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Database: UniProt
Entry: A0A3F3H284_9LACO
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ID   A0A3F3H284_9LACO        Unreviewed;       203 AA.
AC   A0A3F3H284;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   18-JUN-2025, entry version 23.
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:GAP02300.1};
GN   ORFNames=FPFC_011800 {ECO:0000313|EMBL:GAP02300.1};
OS   Fructobacillus pseudoficulneus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructobacillus.
OX   NCBI_TaxID=220714 {ECO:0000313|EMBL:GAP02300.1, ECO:0000313|Proteomes:UP000061227};
RN   [1] {ECO:0000313|EMBL:GAP02300.1, ECO:0000313|Proteomes:UP000061227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15468 {ECO:0000313|EMBL:GAP02300.1,
RC   ECO:0000313|Proteomes:UP000061227};
RX   PubMed=26715526; DOI=10.1186/s12864-015-2339-x;
RA   Endo A., Tanizawa Y., Tanaka N., Maeno S., Kumar H., Shiwa Y., Okada S.,
RA   Yoshikawa H., Dicks L., Nakagawa J., Arita M.;
RT   "Comparative genomics of Fructobacillus spp. and Leuconostoc spp. reveals
RT   niche-specific evolution of Fructobacillus spp.";
RL   BMC Genomics 16:1117-1117(2015).
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; DF968063; GAP02300.1; -; Genomic_DNA.
DR   RefSeq; WP_059375751.1; NZ_DF968063.1.
DR   AlphaFoldDB; A0A3F3H284; -.
DR   STRING; 220714.SAMN05660469_0254; -.
DR   OrthoDB; 5293449at2; -.
DR   Proteomes; UP000061227; 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:GAP02300.1};
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:GAP02300.1};
KW   Hydrolase {ECO:0000313|EMBL:GAP02300.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:GAP02300.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061227}.
FT   DOMAIN          71..90
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          106..125
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   REGION          154..203
FT                   /note="Domain III"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   203 AA;  21508 MW;  B7CAF1525FB4A885 CRC64;
     MFEYLKGLIT DVRPGYIVLE SKDGVGYKIF PANPYHFVVD QSATVYVEQI VRETEQALYG
     FATLTEKGLF NKLLNVSGIG PKSALAILAG ADPASLVAAI DQDEVTYLTQ FPGVGKKTAQ
     QIILDLKGKM GDFANLAEGA EAQLAGEKKT LTAADNQNLA DALAALEALG YAQKDITKVK
     KALAGVNAAT EDLISQALAL LVS
//
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