ID A0A090L1J7_STRRB Unreviewed; 806 AA.
AC A0A090L1J7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=SRAE_1000191400 {ECO:0000313|EMBL:CEF63656.1,
GN ECO:0000313|WBParaSite:SRAE_1000191400.1,
GN ECO:0000313|WormBase:SRAE_1000191400};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63656.1};
RN [1] {ECO:0000313|EMBL:CEF63656.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000191400.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF63656.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000191400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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 EMBL; LN609528; CEF63656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L1J7; -.
DR STRING; 34506.A0A090L1J7; -.
DR EnsemblMetazoa; SRAE_1000191400.1; SRAE_1000191400.1; WBGene00258526.
DR WBParaSite; SRAE_1000191400.1; SRAE_1000191400.1; WBGene00258526.
DR WormBase; SRAE_1000191400; SRP03545; WBGene00258526; -.
DR eggNOG; KOG1112; Eukaryota.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000035682; Chromosome X.
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; PF03477; ATP-cone; 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:UP000035682}.
FT DOMAIN 7..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 806 AA; 91464 MW; C9638565CC5AE014 CRC64;
MKRTNSLYVE KRDGRRENVH FDKITSRISK LCYKLNMDYI DPCLVTFKVI QGLYNGVSTV
ELDNLAAEVS ASMTTIHPDY AILAARIAVS NMHKQTKKSF SEAMSDLYNY RHSVTGVHLP
MISEETHNII KKHADKLNSA IVYNRDFDFS YFGFKTLERS YLLKINGKVA ERPQHLLMRV
AVGIHGDDIN SVIETYDYMS QKWFTHASPT LFNAGTRRPQ LSSCFLLTMS DDSIEGIYDT
LKQCALISKS AGGIGLNVHC IRANGSFIGG TNGTSNGLIP MLRVFNNTAR YVDQGGNKRP
GAFAIYLEPW HADILEFLDL KKNTGPEEER ARDLFYGLWI PDLFMKRVEK DSYWSLMCPH
ECPGLEDTWG EAFEELYHKY ENEKRYRKQI KARVIWQKIC ESQIETGTPY MVYKDHCNRK
SNQQNLGTIK CSNLCTEIVE YCAPDEVAVC NLGSIALNRF VEVVDGKPAF NFKQLHVVSK
ILTKNLNKII DVNYYPVPEA RKSNMRHRPI GIGVQGLADA FMLMRYPFTS PAAKELNKLI
FETIYHGALE ASCEVAERDG PYETYDGSPV SKGILQYDMW NVKPSDLWDW ETLKADIAKH
GVRNSLLLAP MPTASTAQIL GNNESIEPYT SNIYTRRVLS GDFQIVNPHL LKDLIDLNIW
SEELMNEIIA NNGSIQNIKE IPPNIKELYK TVWEISQKDI IEMAADRGAF IDQSQSLNLH
VAKPSYAICS SMHFHSWKRG LKTGMYYLRT KPAADAVKFS VDKSAIQNSS KTPLGEKHDN
AKENVMKGKV NSIREEDESM CLSCSG
//
