ID RUVC_MYCBO Reviewed; 188 AA. AC P66761; A0A1R3Y1N2; Q50627; X2BL50; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 104. 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=BQ2027_MB2625C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) CC DNA during genetic recombination and DNA repair. Endonuclease that CC resolves HJ intermediates. Cleaves cruciform DNA by making single- CC stranded nicks across the HJ at symmetrical positions within the CC homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; CC requires a central core of homology in the junction. The consensus CC cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side CC of the TT dinucleotide at the point of strand exchange. HJ branch CC migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds CC its consensus sequence, where it cleaves and resolves the cruciform CC DNA. {ECO:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00034}; CC Note=Binds 2 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00034}; CC -!- SUBUNIT: Homodimer which binds Holliday junction (HJ) DNA. The HJ CC becomes 2-fold symmetrical on binding to RuvC with unstacked arms; it CC has a different conformation from HJ DNA in complex with RuvA. In the CC full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms CC which resolves the HJ. {ECO:0000255|HAMAP-Rule:MF_00034}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034}. CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000255|HAMAP- CC Rule:MF_00034, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LT708304; SIU01243.1; -; Genomic_DNA. DR RefSeq; NP_856271.1; NC_002945.3. DR RefSeq; WP_003413426.1; NC_002945.4. DR AlphaFoldDB; P66761; -. DR SMR; P66761; -. DR GeneID; 45426596; -. DR PATRIC; fig|233413.5.peg.2886; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule. DR GO; GO:0008821; F:crossover junction DNA endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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; Ribonuclease H-like superfamily/Ribonuclease H; 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 NCBIfam; TIGR00228; ruvC; 1. DR PANTHER; PTHR30194; CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE RUVC; 1. DR PANTHER; PTHR30194:SF3; CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE RUVC; 1. DR Pfam; PF02075; RuvC; 1. DR PRINTS; PR00696; RSOLVASERUVC. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS01321; RUVC; 1. PE 3: Inferred from homology; KW Cytoplasm; DNA damage; DNA recombination; DNA repair; DNA-binding; KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1..188 FT /note="Crossover junction endodeoxyribonuclease RuvC" FT /id="PRO_0000183111" FT ACT_SITE 7 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT ACT_SITE 68 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT ACT_SITE 141 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 68 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 141 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" SQ SEQUENCE 188 AA; 19786 MW; 1D8619C9150406FB CRC64; MRVMGVDPGL TRCGLSLIES GRGRQLTALD VDVVRTPSDA ALAQRLLAIS DAVEHWLDTH HPEVVAIERV FSQLNVTTVM GTAQAGGVIA LAAAKRGVDV HFHTPSEVKA AVTGNGSADK AQVTAMVTKI LALQAKPTPA DAADALALAI CHCWRAPTIA RMAEATSRAE ARAAQQRHAY LAKLKAAR //