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Database: UniProt
Entry: RUVC_ALKOO
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ID   RUVC_ALKOO              Reviewed;         164 AA.
AC   A8MHI5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Clos_1727;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) 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: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; CP000853; ABW19267.1; -; Genomic_DNA.
DR   RefSeq; WP_012159579.1; NC_009922.1.
DR   AlphaFoldDB; A8MHI5; -.
DR   SMR; A8MHI5; -.
DR   STRING; 350688.Clos_1727; -.
DR   KEGG; aoe:Clos_1727; -.
DR   eggNOG; COG0817; Bacteria.
DR   HOGENOM; CLU_091257_3_1_9; -.
DR   OrthoDB; 9805499at2; -.
DR   Proteomes; UP000000269; 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..164
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_1000057261"
FT   ACT_SITE        7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   ACT_SITE        140
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         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
SQ   SEQUENCE   164 AA;  18108 MW;  0930A15541E1E344 CRC64;
     MIILGIDPGL AILGYGIINY EGNRFKVLDY GAITTPSTMA TPERLKTIYR ELDRIITEYN
     PDTVAIEELF FNTNVKTALL VGHARGVAVL SAANHNKEIF EYTPLQVKQG VVGYGRADKS
     QIQQMVKTLL NLTKVPKPDD VADALAVAIC HAHTGNFTEM FKIK
//
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