ID A0A1M6LPP2_9FIRM Unreviewed; 167 AA. AC A0A1M6LPP2; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 24-JAN-2024, entry version 29. DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000256|HAMAP-Rule:MF_00034}; DE EC=3.1.21.10 {ECO:0000256|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction nuclease RuvC {ECO:0000256|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction resolvase RuvC {ECO:0000256|HAMAP-Rule:MF_00034}; GN Name=ruvC {ECO:0000256|HAMAP-Rule:MF_00034}; GN ORFNames=SAMN02745227_00598 {ECO:0000313|EMBL:SHJ73166.1}; OS Anaerobranca californiensis DSM 14826. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteinivoraceae; OC Anaerobranca. OX NCBI_TaxID=1120989 {ECO:0000313|EMBL:SHJ73166.1, ECO:0000313|Proteomes:UP000243547}; RN [1] {ECO:0000313|Proteomes:UP000243547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14826 {ECO:0000313|Proteomes:UP000243547}; RA Varghese N., Submissions S.; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP- CC Rule:MF_00034}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00034}; CC Note=Binds 2 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00034}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00034}. CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000256|ARBA:ARBA00009518, CC ECO:0000256|HAMAP-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; FRAI01000005; SHJ73166.1; -; Genomic_DNA. DR RefSeq; WP_072906180.1; NZ_FRAI01000005.1. DR AlphaFoldDB; A0A1M6LPP2; -. DR STRING; 1120989.SAMN02745227_00598; -. DR OrthoDB; 9805499at2; -. DR Proteomes; UP000243547; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00034}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00034}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00034}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00034}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00034}; KW Reference proteome {ECO:0000313|Proteomes:UP000243547}. FT ACT_SITE 7 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT ACT_SITE 67 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT ACT_SITE 140 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT BINDING 140 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" SQ SEQUENCE 167 AA; 18526 MW; DCBA77F85DDA0A86 CRC64; MRIMGIDPGL AIVGFGIIDL DVRKVKVVDY GTIQTDNSLC YTDRLLCVGN SLEKILKIYQ PDVVAIEELF FNKNSKTAFA ISQVRGVIIY TVLKKEIPLY EYTPLQVKQG VVGYGRATKN QVQLMVKNLL NLKEIPKPDD AADGLAVALC HKNFLRSNGI NLQGVVK //