ID RUSA_AQUAE Reviewed; 126 AA. AC O67766; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 27-MAR-2024, entry version 115. DE RecName: Full=Crossover junction endodeoxyribonuclease RusA; DE EC=3.1.21.10; DE AltName: Full=Holliday junction nuclease RusA; DE AltName: Full=Holliday junction resolvase; GN Name=rusA; OrderedLocusNames=aq_1953; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). RN [2] RP FUNCTION. RX PubMed=11972790; DOI=10.1046/j.1365-2958.2002.02916.x; RA Sharples G.J., Bolt E.L., Lloyd R.G.; RT "RusA proteins from the extreme thermophile Aquifex aeolicus and RT lactococcal phage r1t resolve Holliday junctions."; RL Mol. Microbiol. 44:549-559(2002). CC -!- FUNCTION: Endonuclease that resolves Holliday junction intermediates CC made during homologous genetic recombination and DNA repair. Exhibits CC sequence and structure-selective cleavage of four-way DNA junctions, CC where it introduces symmetrical nicks in two strands of the same CC polarity at the 5' side of CC dinucleotides. CC {ECO:0000269|PubMed:11972790}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RusA family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC07739.1; Type=Erroneous initiation; Evidence={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; AE000657; AAC07739.1; ALT_INIT; Genomic_DNA. DR PIR; B70467; B70467. DR RefSeq; NP_214335.1; NC_000918.1. DR AlphaFoldDB; O67766; -. DR SMR; O67766; -. DR STRING; 224324.aq_1953; -. DR EnsemblBacteria; AAC07739; AAC07739; aq_1953. DR KEGG; aae:aq_1953; -. DR eggNOG; COG4570; Bacteria. DR HOGENOM; CLU_139466_1_0_0; -. DR InParanoid; O67766; -. DR OrthoDB; 14362at2; -. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0008821; F:crossover junction DNA endonuclease activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.30.1330.70; Holliday junction resolvase RusA; 1. DR InterPro; IPR016281; Endonuclease_RusA. DR InterPro; IPR008822; Endonuclease_RusA-like. DR InterPro; IPR036614; RusA-like_sf. DR Pfam; PF05866; RusA; 1. DR PIRSF; PIRSF001007; RusA; 1. DR SUPFAM; SSF103084; Holliday junction resolvase RusA; 1. PE 3: Inferred from homology; KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1..126 FT /note="Crossover junction endodeoxyribonuclease RusA" FT /id="PRO_0000192008" FT BINDING 76 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" SQ SEQUENCE 126 AA; 14778 MW; 05BC64FAA7B9F9B1 CRC64; MISEMEEIEL YLSKLPVPKS NRYIRPKGGK VFKPPRVTNW EARAIWELRE QFKGDAIDYE ISVDITLILP NRRKRDIDNM LKSLWDVMEK AGVIKNDNLI FEVHTVKKIE KGKEGVIIKI RPFQSP //