ID RUVV_VACCW Reviewed; 187 AA.
AC Q80HV3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 22-FEB-2023, entry version 71.
DE RecName: Full=Resolvase OPG149;
DE EC=3.1.-.-;
DE AltName: Full=DNA holliday junction resolvase A22;
GN Name=OPG149; OrderedLocusNames=VACWR142; ORFNames=A22R;
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 [LARGE SCALE 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 [2]
RP PALMITOYLATION.
RX PubMed=11017799; DOI=10.1006/viro.2000.0522;
RA Grosenbach D.W., Hansen S.G., Hruby D.E.;
RT "Identification and analysis of vaccinia virus palmitylproteins.";
RL Virology 275:193-206(2000).
RN [3]
RP FUNCTION.
RX PubMed=10890916; DOI=10.1073/pnas.150238697;
RA Garcia A.D., Aravind L., Koonin E.V., Moss B.;
RT "Bacterial-type DNA holliday junction resolvases in eukaryotic viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8926-8931(2000).
RN [4]
RP FUNCTION.
RX PubMed=11413313; DOI=10.1128/jvi.75.14.6460-6471.2001;
RA Garcia A.D., Moss B.;
RT "Repression of vaccinia virus Holliday junction resolvase inhibits
RT processing of viral DNA into unit-length genomes.";
RL J. Virol. 75:6460-6471(2001).
RN [5]
RP FUNCTION.
RX PubMed=16781759; DOI=10.1016/j.virol.2006.05.007;
RA Culyba M.J., Harrison J.E., Hwang Y., Bushman F.D.;
RT "DNA cleavage by the A22R resolvase of vaccinia virus.";
RL Virology 352:466-476(2006).
CC -!- FUNCTION: Plays a role in DNA replication by cleaving viral DNA
CC concatamers to yield unit-length viral genomes. The concatamer
CC junctions contain inverted repeat sequences that can be extruded as
CC cruciforms, yielding Holliday junctions that A22 protein cleaves.
CC {ECO:0000269|PubMed:10890916, ECO:0000269|PubMed:11413313,
CC ECO:0000269|PubMed:16781759}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16781759};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:16781759};
CC -!- SIMILARITY: Belongs to the RuvC family. Poxviruses-type subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially reported be palmyoylated (PubMed:11017799).
CC However, additional data are required to confirm this result.
CC {ECO:0000305|PubMed:11017799}.
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DR EMBL; AY243312; AAO89421.1; -; Genomic_DNA.
DR RefSeq; YP_233024.1; NC_006998.1.
DR SMR; Q80HV3; -.
DR DNASU; 3707672; -.
DR GeneID; 3707672; -.
DR KEGG; vg:3707672; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR006932; HJ-resolvase_A22.
DR InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF04848; Pox_A22; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Hydrolase; Magnesium; Nuclease;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..187
FT /note="Resolvase OPG149"
FT /id="PRO_0000183157"
SQ SEQUENCE 187 AA; 21879 MW; D531DE38A944DF92 CRC64;
METLTSSSQS LISSPMSKKD YSSEIICAFD IGAKNPARTV LEVKDNSVRV LDISKLDWSS
DWERRIAKDL SQYEYTTVLL ERQPRRSPYV KFIYFIKGFL YHTSAAKVIC VSPVMSGNSY
RDRKKRSVEA FLDWMDTFGL RDSVPDRRKL DDVADSFNLA MRYVLDKWNT NYTPYNRCKS
RNYIKKM
//
