ID A0A3N5BKL5_9BACI Unreviewed; 207 AA.
AC A0A3N5BKL5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
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=EDC24_0684 {ECO:0000313|EMBL:RPF55800.1};
OS Aquisalibacillus elongatus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Aquisalibacillus.
OX NCBI_TaxID=485577 {ECO:0000313|EMBL:RPF55800.1, ECO:0000313|Proteomes:UP000276443};
RN [1] {ECO:0000313|EMBL:RPF55800.1, ECO:0000313|Proteomes:UP000276443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18090 {ECO:0000313|EMBL:RPF55800.1,
RC ECO:0000313|Proteomes:UP000276443};
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 (NOV-2018) 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:RPF55800.1}.
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DR EMBL; RKRF01000007; RPF55800.1; -; Genomic_DNA.
DR RefSeq; WP_124219728.1; NZ_RKRF01000007.1.
DR AlphaFoldDB; A0A3N5BKL5; -.
DR OrthoDB; 9783592at2; -.
DR Proteomes; UP000276443; 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; NF002581; PRK02234.1-2; 1.
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:UP000276443}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT SITE 99
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
SQ SEQUENCE 207 AA; 24443 MW; FEFFA08D797AB6A4 CRC64;
MNYPKGSRKT SNKQQPTNKQ PTQFGNRGMT LEKELNETNK FYLETNRAVI HKKPIPIQVV
QVDYPKRSAA VIKEAYYQQP STTDYNGLYR GYYIDFEAKQ TNNKTSLPFA NIHEHQVKHM
KQIDEHGGIS FFIIRFKQHN ETFLLPIRPF IQVWEKQFEG KRKSIPYEYI TKHGYKIPFT
LQAKVNYLDI IDLVYFNGGD NNESKRK
//
