ID M1YKF7_NITG3 Unreviewed; 169 AA.
AC M1YKF7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:CCQ90973.1};
GN ORFNames=NITGR_520015 {ECO:0000313|EMBL:CCQ90973.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ90973.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ90973.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ90973.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ90973.1}.
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DR EMBL; CAQJ01000058; CCQ90973.1; -; Genomic_DNA.
DR RefSeq; WP_005009191.1; NZ_HG422173.1.
DR AlphaFoldDB; M1YKF7; -.
DR STRING; 1266370.NITGR_520015; -.
DR HOGENOM; CLU_091257_3_1_0; -.
DR InParanoid; M1YKF7; -.
DR OrthoDB; 9805499at2; -.
DR Proteomes; UP000011704; Unassembled WGS sequence.
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 {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:CCQ90973.1};
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:UP000011704}.
FT ACT_SITE 7
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT ACT_SITE 67
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
SQ SEQUENCE 169 AA; 18532 MW; D34B0AFE28F02DB7 CRC64;
MRVLGIDPGS NCTGYGIVES GRNTLKSIHW GSIKSKSRTP FPDRLKTIYD DLTRVIGEYK
PEIVAIEDLF FAVNAQSTIK LGQTRGVALL AAVNASLTVA EYTPLEVKLS IVGYGRADKN
QVRDMVTTLL RLKEKPEPLD ASDALAVAIC HLHNHGTSNR LKEALSSRR
//
