RUVC_FRATM
ID RUVC_FRATM Reviewed; 171 AA.
AC B2SH69;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=FTM_1202;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(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; CP000915; ACD31077.1; -; Genomic_DNA.
DR RefSeq; WP_003026245.1; NC_010677.1.
DR AlphaFoldDB; B2SH69; -.
DR SMR; B2SH69; -.
DR KEGG; ftm:FTM_1202; -.
DR HOGENOM; CLU_091257_2_1_6; -.
DR OMA; AICHIWR; -.
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..171
FT /note="Crossover junction endodeoxyribonuclease RuvC"
FT /id="PRO_1000090528"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 138
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"
SQ SEQUENCE 171 AA; 18297 MW; B0F8E840F4C22DAD CRC64;
MVILGIDPGS RITGFGVIKV QDNKIYYVAS GCIRITEITT PKRLKQIADG ITQIINIYAP
TEAAIEQIFM FQNPMGAIKL GQARGVAMCT LAINNLEVSE YSAKQIKQAV VGTGGAAKSQ
VQHMVQSLLG LSKKPPEDAA DALAIAICHY HSSKSLAKIS GASRVSQKRI K