ID A0A2G9NT24_9ARCH Unreviewed; 1115 AA.
AC A0A2G9NT24;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=COU54_01415 {ECO:0000313|EMBL:PIN93862.1};
OS Candidatus Pacearchaeota archaeon CG10_big_fil_rev_8_21_14_0_10_31_24.
OC Archaea; Candidatus Pacearchaeota.
OX NCBI_TaxID=1974438 {ECO:0000313|EMBL:PIN93862.1, ECO:0000313|Proteomes:UP000231401};
RN [1] {ECO:0000313|Proteomes:UP000231401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) 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:PIN93862.1}.
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DR EMBL; PFCV01000020; PIN93862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9NT24; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000231401; 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
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; TIGR01445; intein_Nterm; 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 SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 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.
DR PROSITE; PS50817; INTEIN_N_TER; 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}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00023000};
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 Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 31..123
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 1115 AA; 128323 MW; 65D508039332FF48 CRC64;
MNRKLYPSFI IKDIMSDNKN KQPRQTDRKK TYVQKRNGKL EQVSFDKVKS RIENLCDQEP
PLFEVDSSKI SIEVINRIYD GVTTTELDAQ AARICANMVT KHPEYGTLAS RLVVSNHQKN
TCVRFLIGED EHTRDRTFAE TMDMLYLTND ENGDHSPIIN KTMRDFAMKN SKHIEKIIDY
RRDYDIDFFG FKTLERAYLL KIGDDIMERP QHMWMRVAIV VTNYDLNYIP KTYNLLSNGM
YTHATPTLFN SGTVTQQLSS CFLVAMSADS LDGIYETLWS TAKISKRAGG IGIHLGNLRS
RGALIRGTNG RSLGIMPVLK LYNASAELIN QGGKRKGSYA MYFEPWHPDI FSFIEAKRGQ
TGEESSRALD LFYALWIPDR FMHAVVAAIE YENKPETEKT EKLYSQAQWY LMDPDKCPGL
QDVYGDDFEE LYQSYVDKKM YKKQIYVMDL WKEIVTSQIE SGVPYMLYKD ACNKKSNQQN
LGTIKSSNLC VSGDTRILTD NGYIEIKELM GTEQNVWNGF KFTTAKIRKT NQYQPLLRVT
TKSGLYVDVS RNHKFCLEDN KLVKAKELKV GDSLRKCEYP VIHTTNDPRM ANITTQNYVK
KLQYIRNVYT NNPMKKCYEY NPKNIEDRRE QLLILQTIGI QPYNVESKIV ILESQLNSIQ
LSVNATPSEQ FASIPAFNSE VVESIELLIG IHDTYCFAEQ ELSMGMFSGI YTHNCSEIIE
FSDEKETAVC NLCSIAVNKY VDRLPFPNSD EDYILESFNH ELLLEHMETY VRNMDNVIDA
NDYPTEEGKR SNMRHRPIGI GIQGLADTFF LLRVPFDSDI ALKLDREIFE TIYYGYLKFS
CKLAQERGKY ESFDLNGGCP LSKGLLQFDL WENFDKSLLS GRYDWDTLRE DIKTHGVRNS
LGLCCMPTAS SSQILGNVEC IEPIKSNVFK RRTLAGEFVV LNKYLVQDLI DAKLWSYEMK
QRIIAADGSI QDYPVSVPME KRDPKTARFP DIPKEMKNLY KTVWEMKQRV IIDHAGPKGR
GPFIDQSQSM NLFFEKPTAQ VITRAHIYGW REGLKTGSYY IRTRAAASAL KFTVSVNETN
TNNSAENHVD QETPEKEQEQ ELICHKEDGC WHCSA
//