RECU_STRT1
ID RECU_STRT1 Reviewed; 198 AA.
AC Q5M1K7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=str0231;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV61845.1; -; Genomic_DNA.
DR RefSeq; WP_002949408.1; NC_006449.1.
DR AlphaFoldDB; Q5M1K7; -.
DR SMR; Q5M1K7; -.
DR GeneID; 66898162; -.
DR KEGG; stc:str0231; -.
DR HOGENOM; CLU_096340_0_0_9; -.
DR OMA; TDYNGIY; -.
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.
FT CHAIN 1..198
FT /note="Holliday junction resolvase RecU"
FT /id="PRO_1000016757"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT SITE 100
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
SQ SEQUENCE 198 AA; 22827 MW; 7488D6A0C5CC271F CRC64;
MVNYPHQISR KIAQVRTKKS NRVDFANRGM NFESAINATN DYYLSRGLAV IHKKPTPVQI
VKVDYPKRSR AKIVEAYFRQ ASTTDYSGVY KGYYIDFEAK ETRQKTSMPM KNFHAHQIKH
MSQVINQDGI CFVLLHFSTL KETYLLPAKD LIAFYQIDKG TKSMPLDYIK KRGYAIAESA
YPQVPYLEII EKLLGGNT