G5_VACCW
ID G5_VACCW Reviewed; 434 AA.
AC Q80HX0; Q85325;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Putative nuclease G5;
DE EC=3.1.-.-;
GN Name=VACWR082; ORFNames=G5R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2024483; DOI=10.1016/0042-6822(91)90585-y;
RA Meis R.J., Condit R.C.;
RT "Genetic and molecular biological characterization of a vaccinia virus gene
RT which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT).";
RL Virology 182:442-454(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15367589; DOI=10.1128/jvi.78.19.10238-10248.2004;
RA da Fonseca F.G., Weisberg A.S., Caeiro M.F., Moss B.;
RT "Vaccinia virus mutants with alanine substitutions in the conserved G5R
RT gene fail to initiate morphogenesis at the nonpermissive temperature.";
RL J. Virol. 78:10238-10248(2004).
RN [4]
RP SIMILARITY.
RX PubMed=17021162; DOI=10.1093/bioinformatics/btl506;
RA Da Silva M., Shen L., Tcherepanov V., Watson C., Upton C.;
RT "Predicted function of the vaccinia virus G5R protein.";
RL Bioinformatics 22:2846-2850(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-33 AND ASP-198.
RX PubMed=19805122; DOI=10.1073/pnas.0909529106;
RA Senkevich T.G., Koonin E.V., Moss B.;
RT "Predicted poxvirus FEN1-like nuclease required for homologous
RT recombination, double-strand break repair and full-size genome formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17921-17926(2009).
CC -!- FUNCTION: Putative nuclease that seems to be required for double-strand
CC break repair, homologous recombination, and production of full-length
CC viral genomic DNA. {ECO:0000269|PubMed:15367589,
CC ECO:0000269|PubMed:19805122}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15367589}.
CC Note=Present in the virion core.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:15367589}.
CC -!- DISRUPTION PHENOTYPE: When G5 is deleted, most of the DNA made in
CC infected cells is not packaged in virus particles.
CC {ECO:0000269|PubMed:19805122}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC subfamily. {ECO:0000305}.
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DR EMBL; J03399; AAB59815.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89361.1; -; Genomic_DNA.
DR RefSeq; YP_232964.1; NC_006998.1.
DR DNASU; 3707538; -.
DR GeneID; 3707538; -.
DR KEGG; vg:3707538; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR007678; Poxvirus_G5.
DR Pfam; PF04599; Pox_G5; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Early protein; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome; Virion.
FT CHAIN 1..434
FT /note="Putative nuclease G5"
FT /id="PRO_0000412281"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 33
FT /note="D->A: Complete loss of function."
FT /evidence="ECO:0000269|PubMed:19805122"
FT MUTAGEN 198
FT /note="D->A: Complete loss of function."
FT /evidence="ECO:0000269|PubMed:19805122"
SQ SEQUENCE 434 AA; 49847 MW; 194E91E093D98F06 CRC64;
MGIKNLKSLL LENKSLTILD DNLYKVYNGI FVDTMSIYIA VANCVRNLEE LTTVFIKYVN
GWVKKGGHVT LFIDRGSIKI KQDVRDKRRK YSKLTKDRKM LELEKCTSEI QNVTGFMEEE
IKAEMQLKID KLTFQIYLSD SDNIKISLNE ILTHFNNNEN VTLFYCDERD AEFVMCLEAK
THFSTTGEWP LIISTDQDTM LFASADNHPK MIKNLTQLFK YVPSAEDNYL AKLTALVNGC
DFFPGLYGAS ITPNNLNKIQ LFSDFTIDNI VTSLAIKNYY RKTNSTVDVR NIVTFINDYA
NLDDVYSYIP PCQCTVQEFI FSALDEKWNE FKSSYLESVP LPCQLMYALE PRKEIDVSEV
KTLSSYIDFE NTKSDIDVIK SISSIFGYSN ENCNTIVFGI YKDNLLLSIN SSFYFNDSLL
ITNTKSDNII NIGY
