RUVC_SYNS9
ID RUVC_SYNS9 Reviewed; 154 AA.
AC Q3AYZ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
GN OrderedLocusNames=Syncc9902_0712;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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:0000255|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=3.1.21.10; 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 1 Mg(2+) ion per subunit. {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; CP000097; ABB25680.1; -; Genomic_DNA.
DR RefSeq; WP_009790266.1; NC_007513.1.
DR AlphaFoldDB; Q3AYZ7; -.
DR SMR; Q3AYZ7; -.
DR STRING; 316279.Syncc9902_0712; -.
DR EnsemblBacteria; ABB25680; ABB25680; Syncc9902_0712.
DR KEGG; sye:Syncc9902_0712; -.
DR eggNOG; COG0817; Bacteria.
DR HOGENOM; CLU_091257_3_1_3; -.
DR OMA; AICHIWR; -.
DR OrthoDB; 1815080at2; -.
DR Proteomes; UP000002712; Chromosome.
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 PROSITE; PS01321; RUVC; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..154
FT /note="Crossover junction endodeoxyribonuclease RuvC"
FT /id="PRO_1000002845"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00034"
SQ SEQUENCE 154 AA; 17037 MW; C75FA11FE797B6CA CRC64;
MRILGIDPGL ARVGYGVIDT SGGQQRMLDC GIIRTEPGYS EGDRMVVIAS DLRQLIRAWR
PELAAVEKFF FYRSSTTISV VQARGVVMMT LARFKVPVVE FPPMQIKLAL AGFGHAEKDE
VLEAVMRELN LTDPPRPDDA ADALAVALTG WFQR
