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Database: UniProt
Entry: A0A0P0C7G2_9BACT
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ID   A0A0P0C7G2_9BACT        Unreviewed;       196 AA.
AC   A0A0P0C7G2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=DC20_10545 {ECO:0000313|EMBL:ALI99331.1};
OS   Rufibacter tibetensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI99331.1, ECO:0000313|Proteomes:UP000061382};
RN   [1] {ECO:0000313|EMBL:ALI99331.1, ECO:0000313|Proteomes:UP000061382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1351 {ECO:0000313|EMBL:ALI99331.1,
RC   ECO:0000313|Proteomes:UP000061382};
RA   Dai J.;
RT   "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT   radiation-resistant bacterium from tibet plateau.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP012643; ALI99331.1; -; Genomic_DNA.
DR   RefSeq; WP_062543795.1; NZ_CP012643.1.
DR   AlphaFoldDB; A0A0P0C7G2; -.
DR   STRING; 512763.DC20_10545; -.
DR   KEGG; rti:DC20_10545; -.
DR   PATRIC; fig|512763.3.peg.2320; -.
DR   OrthoDB; 5293449at2; -.
DR   Proteomes; UP000061382; Chromosome.
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:ALI99331.1};
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:ALI99331.1};
KW   Hydrolase {ECO:0000313|EMBL:ALI99331.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ALI99331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061382}.
FT   DOMAIN          72..91
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          107..126
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   REGION          146..196
FT                   /note="Domain III"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   196 AA;  21440 MW;  E8C803BFD6CB8F4B CRC64;
     MIAYLDGRLA QKDPTFVIID VGGVGYELRI SLNTFGQLPE GERCRLYTHQ HIKEDAHTLY
     GFATLAEKSA FLHLISISGV GPNTGLMILS SLTVQEVQQA IVREDVRTIQ QVKGIGAKTA
     QRIILELRDK FRKGLGPDAV NVSFGAHNTS RDEALSALVT LGFAKNVAEK TLDTIIKREG
     ASLTVEEMIK FALKSS
//
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