ID   A0A183B517_9TREM        Unreviewed;       747 AA.
AC   A0A183B517;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN   ORFNames=ECPE_LOCUS14302 {ECO:0000313|EMBL:VDP91574.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001434201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0001434201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP91574.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP91574.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-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|ARBA:ARBA00024942,
CC       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   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; UZAN01057213; VDP91574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183B517; -.
DR   WBParaSite; ECPE_0001434201-mRNA-1; ECPE_0001434201-mRNA-1; ECPE_0001434201.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; 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; -; 2.
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; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 2.
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:UP000272942}.
FT   DOMAIN          17..108
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   747 AA;  84649 MW;  7DECB94FED3CAC69 CRC64;
     MPGDQKLLRA FSGIDKIYVI KRDGSTEGVH VEKIMKRIRA LCYGLNESYI DVEAVTRRVV
     AGLYPGVTTA ELDNLAAEIC ATMTTRHYDY ETLAARLAIS NLHKKTKSKF SEVMEDLYQY
     IHPRTKRHSP LIAERVIEII RKNAERLDSA IDYQRDFNYN YFGFRTLERS YLLKIKNEVY
     ERPQHMVMRV SIGIHMDDID GAIETYNLMS EKWFTHASPT LFNAGTPKPQ LSSCFLLTMK
     EDSIEGIYDT LKQCAVISKN AGGVGLNVHC IRSLGTYIAG TNGESNGINR WGEEFEALYT
     QYEKEGRGRR TVRAQEVWHA IIQAQIETGN PFMLYKDACN RKSNQQNLGT IKCSNLCTEI
     VEYSSPEEIA VCNLASISVG HFVDPEKRTF DFEKLQYVTR VATRNLNKVI DVNFYPVEEA
     YRSNMRHRPI GLGVQGLADA FFLLRYPFDS PEAIELNRRI FETIYFAALD ASCELAEQLG
     PYESYEGCPV SKGILQPDMW GVDTEELSKV SGLDWAGLRA RIKKFGLRNS LLMAPMPTAS
     TAQILGNTES IEPQTSNVYS RRVLSGEFQI VNPYLLRDLI QLDLWSEELK SAIVANQGSI
     QHIQGIPENL KQLYKTVWEI SQKTLIDMAA ARGPFIDQSQ SLNLYLAQPS YGRITSMHFY
     GWKKGLKTGM YYLRTRPAAD PIKFTIDKTS VRALMERGVT NTSNGPTIDP EVEAQEEARI
     MEEIKRRNAE SITCSLNNPE GCLSCQG
//