ID   A0A0R3RWU1_9BILA        Unreviewed;      1037 AA.
AC   A0A0R3RWU1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000664701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000664701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0R3RWU1; -.
DR   STRING; 1147741.A0A0R3RWU1; -.
DR   WBParaSite; EEL_0000664701-mRNA-1; EEL_0000664701-mRNA-1; EEL_0000664701.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000050640; Unplaced.
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; IPR010754; OPA3-like.
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; PF07047; OPA3; 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}.
FT   DOMAIN          40..131
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   1037 AA;  117999 MW;  A24450682EFD25C5 CRC64;
     MSAARVVAER VYDEVVLAAD PIGTVLKTTM VRPNQRVSNS YVVKRDGRHE AVSFDKIARR
     IMKLCYGLSQ DRVDHIEISQ KVIAGLYKGV TTVELDNLAA EIAADMITKH PDYATLASRI
     AVSNLHKKTE KLFSKVSRRL YSATHPKSGR HMPLISKELF DIVQSNADIL DSAIIHERDY
     HYRYFGIKTL ERSYLLQIDG QIVERPQHML MRVALGIHGE DIEAALETYN LMSERWFTHA
     TPTLFNSGTC TPQMSSCFLL TMFEDSIEGI FETLKKCALI SKSAGGIGLN VHCIRATGSA
     IAGTNGVSNG LVPMLRVYNN AARYVDQGGN KRPGAFAIYL EPWHADIFDF LELRKNVGDE
     LERCRDLFFG LWVPDLFMER VRDDKVWSLM CPAECPGLED SWGETFEKLY TKYEEEGRYR
     KQFPARKLWE AIVFSQIETG MPYMVYKDTC NRKTNQQNLG TIKCSNLCTE VVLYSSREEI
     AVCNLASIAL NRFVTPEMVF DFNKLREVTK VVVRNLNKVI DRNYYPVPEA ERSNKRHRPI
     GIGVQGLADA FILMRYPFTS EKARNLNKRI FETVYYAALE ASCELAQEQG PYESYEGSPV
     SKGILQFDMW DVTPTDQWDW ESLREKIAVH GIRNSVLLAP MPTASTAQIL GNNESIEPYT
     SNVYTRNVLS GSFQIFNMHL MNDLMHLNLW DDDMKLAIIK NKGSIQNIER IPQEIRDLYK
     TVWEMSQRDI IDMAADRGAF IDQSQSLNIF IARPNYGNIT SMHFYGWQKG LKTGMYYLRT
     RPAVDAVQFT VDKTRLKEYS NVSADKGSKS ASDFTLDPAG ELATKMMECA ISSGDDCLIL
     LPRLIPERLE VVHDDPPNEF GLVVAFGRQM SRPLARKIIA YAIKHPYLRN RILVPVGRSL
     HAISFRLRIK SIGLAVPSKT PTVTEQQAIE MASETLVEAL IYLLTVLLIY AIYRSNPEKA
     KASDVEKYVK ENEERIIKFE EKLKEQDELT VKIVKIIREK NLDEKNILAD KGHKGQLLSF
     IGDKMKTLMP GQDKTSR
//