ID A0A4V2RD21_9BACI Unreviewed; 204 AA.
AC A0A4V2RD21;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
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=EV146_109238 {ECO:0000313|EMBL:TCN23080.1};
OS Mesobacillus foraminis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Mesobacillus.
OX NCBI_TaxID=279826 {ECO:0000313|EMBL:TCN23080.1, ECO:0000313|Proteomes:UP000295689};
RN [1] {ECO:0000313|EMBL:TCN23080.1, ECO:0000313|Proteomes:UP000295689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV53 {ECO:0000313|EMBL:TCN23080.1,
RC ECO:0000313|Proteomes:UP000295689};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:TCN23080.1}.
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DR EMBL; SLVV01000009; TCN23080.1; -; Genomic_DNA.
DR RefSeq; WP_121612043.1; NZ_CP033044.1.
DR AlphaFoldDB; A0A4V2RD21; -.
DR OrthoDB; 9783592at2; -.
DR Proteomes; UP000295689; 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:UP000295689}.
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
FT SITE 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00130"
SQ SEQUENCE 204 AA; 23982 MW; B5F94B46ABCC4360 CRC64;
MNFHYPNGKR YVPKTNTAAP KIRKEKNFAY SNRGMTLEED LNETNLYYLE QNIAVIHKKP
TPVQIVNVDY PKRSAAVIKE AYFKQASTTD YNGVYKGKYI DFEAKETKFT SSFPLKNFHT
HQIRHMRDVL SHQGVCFVIL RFTSLEEVFL LEASYLLSFW DRMEEGGRKS ITKEEVEKYG
HQIPLGFQPR IDYIKVIDYL YNLS
//
