ID A0A1F4QFC9_9BACT Unreviewed; 204 AA.
AC A0A1F4QFC9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Holliday junction branch migration complex subunit RuvA {ECO:0000256|HAMAP-Rule:MF_00031};
GN Name=ruvA {ECO:0000256|HAMAP-Rule:MF_00031};
GN ORFNames=A3H39_19140 {ECO:0000313|EMBL:OGB94480.1};
OS candidate division NC10 bacterium RIFCSPLOWO2_02_FULL_66_22.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1801658 {ECO:0000313|EMBL:OGB94480.1, ECO:0000313|Proteomes:UP000177374};
RN [1] {ECO:0000313|EMBL:OGB94480.1, ECO:0000313|Proteomes:UP000177374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ)
CC DNA during genetic recombination and DNA repair, while the RuvA-RuvB
CC complex plays an important role in the rescue of blocked DNA
CC replication forks via replication fork reversal (RFR). RuvA
CC specifically binds to HJ cruciform DNA, conferring on it an open
CC structure. The RuvB hexamer acts as an ATP-dependent pump, pulling
CC dsDNA into and through the RuvAB complex. HJ branch migration allows
CC RuvC to scan DNA until it finds its consensus sequence, where it
CC cleaves and resolves the cruciform DNA. {ECO:0000256|HAMAP-
CC Rule:MF_00031}.
CC -!- SUBUNIT: Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ)
CC complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters
CC through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA
CC strand where it exits the tetramer. Each RuvB hexamer is contacted by
CC two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this
CC complex drives branch migration. In the full resolvosome a probable
CC DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
CC {ECO:0000256|HAMAP-Rule:MF_00031}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00031}.
CC -!- DOMAIN: Has three domains with a flexible linker between the domains II
CC and III and assumes an 'L' shape. Domain III is highly mobile and
CC contacts RuvB. {ECO:0000256|HAMAP-Rule:MF_00031}.
CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000256|HAMAP-
CC Rule:MF_00031}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00031}.
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:OGB94480.1}.
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DR EMBL; METH01000040; OGB94480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4QFC9; -.
DR STRING; 1801658.A3H39_19140; -.
DR Proteomes; UP000177374; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00031; DNA_HJ_migration_RuvA; 1.
DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000085; RuvA.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR011114; RuvA_C.
DR InterPro; IPR036267; RuvA_C_sf.
DR NCBIfam; TIGR00084; ruvA; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF07499; RuvA_C; 1.
DR Pfam; PF01330; RuvA_N; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46929; DNA helicase RuvA subunit, C-terminal domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:OGB94480.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00031};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00031};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00031};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00031};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00031}; Helicase {ECO:0000313|EMBL:OGB94480.1};
KW Hydrolase {ECO:0000313|EMBL:OGB94480.1};
KW Nucleotide-binding {ECO:0000313|EMBL:OGB94480.1}.
FT DOMAIN 73..92
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 108..127
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT REGION 1..64
FT /note="Domain I"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
FT REGION 150..204
FT /note="Domain III"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ SEQUENCE 204 AA; 21983 MW; 73A9FE96391691B2 CRC64;
MIAQIRGRLT SKEPHRVVVD VNGVGYQLFI PLSTFYQLPE VSAEVFLHTH THVREDAIQL
FGFHTRDEQA LFELLQGVSG IGPRLATNIL SGISVEELVP ALSEGNVARL RAVPGVGKKL
AERLVVELRE KVGSARLGQP TAAPAGPAPL TDRALEDVVS ALANLGCNRK EAIKAAEAAR
QQLGPTAEFE KLIKAALRAL SESR
//
