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Database: UniProt
Entry: G4VIG3_SCHMA
LinkDB: G4VIG3_SCHMA
Original site: G4VIG3_SCHMA 
ID   G4VIG3_SCHMA            Unreviewed;       837 AA.
AC   G4VIG3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_009030.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_009030.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_009030.1};
RG   WormBaseParasite;
RL   Submitted (DEC-2018) 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|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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   RefSeq; XP_018651820.1; XM_018796704.1.
DR   AlphaFoldDB; G4VIG3; -.
DR   STRING; 6183.G4VIG3; -.
DR   EnsemblMetazoa; Smp_009030.1; Smp_009030.1; Smp_009030.
DR   GeneID; 8351089; -.
DR   KEGG; smm:Smp_009030; -.
DR   WBParaSite; Smp_009030.1; Smp_009030.1; Smp_009030.
DR   CTD; 8351089; -.
DR   eggNOG; KOG1112; Eukaryota.
DR   HOGENOM; CLU_000404_1_0_1; -.
DR   InParanoid; G4VIG3; -.
DR   OMA; RGSIQNI; -.
DR   OrthoDB; 5472715at2759; -.
DR   PhylomeDB; G4VIG3; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000008854; 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:UniProtKB-UniPathway.
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:UP000008854}.
FT   DOMAIN          17..108
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   837 AA;  94931 MW;  D7B67F4A0F7AF130 CRC64;
     MSSGQKLLRE FSGIDKIYVV KRDGRNEAIH CEKITKRIRA MCYGLNESYI DVEAVTKRVV
     SGLYPGVTTV ELDNLAAETC ASMITKHHEY AILAARLAVS NLHKETKSRF SDVVEDLYCY
     INPRTKKHSP LVSKSLRDFV RENAGRLNDA IDYQRDYTYN YFGFKTLERS YLLKINGKVH
     ERPQHMLMRV SIGIHTSDID SAIETYNLMS EKWFTHASPT LFNAGTPKPQ LSSCFLITMK
     DDSIEGIYDT LKECAVISKN AGGIGLNVHN IRSLGTYIAG TNGESNGIVP MLRVFNSTAR
     YVDQGGNKRP GAFAMYLEPW HPDVFQFIEM RKNTGAEEIR ARDLFFALWI PDLFMRRVES
     NDKWTLMDPH ECPGLPEVWG EDFDTLYEKY EREGRGRQTV KAQELWYAII ECQIETGNPF
     MLYKDSCNRK SNHQHLGTIR CSNLCTEIVE YSSPDETAVC NLASISLGKF VNRDNLTFDF
     AKLQEVTKVV TRNLNKVIDV TFYPVEEARR SNMRHRPIGI GVQGLADAFC LLRYPFDSPE
     AADLNKRIFE TMYFASLDAS CQLAVDQGTY ESYQGSPVSK GILQPDMWGV DTEELSKVSG
     LDWSGLRARI NKYGLRNSLL LAPMPTASTS QILGNNESTE PFTSNVFSRR VLSGEFQIVN
     PYLLDDLTKL ELWSEELKTA IVLNQGSIQH IDGIPKELKP LYKTVWEISQ KKIIDMAAGR
     APFIDQSQSL NLHLAQPNYG KITSMHFYAW RKGLKTGMYY LRTRPAADPI KFSVDKTILR
     VLTDSTTKTN EPQNNDSIDQ TVEAIEELRI IEEIQKRNLD SIACSLNNPE GCLSCQG
//
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