ID   RUVC_PASMU              Reviewed;         190 AA.
AC   P57894;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Crossover junction endodeoxyribonuclease RuvC;
DE            EC=3.1.21.10;
DE   AltName: Full=Holliday junction nuclease RuvC;
DE   AltName: Full=Holliday junction resolvase RuvC;
GN   Name=ruvC; OrderedLocusNames=PM0978;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000305}.
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DR   EMBL; AE004439; AAK03062.1; -; Genomic_DNA.
DR   RefSeq; WP_005751719.1; NC_002663.1.
DR   AlphaFoldDB; P57894; -.
DR   SMR; P57894; -.
DR   STRING; 747.DR93_997; -.
DR   EnsemblBacteria; AAK03062; AAK03062; PM0978.
DR   KEGG; pmu:PM0978; -.
DR   HOGENOM; CLU_091257_2_1_6; -.
DR   OMA; AICHIWR; -.
DR   Proteomes; UP000000809; 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; Reference proteome.
FT   CHAIN           1..190
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_0000183115"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  20702 MW;  F9A7003CD07B9831 CRC64;
     MAIILGIDPG SRVTGYGVIR QAGRHLEYLG SGVIRTSVTD LPTRLKRIYM GVNEIILQYQ
     PDMFAIEEVF LAKNANSALK LGQARGAAIV AAVNHDLPVF EYAARLVKQT VVGIGSADKI
     QVQDMVTRIL TLSEKPQADA ADALAIAITH AHSLQHAFHV TNSAQATEKP EKTTALLKAR
     YSRGRFRLKI