RECU_ALKCK
ID RECU_ALKCK Reviewed; 207 AA.
AC Q5WGB6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Holliday junction resolvase RecU {ECO:0000255|HAMAP-Rule:MF_00130};
DE EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00130};
DE AltName: Full=Recombination protein U homolog {ECO:0000255|HAMAP-Rule:MF_00130};
GN Name=recU {ECO:0000255|HAMAP-Rule:MF_00130}; OrderedLocusNames=ABC2054;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_00130};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00130};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00130};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00130}.
CC -!- SIMILARITY: Belongs to the RecU family. {ECO:0000255|HAMAP-
CC Rule:MF_00130}.
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DR EMBL; AP006627; BAD64589.1; -; Genomic_DNA.
DR RefSeq; WP_011246897.1; NC_006582.1.
DR AlphaFoldDB; Q5WGB6; -.
DR SMR; Q5WGB6; -.
DR STRING; 66692.ABC2054; -.
DR EnsemblBacteria; BAD64589; BAD64589; ABC2054.
DR KEGG; bcl:ABC2054; -.
DR eggNOG; COG3331; Bacteria.
DR HOGENOM; CLU_096340_0_0_9; -.
DR OMA; TDYNGIY; -.
DR OrthoDB; 1756221at2; -.
DR Proteomes; UP000001168; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
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 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 Pfam; PF03838; RecU; 1.
DR PIRSF; PIRSF037785; RecU; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00648; recU; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..207
FT /note="Holliday junction resolvase RecU"
FT /id="PRO_1000016722"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT SITE 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
SQ SEQUENCE 207 AA; 23863 MW; 54E08BC1E371BA21 CRC64;
MPIRYPNGQP YSRSPKQGQA KKPLPADTYS GRGMTLEQDI DEANLYYLSQ QRAVVHKKPT
PVQIVKVDYP KRSAAVIREA YFKQASTTDY NGVYRGAYID FEAKETKNKT SFPLKNIHPH
QVDHMREVSK HGGICFVLIR FFQSAEVFLL DAKHLIDYYD NQDVRKSIKK TEIERLGHQV
KTGLHPPIDY LRTLDAVYFN GDAKERT
