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Database: UniProt
Entry: A0A418UZL8_9DEIO
LinkDB: A0A418UZL8_9DEIO
Original site: A0A418UZL8_9DEIO 
ID   A0A418UZL8_9DEIO        Unreviewed;       695 AA.
AC   A0A418UZL8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
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=nrdE {ECO:0000313|EMBL:RJF68917.1};
GN   ORFNames=D3875_21445 {ECO:0000313|EMBL:RJF68917.1};
OS   Deinococcus cavernae.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2320857 {ECO:0000313|EMBL:RJF68917.1, ECO:0000313|Proteomes:UP000286287};
RN   [1] {ECO:0000313|EMBL:RJF68917.1, ECO:0000313|Proteomes:UP000286287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2S05-167 {ECO:0000313|EMBL:RJF68917.1,
RC   ECO:0000313|Proteomes:UP000286287};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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|ARBA:ARBA00000206,
CC         ECO:0000256|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RJF68917.1}.
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DR   EMBL; QYUJ01000030; RJF68917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418UZL8; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000286287; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:UniProtKB-UniPathway.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573:SF30; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286287}.
FT   DOMAIN          553..575
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   695 AA;  78403 MW;  927B0BC6D8B07FFE CRC64;
     MEPWIELNNK VLAGSAVDTR FDTDALQVYF QEKVNPNTVF FHDLAEKIRY LTEHGVWDRA
     IFERYRPEEV QAVFDRAYSY KFRFRSFMGA YKFYSEYATM TPNRTRWLER YEDRLSITAL
     SRSETVEDAL ELVHHLVNQT FTPATPTLMN AGKANTGRLV SCFLLQDCTD NLDSITKTLA
     FVAELSKGGG GIGVEVSNLR ARGEALRGIQ NVTKGVMGVA KMLDNMLRYA DQAGQRPGAG
     AVYLSVMHAD FSDLLNAKKI ATDEDARLKT LSVGATIPDV FMEKVRAGED IYQFYPHSLF
     QHTGREFTDI DWTREYQALA DNPLIRKKRV PARRVLEDIA VTQGESGYPY LLFEGHANRA
     NPIPNVGSIK MSNLCSEILQ PTTPSYFHSY GQEHRDRIGL DVSCNLASLV IEQTMHSGEI
     GRVVGAAVRM LDHVARSTSI TEVPAVRRAN DEMRSIGLGA MGLHSFLAGK ELIYGSPEAL
     EFVDVFFAAV HYHARKASME IARETGFVFG GFEGSRYQSG EHFAQYLERD FHPQTPEVAA
     LFEGHTLPTR ADWRQLVQDI RTHGLAHSFV MAIAPTGSIS YVSHASASIM PITEKVETRT
     SNKARTIYPM PHLSDDTEWY YEEAYDMDQR RVLDTVAAAQ RHVDQGISCT LFVPASATTR
     TLQRYYLYAY RLGIKTLYYT RLRKTNVQDC LSCVV
//
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