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Entry: A0A512JM54_9HYPH
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Original site: A0A512JM54_9HYPH 
ID   A0A512JM54_9HYPH        Unreviewed;       205 AA.
AC   A0A512JM54;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   18-JUN-2025, entry version 21.
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:GEP11041.1};
GN   ORFNames=MGN01_28860 {ECO:0000313|EMBL:GEP11041.1};
OS   Methylobacterium gnaphalii.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=1010610 {ECO:0000313|EMBL:GEP11041.1, ECO:0000313|Proteomes:UP000321750};
RN   [1] {ECO:0000313|EMBL:GEP11041.1, ECO:0000313|Proteomes:UP000321750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107716 {ECO:0000313|EMBL:GEP11041.1,
RC   ECO:0000313|Proteomes:UP000321750};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Methylobacterium gnaphalii NBRC 107716.";
RL   Submitted (JUL-2019) 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:GEP11041.1}.
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DR   EMBL; BJZV01000015; GEP11041.1; -; Genomic_DNA.
DR   RefSeq; WP_147047409.1; NZ_BJZV01000015.1.
DR   AlphaFoldDB; A0A512JM54; -.
DR   OrthoDB; 5293449at2; -.
DR   Proteomes; UP000321750; 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; 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   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:GEP11041.1};
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:GEP11041.1};
KW   Hydrolase {ECO:0000313|EMBL:GEP11041.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:GEP11041.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321750}.
FT   DOMAIN          1..62
FT                   /note="DNA helicase Holliday junction RuvA type"
FT                   /evidence="ECO:0000259|Pfam:PF01330"
FT   DOMAIN          157..203
FT                   /note="Holliday junction DNA helicase RuvA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07499"
FT   REGION          1..64
FT                   /note="Domain I"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
FT   REGION          159..205
FT                   /note="Domain III"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   205 AA;  21351 MW;  62C3BC6CB32D1B9F CRC64;
     MIGKLKGIVD SYGEDFVILD VQGVGYVVHC SARTLQRLPK PGEAAELAID THVREDMIRL
     YGFRSDAERE WFRLLQTVQG VGSKVALAVL SVLEPGALAT ALATGDKGAI ARAPGVGPRL
     AARLAAELKD KAPAFSPADP ALIALTGAVE DRTAPPPVAD AISALVNLGY PQVQASAAIA
     TVLKGAPEGA EAKVLIRLGL RELAK
//
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