ID A0A1E7FRA2_9STRA Unreviewed; 789 AA.
AC A0A1E7FRA2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=FRACYDRAFT_205957 {ECO:0000313|EMBL:OEU20689.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU20689.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU20689.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU20689.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; KV784354; OEU20689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7FRA2; -.
DR EnsemblProtists; OEU20689; OEU20689; FRACYDRAFT_205957.
DR KEGG; fcy:FRACYDRAFT_205957; -.
DR InParanoid; A0A1E7FRA2; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000095751; 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 CDD; cd01679; RNR_I; 1.
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; 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.
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};
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:UP000095751}.
FT DOMAIN 1..62
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 789 AA; 89006 MW; F6CAF7E99E21794A CRC64;
MTKLDLESLT QSILRGMYPD VTSYEIDTLA AETAASMATQ HVLYARLAAR ILVSLNQRYT
SRTFSQAMKV LNDETNYINP EIVDIVRRRG DEINERICDE RDLEITYFGF KTLERSYLLK
ADDGRILERP QYLFMRVALG IHCAGRSSSM MSEEEENKCL QAAFETYDLM SEGYFTHASP
TLFHSGTTHP QLSSCFLIQM SDDSISGIYD TLKRCAVISK AAGGIGLSVH NIRARGSPIR
GTRGVSNGLV PMLRVYDVTS RYVDQGGGKR PGAFAVYIEP WHGDIFDVLN LKKNHGKEEQ
RARDLFYGLW IPDLFMQRVE DDEVWSLMCP SLCPGLAECH GEEFEELYEK YEREGRYTRQ
VRAREVWSAI LESQIETGTP YMLFKDAANK KSNQKNLGTI QCSNLCTEII QYTDEEEVAV
CNLASICLPK FVVSDRGTYG SVDPDSGRAY FDHEALHKTT KTITRNLNRI IDINSYPIPG
AKTSNQRHRP IGLGVSGLAD AFIRLGLPFT CDKAKELNEA IFETIYHAAL EASIELAEEE
GHYETFIGSP ASKGEFQFDM WGIRADTLPS KRIKNGEAFL GKYPEAYQAE GYDWEKLRDS
MVKNGMRNSL LLAPMPTAST SQILGVNECF EPFSSNLYVR RVKAGEFIMA NPHLLQDLTD
RGLWTPEVRN QLMRDGGSVA NIDAVPSRLK EIYKTVWEIK MKIIIDMASD RGKFIDQSQS
LNLFIADPTT DKLTAMHFYA WKKGLKTGMY YLRTKPAVNA IQYTVEKGSV PSNSVPIVDD
EDVCMSCQS
//
