RUVC_CAMJD
ID RUVC_CAMJD Reviewed; 160 AA.
AC A7H674;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=JJD26997_2104;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000768; ABS44142.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H674; -.
DR SMR; A7H674; -.
DR EnsemblBacteria; ABS44142; ABS44142; JJD26997_2104.
DR KEGG; cjd:JJD26997_2104; -.
DR HOGENOM; CLU_091257_3_0_7; -.
DR OMA; AICHIWR; -.
DR Proteomes; UP000002302; 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..160
FT /note="Crossover junction endodeoxyribonuclease RuvC"
FT /id="PRO_1000002740"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
SQ SEQUENCE 160 AA; 17696 MW; 286E79AC765EF3A8 CRC64;
MNLKILGIDP GSKNCGYAII ERSKGKNILI EAGLIKIKPS TLQYQITELC EGLDLIFKNH
SFDEVAIEDI FFAYNPKTVL KLAQFRGALS LKILQIHGDF AEYTPLQVKK AVTGKAKATK
EQVAFMVKRL LGLSKDIKPL DITDAIAIAL THAANLRTRV