ID   HJC_SIRV1               Reviewed;         121 AA.
AC   Q98VP9; Q5TJ92;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Holliday junction resolvase;
DE            EC=3.1.21.10 {ECO:0000269|PubMed:11399079};
GN   Name=hjc; ORFNames=121;
OS   Sulfolobus islandicus rod-shaped virus 1 (SIRV-1) (Sulfolobus virus
OS   SIRV-1).
OC   Viruses; Adnaviria; Zilligvirae; Taleaviricota; Tokiviricetes;
OC   Ligamenvirales; Rudiviridae; Icerudivirus; Icerudivirus SIRV1.
OX   NCBI_TaxID=157898;
OH   NCBI_TaxID=43080; Sulfolobus islandicus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate variant VIII;
RX   PubMed=11878892; DOI=10.1006/viro.2001.1190;
RA   Peng X., Blum H., She Q., Mallok S., Bruegger K., Garrett R.A., Zillig W.,
RA   Prangishvili D.;
RT   "Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and
RT   SIRV2: relationships to the archaeal lipothrixvirus SIFV and some eukaryal
RT   viruses.";
RL   Virology 291:226-234(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate variant XX;
RX   PubMed=15469509; DOI=10.1111/j.1365-2958.2004.04287.x;
RA   Peng X., Kessler A., Phan H., Garrett R.A., Prangishvili D.;
RT   "Multiple variants of the archaeal DNA rudivirus SIRV1 in a single host and
RT   a novel mechanism of genomic variation.";
RL   Mol. Microbiol. 54:366-375(2004).
RN   [3]
RP   FUNCTION AS A HOLLIDAY JUNCTION RESOLVASE, CATALYTIC ACTIVITY, COFACTOR,
RP   AND DNA-BINDING.
RC   STRAIN=KVEM10H3;
RX   PubMed=11399079; DOI=10.1006/jmbi.2001.4761;
RA   Birkenbihl R.P., Neef K., Prangishvili D., Kemper B.;
RT   "Holliday junction resolving enzymes of archaeal viruses SIRV1 and SIRV2.";
RL   J. Mol. Biol. 309:1067-1076(2001).
CC   -!- FUNCTION: A structure-specific endonuclease that binds and cleaves the
CC       four-way Holliday junctions in DNA created during repair and
CC       rearrangement by the ubiquitous process of homologous recombination.
CC       Introduces paired nicks in opposing strands; on immobile junction
CC       cleaves 2 bases 3' of the junction point, on mobile strands the
CC       cleavage site varies. Cleaves Y and loop-out structures with much lower
CC       efficiency. Binds 4-way junction DNA but not sequence-identical linear
CC       dsDNA. {ECO:0000269|PubMed:11399079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC         single-stranded crossover between two homologous DNA duplexes
CC         (Holliday junction).; EC=3.1.21.10;
CC         Evidence={ECO:0000269|PubMed:11399079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11399079};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Holliday junction resolvase Hjc family. Hje
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ306728; CAC37359.1; -; Genomic_DNA.
DR   EMBL; AJ414696; CAC93982.1; -; Genomic_DNA.
DR   EMBL; AJ748296; CAG38846.1; -; Genomic_DNA.
DR   RefSeq; NP_666615.1; NC_004087.1.
DR   SMR; Q98VP9; -.
DR   GeneID; 951380; -.
DR   KEGG; vg:951380; -.
DR   Proteomes; UP000002270; Genome.
DR   Proteomes; UP000223181; Genome.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR002732; Hjc.
DR   InterPro; IPR014428; Hjc_arc.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   PANTHER; PTHR39651; PTHR39651; 1.
DR   Pfam; PF01870; Hjc; 1.
DR   PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..121
FT                   /note="Holliday junction resolvase"
FT                   /id="PRO_0000342290"
FT   ACT_SITE        31
FT                   /evidence="ECO:0000255"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   SITE            55
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   121 AA;  14190 MW;  1E8E8203A39EBE9D CRC64;
     MNIRQSGKYY EYKTLEILEK NGFKALRIPV SGTGKQALPD LIATKNNTIY PIEVKSTSKD
     VVTVRNFQIE KLFKFCEIFN FCECHPLVTV YYKKYKIVIV YELSQDVRTK EKIKFKYGIN
     S