ID   RUSA_ECOUT              Reviewed;         120 AA.
AC   Q1RCY4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=UTI89_C1298;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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. Corrects the defects in
CC       genetic recombination and DNA repair associated with inactivation of
CC       RuvAB or RuvC (By similarity). {ECO:0000250}.
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}.
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DR   EMBL; CP000243; ABE06780.1; -; Genomic_DNA.
DR   RefSeq; WP_001099712.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1RCY4; -.
DR   SMR; Q1RCY4; -.
DR   KEGG; eci:UTI89_C1298; -.
DR   HOGENOM; CLU_139466_0_2_6; -.
DR   Proteomes; UP000001952; 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.
FT   CHAIN           1..120
FT                   /note="Crossover junction endodeoxyribonuclease RusA"
FT                   /id="PRO_0000324833"
FT   REGION          13..16
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          66..73
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   120 AA;  13846 MW;  38401669E8819EA6 CRC64;
     MNTYSITLPW PPSNNRYYRH NRGRTHVSAE GQAYRDNVAR IIKNAMLDIG LAMPVKIRIE
     CHMPDRRRRD LDNLQKAAFD ALTKAGFWLD DAQVVDYRVV KMPVTKGGRL ELTITEMGNE
//