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}.
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 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
//