ID A0A1M6LPP2_9FIRM Unreviewed; 167 AA. AC A0A1M6LPP2; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 07-APR-2021, entry version 17. DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000256|ARBA:ARBA00014685, ECO:0000256|HAMAP-Rule:MF_00034}; DE EC=3.1.22.4 {ECO:0000256|ARBA:ARBA00012051, ECO:0000256|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction nuclease RuvC {ECO:0000256|ARBA:ARBA00020124, ECO:0000256|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction resolvase RuvC {ECO:0000256|ARBA:ARBA00019848, 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; Firmicutes; Clostridia; Clostridiales; 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: 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:0000256|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=3.1.22.4; CC Evidence={ECO:0000256|ARBA:ARBA00000362, 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 1 Mg(2+) ion per subunit. {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 EnsemblBacteria; SHJ73166; SHJ73166; SAMN02745227_00598. DR Proteomes; UP000243547; Unassembled WGS sequence. 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 {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}; Endonuclease {ECO:0000313|EMBL:SHJ73166.1}; 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|HAMAP-Rule:MF_00034}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00034}; KW Reference proteome {ECO:0000313|Proteomes:UP000243547}. FT METAL 7 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT METAL 67 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT METAL 140 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034" FT METAL 143 FT /note="Magnesium" 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 //