RUVC_RICAE
ID RUVC_RICAE Reviewed; 157 AA.
AC C3PMF5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=RAF_ORF0148;
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5;
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(2009).
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; CP001612; ACP53115.1; -; Genomic_DNA.
DR RefSeq; WP_012719398.1; NC_012633.1.
DR AlphaFoldDB; C3PMF5; -.
DR SMR; C3PMF5; -.
DR EnsemblBacteria; ACP53115; ACP53115; RAF_ORF0148.
DR KEGG; raf:RAF_ORF0148; -.
DR HOGENOM; CLU_091257_1_0_5; -.
DR OMA; AICHIWR; -.
DR Proteomes; UP000002305; 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_1000202041"
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; 17247 MW; C688E9E833E222F4 CRC64;
MIILGIDPAL GSLGWAVVAK ENAQLKYLAS GIIRTNSKDA IHHRLAFINS TLEKVILEYQ
PNMAAIEETF VNTNSVTSLK LGYARGAIMS LIGRYNLDMR EFKPNTVKKT VTGYGHAEKD
QMLHMIKLLL SGTALITNSD EADAVAIAYT CLVTKNY