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Database: UniProt
Entry: A0A0Q6Q8W9_9MICO
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ID   A0A0Q6Q8W9_9MICO        Unreviewed;       202 AA.
AC   A0A0Q6Q8W9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   ORFNames=ASC63_12780 {ECO:0000313|EMBL:KQV08024.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV08024.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV08024.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08024.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV08024.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08024.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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: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:KQV08024.1}.
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DR   EMBL; LMCU01000001; KQV08024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6Q8W9; -.
DR   STRING; 1736426.ASC63_12780; -.
DR   OrthoDB; 9805499at2; -.
DR   Proteomes; UP000051914; 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|ARBA:ARBA00022490, 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00034};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00034};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00034};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT   REGION          162..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        9
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00034"
SQ   SEQUENCE   202 AA;  21277 MW;  5CB656A7B8D7CBFA CRC64;
     MSVRVFGIDP GLTRCGVGIV DVAANRTAKL VHVSVIRTAP ELPLEQRLLA IGTGIEELLD
     EYEPAAFAIE RVFAQHNLRT VMGTAQISGV AMHAAAKRRL AVGLHTPSEV KAAITGYGAA
     EKKQVQVMVA RILGLADLPK PADAADALAI AICHAWRTPV GPEGSGGEAT DAPSSRLTPA
     QQAWHAAERS TRASVAPRRL TK
//
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