ID A0A0W1AM55_9GAMM Unreviewed; 200 AA.
AC A0A0W1AM55;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ECO:0000313|EMBL:KTD82390.1};
GN ORFNames=Lwal_0867 {ECO:0000313|EMBL:KTD82390.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD82390.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD82390.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD82390.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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, 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:KTD82390.1}.
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DR EMBL; LNZB01000015; KTD82390.1; -; Genomic_DNA.
DR RefSeq; WP_058479682.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1AM55; -.
DR STRING; 66969.Lwal_0867; -.
DR PATRIC; fig|66969.6.peg.942; -.
DR OrthoDB; 5293449at2; -.
DR Proteomes; UP000054729; 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 CDD; cd14332; UBA_RuvA_C; 1.
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 PANTHER; PTHR33796; HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVA; 1.
DR PANTHER; PTHR33796:SF1; HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE 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:KTD82390.1};
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:KTD82390.1};
KW Hydrolase {ECO:0000313|EMBL:KTD82390.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KTD82390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054729}.
FT DOMAIN 74..93
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 109..128
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT REGION 66..143
FT /note="Domain II"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
FT REGION 150..200
FT /note="Domain III"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ SEQUENCE 200 AA; 22102 MW; AD6E676254F056EE CRC64;
MIGWLHGQVV DKHQPGKLVI DVHGVGYDVE TSLNTFFQID SHEKALGLHI HTVVREDALL
LYGFIDKLER SLFRALIKVN GIGPKLAMTI LSSISPNEFI QCIHQENAAL LTKLPGIGKK
TAERLVVEMR DSIKQLGEPS SEVVSKSGTI SVRNQDEAVS ALEALGYKHQ EAFKVVNKID
DGLKTCEQLI REALQILAAR
//
