RECU_STRS2
ID RECU_STRS2 Reviewed; 205 AA.
AC A4VZM0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SSU98_0401;
OS Streptococcus suis (strain 98HAH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391296;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98HAH33;
RX PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA Yang R., Wang J., Yu J.;
RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT of S. suis 2 Chinese isolates.";
RL PLoS ONE 2:E315-E315(2007).
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; CP000408; ABP91559.1; -; Genomic_DNA.
DR AlphaFoldDB; A4VZM0; -.
DR SMR; A4VZM0; -.
DR KEGG; ssv:SSU98_0401; -.
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..205
FT /note="Holliday junction resolvase RecU"
FT /id="PRO_1000016754"
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 205 AA; 23805 MW; EEC9AB039D01DCF8 CRC64;
MVNYPHKVSK KINRTSPISS QRVNFANRGM SFEAAINDSN QYYLAHDIAV IHKKPTPVQI
VKVDYPKRSR AKIVEAYFRQ ASTTDYSGVF KRHYIDFEAK ETRQKASMPM KNFHAHQIEH
MKQVVKQGGI CFVLLHFSTL KETYLLPATH LIEFYQVDMG SKSMPLTFIR QYGFEIQMGR
FPSIPYLEIV EKNLLGGESF ENYNN