|EMBL:ADD96421.1};
RN   [1] {ECO:0000313|EMBL:ADD96421.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20393571; DOI=10.1038/ismej.2010.44;
RA   Ghai R., Martin-Cuadrado A.B., Molto A.G., Heredia I.G., Cabrera R.,
RA   Martin J., Verdu M., Deschamps P., Moreira D., Lopez-Garcia P., Mira A.,
RA   Rodriguez-Valera F.;
RT   "Metagenome of the Mediterranean deep chlorophyll maximum studied by direct
RT   and fosmid library 454 pyrosequencing.";
RL   ISME J. 4:1154-1166(2010).
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406}.
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DR   EMBL; GU943139; ADD96421.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6PL20; -.
DR   UniPathway; UPA00326; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 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};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          5..94
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   431 AA;  49975 MW;  CB5B7BB06948F28E CRC64;
     MSSNILVKKR NGRLQELNID KINLCAERAC EDLENVSWSE IVLDAHVQFY DKITTKEIDK
     ALIMSARQKI EKEPNYSYAA SRLLLATIHK EVFGESRDKD VFEEQHKLSF IKNIKSLVKE
     EILDERLLSF DLKMLSEALV TDRDLKFKYL GLQIIYDRYL HHVNERRLET PQSFWMRVAM
     GLALNEKDKN EKAIEFYNAL STFSLCCSTP TLFNSGSNHS QLSSCYLNTF DDSIDGIFEG
     LWQEARKSKY AGGLGFDCTN FRASNSYVKG TNGKSSGLIP WLKIYNDTLI AVDQGGKRPG
     AGCSYLEPWH LDIEDFLELK KNTGDERRRC HDMNTANWIP DLFIRKVQKN EDWYLFSPSD
     TRELHETYGN EFDKIYKKYC KLADSGDLEN YKIVKAKDLW KKMLRVLFET GHPWMTLKTT
     LIFATLTPMK A
//