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Database: UniProt
Entry: A0A840QQ85_9BACI
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ID   A0A840QQ85_9BACI        Unreviewed;       201 AA.
AC   A0A840QQ85;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   18-JUN-2025, entry version 12.
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=HNQ41_001781 {ECO:0000313|EMBL:MBB5173592.1};
OS   Texcoconibacillus texcoconensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Texcoconibacillus.
OX   NCBI_TaxID=1095777 {ECO:0000313|EMBL:MBB5173592.1, ECO:0000313|Proteomes:UP000551878};
RN   [1] {ECO:0000313|EMBL:MBB5173592.1, ECO:0000313|Proteomes:UP000551878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24696 {ECO:0000313|EMBL:MBB5173592.1,
RC   ECO:0000313|Proteomes:UP000551878};
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 (AUG-2020) 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:MBB5173592.1}.
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DR   EMBL; JACHHB010000007; MBB5173592.1; -; Genomic_DNA.
DR   RefSeq; WP_184664041.1; NZ_JACHHB010000007.1.
DR   AlphaFoldDB; A0A840QQ85; -.
DR   Proteomes; UP000551878; 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:UP000551878}.
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT   SITE            103
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
SQ   SEQUENCE   201 AA;  23528 MW;  88F5D972E05479BC CRC64;
     MAFRYPNGKK YVNNTQNTPK KRSQNISYSN RGMSLEKDLN ETNEYYRSRG VAVIHKKPTP
     LQIVDVDYPR RSAAVVTEAY FKKPSTTDYN GVYRGYHIDF EAKETKNKQS FPLKNFHEHQ
     IEHMQRVLQQ GGIAFAILRF TAVDETYFLS AEHLCSFYMH RQNERKSIPK SEIEEKGHLI
     PVGLHPRINY LKILDQIISN E
//
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