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Database: UniProt
Entry: RUVC_RHILO
LinkDB: RUVC_RHILO
Original site: RUVC_RHILO 
ID   RUVC_RHILO              Reviewed;         169 AA.
AC   Q98F72;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 110.
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}; OrderedLocusNames=mll3901;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; BA000012; BAB50695.1; -; Genomic_DNA.
DR   RefSeq; WP_010912038.1; NC_002678.2.
DR   AlphaFoldDB; Q98F72; -.
DR   SMR; Q98F72; -.
DR   KEGG; mlo:mll3901; -.
DR   PATRIC; fig|266835.9.peg.3105; -.
DR   eggNOG; COG0817; Bacteria.
DR   HOGENOM; CLU_091257_1_0_5; -.
DR   Proteomes; UP000000552; 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.
FT   CHAIN           1..169
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_0000183125"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   ACT_SITE        143
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         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
SQ   SEQUENCE   169 AA;  17840 MW;  4C8D36002C8F1518 CRC64;
     MGDAIRIIGI DPGLRRTGWG IVESLGNSLR FVASGTVRSE DKAALATRLC QLHDGLAEVL
     HAAMPHEAAV EQTFVNKDAV ATLKLGQARG IAMLVPARAG LVVAEYAPNA VKKAVIGVGH
     GDKKQIHMMV KVLLPKATFD TEHAADALAI AICHAHHRQS AAYRMALAG
//
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