RUVC_RICBR
ID RUVC_RICBR Reviewed; 157 AA.
AC Q1RHA5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
DE EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00034};
DE AltName: Full=Holliday junction nuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
DE AltName: Full=Holliday junction resolvase RuvC {ECO:0000255|HAMAP-Rule:MF_00034};
GN Name=ruvC {ECO:0000255|HAMAP-Rule:MF_00034}; OrderedLocusNames=RBE_1178;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
CC -!- FUNCTION: Nuclease that resolves Holliday junction intermediates in
CC genetic recombination. Cleaves the cruciform structure in supercoiled
CC DNA by nicking to strands with the same polarity at sites symmetrically
CC opposed at the junction in the homologous arms and leaves a 5'-terminal
CC phosphate and a 3'-terminal hydroxyl group. {ECO:0000255|HAMAP-
CC Rule:MF_00034}.
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_00034};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00034};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00034};
CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000255|HAMAP-
CC Rule:MF_00034}.
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DR EMBL; CP000087; ABE05259.1; -; Genomic_DNA.
DR RefSeq; WP_011477837.1; NC_007940.1.
DR AlphaFoldDB; Q1RHA5; -.
DR SMR; Q1RHA5; -.
DR STRING; 336407.RBE_1178; -.
DR EnsemblBacteria; ABE05259; ABE05259; RBE_1178.
DR KEGG; rbe:RBE_1178; -.
DR eggNOG; COG0817; Bacteria.
DR HOGENOM; CLU_091257_1_0_5; -.
DR OMA; AICHIWR; -.
DR OrthoDB; 1815080at2; -.
DR Proteomes; UP000001951; Chromosome.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease 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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd16962; RuvC; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00034; RuvC; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR020563; X-over_junc_endoDNase_Mg_BS.
DR InterPro; IPR002176; X-over_junc_endoDNase_RuvC.
DR PANTHER; PTHR30194; PTHR30194; 1.
DR Pfam; PF02075; RuvC; 1.
DR PRINTS; PR00696; RSOLVASERUVC.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00228; ruvC; 1.
DR PROSITE; PS01321; RUVC; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Hydrolase; Magnesium;
KW Metal-binding; Nuclease.
FT CHAIN 1..157
FT /note="Crossover junction endodeoxyribonuclease RuvC"
FT /id="PRO_0000278069"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
SQ SEQUENCE 157 AA; 17204 MW; 0E892FC688E9823C CRC64;
MIVLGIDPAL GSLGWAVVAK ESAKLKYLAS GVIKTSSKDE IHHRLSYINS ILEKVILEYK
PNMAAIEETF VNTNSVTSLK LGYARGAIMS LIGRYDLDMR EFKPNTIKKT VTGYGHAEKD
QILHMIKLLL PGTAAITNSD EADAVAIAYT CLVTKNY