RIR2_IIV3
ID RIR2_IIV3 Reviewed; 376 AA.
AC Q197B2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Probable ribonucleoside-diphosphate reductase small subunit 048L;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN ORFNames=IIV3-048L;
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {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 small
CC chain family. {ECO:0000305}.
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DR EMBL; DQ643392; ABF82078.1; -; Genomic_DNA.
DR RefSeq; YP_654620.1; NC_008187.1.
DR SMR; Q197B2; -.
DR GeneID; 4156298; -.
DR KEGG; vg:4156298; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001358; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Probable ribonucleoside-diphosphate reductase small
FT subunit 048L"
FT /id="PRO_0000376909"
FT ACT_SITE 147
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 44070 MW; 8D3716EF3DA19D30 CRC64;
MEYEHLWLTA YGCLAVVGAV VVYCAIKQSL VTNWWFYGSI YPQVKLMADR TTFKPFEYPG
CYDKWDTHEH AHWSFKELNM QDDVHDWHNR LSEAEKTFLV QILRFFTQGD VDVAVGYVQY
LQLFQQPEVR MMLFSFGARE AMHIASYSHL ISTLNLPDVT YQEFLKYKAM KDKHEFVFNS
RFKSTTVGRF FNYLLFGYDT HLEEIAVKIA LFSAFIEGVQ LFSSFIMLLN FTRHGLMKKM
GQIIQWSIAD ETHHTNSMME LFSTLVVENK SHIRLGVLEA RVRDTARKIV QLEDGFIDLA
FSMGEMRQLT ADDVKSYIRY ITNRRLQTMG YLPLYSVVEN PLPWVEDLLN APSHTNFFEN
KPTEYAKASL TGDWPW
