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Database: UniProt
Entry: A0A4R6U742_9BACI
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ID   A0A4R6U742_9BACI        Unreviewed;       200 AA.
AC   A0A4R6U742;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 18.
DE   RecName: Full=Holliday junction resolvase RecU {ECO:0000256|ARBA:ARBA00029523, ECO:0000256|HAMAP-Rule:MF_00130};
DE            EC=3.1.21.10 {ECO:0000256|HAMAP-Rule:MF_00130, ECO:0000256|NCBIfam:TIGR00648};
DE   AltName: Full=Recombination protein U homolog {ECO:0000256|HAMAP-Rule:MF_00130};
GN   Name=recU {ECO:0000256|HAMAP-Rule:MF_00130};
GN   ORFNames=EV213_10370 {ECO:0000313|EMBL:TDQ41492.1};
OS   Aureibacillus halotolerans.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Aureibacillus.
OX   NCBI_TaxID=1508390 {ECO:0000313|EMBL:TDQ41492.1, ECO:0000313|Proteomes:UP000295632};
RN   [1] {ECO:0000313|EMBL:TDQ41492.1, ECO:0000313|Proteomes:UP000295632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28697 {ECO:0000313|EMBL:TDQ41492.1,
RC   ECO:0000313|Proteomes:UP000295632};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that resolves Holliday junction intermediates in
CC       genetic recombination. Cleaves mobile four-strand junctions by
CC       introducing symmetrical nicks in paired strands. Promotes annealing of
CC       linear ssDNA with homologous dsDNA. Required for DNA repair, homologous
CC       recombination and chromosome segregation. {ECO:0000256|HAMAP-
CC       Rule:MF_00130}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00130};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00130};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00130};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00130}.
CC   -!- SIMILARITY: Belongs to the RecU family. {ECO:0000256|ARBA:ARBA00023447,
CC       ECO:0000256|HAMAP-Rule:MF_00130}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDQ41492.1}.
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DR   EMBL; SNYJ01000003; TDQ41492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R6U742; -.
DR   Proteomes; UP000295632; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd22354; RecU-like; 1.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   HAMAP; MF_00130; RecU; 1.
DR   InterPro; IPR004612; Resolv_RecU.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   NCBIfam; NF002584; PRK02234.1-5; 1.
DR   NCBIfam; TIGR00648; recU; 1.
DR   Pfam; PF03838; RecU; 1.
DR   PIRSF; PIRSF037785; RecU; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00130};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00130};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00130};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00130};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00130}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00130};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00130};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00130};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00130};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295632}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   SITE            100
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
SQ   SEQUENCE   200 AA;  23059 MW;  EFC32058468441EF CRC64;
     MRYPNGKPYT PASTTETAGN KSPEYARRGM TLEEDLNQSN KYYLNHGVAV IHKKPTPIQI
     VDVHYPKRSA AKITEAYFKQ PSTTDYNGVY RGHYIDFEAK ETRNAASFPM KNLHAHQLLH
     MEEIQRHGGL AFVLIRFTAS QQTFLLDATH VLHFQANLDT YKRKSMPLPY IEEHGQIIAM
     GFAPRIDYLK AVDHYYFSHL
//
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