ID A0A498GA84_9EURY Unreviewed; 837 AA.
AC A0A498GA84;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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 ORFNames=D3D02_06590 {ECO:0000313|EMBL:RLM90421.1};
OS Halobellus sp. Atlit-38R.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=2282131 {ECO:0000313|EMBL:RLM90421.1, ECO:0000313|Proteomes:UP000277703};
RN [1] {ECO:0000313|EMBL:RLM90421.1, ECO:0000313|Proteomes:UP000277703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Atlit-38R {ECO:0000313|EMBL:RLM90421.1,
RC ECO:0000313|Proteomes:UP000277703};
RA Turgeman-Grott I.;
RT "Pervasive acquisition of CRISPR memory from multiple replicons driven by
RT inter-species mating of archaea.";
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|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:RLM90421.1}.
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DR EMBL; QXIJ01000003; RLM90421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498GA84; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000277703; 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:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
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; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000277703}.
FT DOMAIN 620..642
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 94491 MW; F09B863F96DD88FE CRC64;
MASATATQDA AIRELLDRAR RGQTDIVDDD TAADLVREAE RDLYEGASRD EVYEALINVT
TARIERDPAY KRVAAVLHLD RYFDEVTGQE PIDLLGTESE ETTDDTGTSD RDGAADYDAL
YRDTFVANVE RGVEEDLLDE RMTDGRFELD ELADALVLDR DETFEYLAAS TLTQRYFIRI
EQDGEPLELP QAFWMRIAMG LALEEDDPQE RALEFYDVLS RLLFTPSTPT LFHSGTTHPQ
LSSCYLTTVE DDLEHIFDSY KHHAQLSKWS GGLGNDWTNL RAGGALIEST GVESTGTVPF
LKISNDVTAA INRSGKRRGA ACAYLESWHL DFPEFLDLRR NTGDERRRTH DMNTAAWVPD
LFMKRVEADE EWTLFSPDEV PELHSTYGEE FEELYREYEA KAEAGELRQY ERVDAAELWR
TMLTRLFETG HPWITFKDPS NVRSPQDHVG TVHSSNLCTE ITLNTSADEH AVCNLGSVNL
GNHISGDGLD RDALAETIET AMRMLDNVVD LCFYPTDEAE YSNMRHRPIG LGVMGFHDAL
MQVGVPMGSD GAIEKSNRWQ EFVSYHAILN SSRLAKERGT YETYEGSKWD RGILPHDTVD
LLEDERGREI PTDRSETLDW GRVRDHVDEH GMRNSNTMAV APTATVSTIN GTTPSIEPIY
SNLYVKSNMS GDFTIINDRL VADLKARGLW DSEMLDRLKF HDGSIQEIDE IPDDLQELYR
GAFEIDPRHQ LQLTAHRGQW IDQSVSHNVF FPSTDGSLLD DVYKTAWRLG VKTTYYLRTL
GASQIEKSTL DMAEYGRTQR RGVGSAGDED DDGPAADDQN DDSDLARVED PTCEACQ
//
