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 24-JAN-2024, entry version 83.
DE RecName: Full=Crossover junction endodeoxyribonuclease {ECO:0000305};
DE EC=3.1.21.10 {ECO:0000269|PubMed:11399079};
DE AltName: Full=Holliday junction resolvase {ECO:0000303|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 OrthoDB; 14179at10239; -.
DR Proteomes; UP000002270; Genome.
DR Proteomes; UP000223181; Segment.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; 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; HOLLIDAY JUNCTION RESOLVASE HJC; 1.
DR PANTHER; PTHR39651:SF1; HOLLIDAY JUNCTION RESOLVASE HJC; 1.
DR Pfam; PF01870; Hjc; 1.
DR PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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="Crossover junction endodeoxyribonuclease"
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
//
