RIR2_FRG3G
ID RIR2_FRG3G Reviewed; 387 AA.
AC Q6GZQ8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative ribonucleoside-diphosphate reductase small subunit 067L;
DE EC=1.17.4.1;
GN ORFNames=FV3-067L;
OS Frog virus 3 (isolate Goorha) (FV-3).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX NCBI_TaxID=654924;
OH NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT "Comparative genomic analyses of frog virus 3, type species of the genus
RT Ranavirus (family Iridoviridae).";
RL Virology 323:70-84(2004).
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; AY548484; AAT09727.1; -; Genomic_DNA.
DR RefSeq; YP_031646.1; NC_005946.1.
DR SMR; Q6GZQ8; -.
DR PRIDE; Q6GZQ8; -.
DR GeneID; 2947767; -.
DR KEGG; vg:2947767; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008770; 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 SUPFAM; SSF47240; SSF47240; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..387
FT /note="Putative ribonucleoside-diphosphate reductase small
FT subunit 067L"
FT /id="PRO_0000410579"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 43890 MW; 4E4C594687191C0D CRC64;
MFPHVTIVEK PGCGNCVTLK RALKEKSVPH TVMPYVPGVP GSYPIATVGG QRVGYREITK
ALAMDMFTTS KCFKPFRYNW AEDIRTKHEK VHWVETEINL RDDVTDWKSG VMTPGEKAFV
SCVLRLFTQL DVEVGALYLD HLTQVFRCNE IRNMLTSFAC REAIHQKAYS LLNDTLGMPD
CEYQAFADYG EMTDKLDFMR EMDCSTLPGL ARSLLRAVLN EGVSLFAAFV MLLTFQRSGK
MKGMGKVVEW SVRDENIHVE GVSKLFETLN SEYPWVVTKD LIELFKEDAE RVAELEEAFV
DLAFQECGPV CGLEPKQVKD YVLYVINLRA ANMGLPKLIE RAPEACPIPW VKWLIDGADL
TNFFENHVTE YETGGLTGSW SYEPLDI