ID F5YP63_TREPZ Unreviewed; 226 AA.
AC F5YP63;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000256|HAMAP-Rule:MF_00034};
DE EC=3.1.21.10 {ECO:0000256|HAMAP-Rule:MF_00034};
DE AltName: Full=Holliday junction nuclease RuvC {ECO:0000256|HAMAP-Rule:MF_00034};
DE AltName: Full=Holliday junction resolvase RuvC {ECO:0000256|HAMAP-Rule:MF_00034};
GN Name=ruvC {ECO:0000256|HAMAP-Rule:MF_00034};
GN OrderedLocusNames=TREPR_2937 {ECO:0000313|EMBL:AEF84040.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84040.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF84040.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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:0000256|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: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 2 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00034}.
CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000256|ARBA:ARBA00009518,
CC ECO:0000256|HAMAP-Rule:MF_00034}.
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DR EMBL; CP001843; AEF84040.1; -; Genomic_DNA.
DR AlphaFoldDB; F5YP63; -.
DR STRING; 545694.TREPR_2937; -.
DR KEGG; tpi:TREPR_2937; -.
DR eggNOG; COG0817; Bacteria.
DR HOGENOM; CLU_091257_3_2_12; -.
DR Proteomes; UP000009223; 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 {ECO:0000256|HAMAP-Rule:MF_00034};
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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00034};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00034};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00034, ECO:0000313|EMBL:AEF84040.1};
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|HAMAP-Rule:MF_00034};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT ACT_SITE 136
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT ACT_SITE 209
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
SQ SEQUENCE 226 AA; 23251 MW; E17D8BE463A6BFDF CRC64;
MSRSKKAAAE PPAGPVSPAK QPAPAKTGAG VAKPPASGTA GTGLLLKAGA VKASTAKAET
GSLVKASAAR RIIGVDPGLA STGWGVIDIR GRRLVHIAHG SIESKADRPQ AERLFSIYTA
FRQILETYKP GESAMETLYF GRNVSSALPV AEARGVLSLA LVEQGLVVVE FSPNAIKKAV
TGVARADKSQ IQEMVRLILG LDGIPKPDHA ADALAMAICS ANTLLL
//
