ID RUVC_KORVE Reviewed; 166 AA. AC Q1IKI1; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 94. 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=Acid345_3618; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Koribacter. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345; RX PubMed=19201974; DOI=10.1128/aem.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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; CP000360; ABF42619.1; -; Genomic_DNA. DR RefSeq; WP_011524418.1; NC_008009.1. DR AlphaFoldDB; Q1IKI1; -. DR SMR; Q1IKI1; -. DR STRING; 204669.Acid345_3618; -. DR EnsemblBacteria; ABF42619; ABF42619; Acid345_3618. DR KEGG; aba:Acid345_3618; -. DR eggNOG; COG0817; Bacteria. DR HOGENOM; CLU_091257_3_1_0; -. DR OrthoDB; 9805499at2; -. DR Proteomes; UP000002432; 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..166 FT /note="Crossover junction endodeoxyribonuclease RuvC" FT /id="PRO_1000071027" 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 166 AA; 17759 MW; A226450F3E700D56 CRC64; MRVMGIDCGS EYTGFGIVES DDRARLHCIV AGAVHLSARD PLENKLAKIF RELCSVIREH DPEVVAIEDV FYAVNAKSAL KLGHVRGVAM LAVAECGLRV ATYAPLAVKS AVVGYGKAEK CQVQAMVARL LNLPQVPEPA DVADALAIAI CHLHTSATLT RMHAKA //