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Database: UniProt
Entry: RUVC_PROA2
LinkDB: RUVC_PROA2
Original site: RUVC_PROA2 
ID   RUVC_PROA2              Reviewed;         187 AA.
AC   B4S5F6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, 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=Paes_0497;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) 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; CP001108; ACF45553.1; -; Genomic_DNA.
DR   RefSeq; WP_012505090.1; NC_011059.1.
DR   AlphaFoldDB; B4S5F6; -.
DR   SMR; B4S5F6; -.
DR   STRING; 290512.Paes_0497; -.
DR   KEGG; paa:Paes_0497; -.
DR   eggNOG; COG0817; Bacteria.
DR   HOGENOM; CLU_091257_3_1_10; -.
DR   Proteomes; UP000002725; 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..187
FT                   /note="Crossover junction endodeoxyribonuclease RuvC"
FT                   /id="PRO_1000090547"
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   187 AA;  20274 MW;  667030E303FE6C2D CRC64;
     MIVLGVDPGS VHTGYGVVLC NGQKFSLVAC GLIRLSSNQS IADRIKIIYD ELGAIIAEYN
     PQRLALETAY VNRNPQSALK LGQVRGAIVA LTMNKGLELH EYAPREVKYV LTGKGSAGKE
     QVSYMARHFL NIQEPIKPYD VTDALGIALC DLLCDAKGGS PRRGSGSRKS ARGGWEDFVR
     TNPELIV
//
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