RUVC_PSEAE
ID RUVC_PSEAE Reviewed; 174 AA.
AC Q51424;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=PA0965;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8982068; DOI=10.1016/s0378-1119(96)00474-x;
RA Hishida T., Iwasaki H., Ishioka K., Shinagawa H.;
RT "Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and
RT ruvC, involved in processing of homologous recombination intermediates.";
RL Gene 182:63-70(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; D83138; BAA11817.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04354.1; -; Genomic_DNA.
DR PIR; JC5478; JC5478.
DR RefSeq; NP_249656.1; NC_002516.2.
DR RefSeq; WP_003112575.1; NZ_QZGE01000007.1.
DR PDB; 6LW3; X-ray; 2.38 A; A/B=1-153.
DR PDBsum; 6LW3; -.
DR AlphaFoldDB; Q51424; -.
DR SMR; Q51424; -.
DR STRING; 287.DR97_972; -.
DR PaxDb; Q51424; -.
DR PRIDE; Q51424; -.
DR EnsemblBacteria; AAG04354; AAG04354; PA0965.
DR GeneID; 882131; -.
DR KEGG; pae:PA0965; -.
DR PATRIC; fig|208964.12.peg.1003; -.
DR PseudoCAP; PA0965; -.
DR HOGENOM; CLU_091257_2_1_6; -.
DR InParanoid; Q51424; -.
DR OMA; AICHIWR; -.
DR PhylomeDB; Q51424; -.
DR BioCyc; PAER208964:G1FZ6-986-MON; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..174
FT /note="Crossover junction endodeoxyribonuclease RuvC"
FT /id="PRO_0000183121"
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"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6LW3"
FT STRAND 11..22
FT /evidence="ECO:0007829|PDB:6LW3"
FT STRAND 25..35
FT /evidence="ECO:0007829|PDB:6LW3"
FT HELIX 41..59
FT /evidence="ECO:0007829|PDB:6LW3"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6LW3"
FT HELIX 75..94
FT /evidence="ECO:0007829|PDB:6LW3"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6LW3"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:6LW3"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:6LW3"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:6LW3"
SQ SEQUENCE 174 AA; 18557 MW; E639B12CEF5FF517 CRC64;
MTLILGIDPG SRITGFGVVR ETARGCEYVA SGCIRTGNGP LHERLHVVFR SVREVIRTHG
PTALSIEQVF MARNADSALK LGQARGAAIV AAMEEGLSVA EYTASQVKQA VVGTGGADKQ
QVQMMVMHLL KLTQKPQIDA SDALAIALCH AHTQQSLVPH GLVGARRRGG RLRL
