RIR1_IIV3
ID RIR1_IIV3 Reviewed; 630 AA.
AC Q196Z5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN ORFNames=IIV3-065R;
OS Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=345201;
OH NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH NCBI_TaxID=42431; Culex territans.
OH NCBI_TaxID=332058; Culiseta annulata.
OH NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH NCBI_TaxID=7183; Psorophora ferox.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA Kutish G.F., Rock D.L.;
RT "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT virus).";
RL J. Virol. 80:8439-8449(2006).
CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the
CC precursors necessary for viral DNA synthesis. Allows virus growth in
CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides
CC from the corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit
CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit
CC protein complex are also active, composed of (R1)n(R2)n (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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; DQ643392; ABF82095.1; -; Genomic_DNA.
DR RefSeq; YP_654637.1; NC_008187.1.
DR SMR; Q196Z5; -.
DR GeneID; 4156315; -.
DR KEGG; vg:4156315; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001358; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 2.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Disulfide bond; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..630
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000376950"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 319
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 317..321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 459..463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 83
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 90
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 334
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 597
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 598
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 625
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 628
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 83..334
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 630 AA; 71757 MW; B4F309D57AD92677 CRC64;
MITIDESRNN LFDALGLQRL KDSYMKEDES SPQERFAFIA RQFCADDEPL AQRLYDYMSQ
HWLSPSSPQL SFGRTKQGLP IACFLPYLHD TARGLIDTWA EVSELSMIGG GIGLGVGIRQ
PDEKSVGIIP HLRTYDASCT AYKQGQTRRG SYAAYLDISH PEILSFLNTR RVGGDHNYKL
LNLHNGVNVP DSFMKKIWIL STLAPFVKMD PCPTTETLFK KAVTTLKDSR YFGADDRWLG
EVSFAALAEQ LDVVNRWDLI DPHTGKVKET IKATELWERI ILTRAETGEP YIHWIDTSNR
ALPQFQKNLG LSIRQSNLCS EVVLPTDETR TAVCCLASLN LDYFDKWCNN EQFYLDVATY
LDNVLQYFID HAPPTLKRAV HSARSERAIG IGALGFHSYL QSKMVDIESL PAYLINKKIF
KTISSHLERV NLELGELRGE APDCVGTGRR FSHMTAIAPN ATSSIIMGNT SPSCEPFRAN
IYKQDTISGS FVTYNKHLKR LLEERIPDNQ ARERVWSSIK MHDGSVQHLN QLTVQEKKVF
KTWPEINQLS LVMLAADRQK WIDQSQSTSL FFNPDERISY VHKIHLKAWL HGLKTLYYFR
SRKILTVDKV HHTTTTADPK TENDCTFCEG
