ID RUVC_DESVH Reviewed; 166 AA. AC Q729U1; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 111. 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=DVU_2258; OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM OS B-1760 / Hildenborough). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Nitratidesulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., RA Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). 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}. 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; AE017285; AAS96731.1; -; Genomic_DNA. DR RefSeq; WP_010939533.1; NZ_CABHLV010000001.1. DR RefSeq; YP_011471.1; NC_002937.3. DR AlphaFoldDB; Q729U1; -. DR SMR; Q729U1; -. DR STRING; 882.DVU_2258; -. DR PaxDb; 882-DVU_2258; -. DR EnsemblBacteria; AAS96731; AAS96731; DVU_2258. DR KEGG; dvu:DVU_2258; -. DR PATRIC; fig|882.5.peg.2051; -. DR eggNOG; COG0817; Bacteria. DR HOGENOM; CLU_091257_2_1_7; -. DR OrthoDB; 9805499at2; -. DR PhylomeDB; Q729U1; -. DR Proteomes; UP000002194; 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; 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. 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..166 FT /note="Crossover junction endodeoxyribonuclease RuvC" FT /id="PRO_0000225140" FT ACT_SITE 11 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT ACT_SITE 70 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT ACT_SITE 142 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 11 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" FT BINDING 142 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034" SQ SEQUENCE 166 AA; 17245 MW; 5012E7E3C5FEAD66 CRC64; MAASVTVIGI DPGSQCTGWG IVREASGVLT LVDCGAIRPK GGDFAARLGD LYRQLADVVR AHTPDEAAVE DVHAAQNVAT ALKLGQARGV VVAACAAHGV PVIDYRPSVI KKALVGTGRA EKEQVGYMVG QVLGVRPDWK LDTGDALAAA ICHLNQRRLT RLAGLA //