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Database: UniProt
Entry: M1UZ95_9CORY
LinkDB: M1UZ95_9CORY
Original site: M1UZ95_9CORY 
ID   M1UZ95_9CORY            Unreviewed;       206 AA.
AC   M1UZ95;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
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:AGG67013.1};
GN   ORFNames=H924_07855 {ECO:0000313|EMBL:AGG67013.1};
OS   Corynebacterium callunae DSM 20147.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG67013.1, ECO:0000313|Proteomes:UP000011760};
RN   [1] {ECO:0000313|EMBL:AGG67013.1, ECO:0000313|Proteomes:UP000011760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG67013.1,
RC   ECO:0000313|Proteomes:UP000011760};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL   Submitted (FEB-2013) 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; CP004354; AGG67013.1; -; Genomic_DNA.
DR   RefSeq; WP_015651444.1; NZ_ATVF01000003.1.
DR   AlphaFoldDB; M1UZ95; -.
DR   STRING; 1121353.H924_07855; -.
DR   KEGG; ccn:H924_07855; -.
DR   PATRIC; fig|1121353.3.peg.1601; -.
DR   eggNOG; COG0632; Bacteria.
DR   HOGENOM; CLU_087936_2_1_11; -.
DR   OrthoDB; 5293449at2; -.
DR   Proteomes; UP000011760; 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; 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   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:AGG67013.1};
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:AGG67013.1};
KW   Hydrolase {ECO:0000313|EMBL:AGG67013.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:AGG67013.1}.
FT   DOMAIN          1..61
FT                   /note="DNA helicase Holliday junction RuvA type"
FT                   /evidence="ECO:0000259|Pfam:PF01330"
FT   DOMAIN          158..204
FT                   /note="Holliday junction DNA helicase RuvA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07499"
FT   REGION          154..206
FT                   /note="Domain III"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   206 AA;  21627 MW;  574C72D3F2066396 CRC64;
     MIASLRGTVI NIGLSSAVIE CQGVGYEVTT TPNTLSRLIR GEEALILTTM VVREDAMKLY
     GFIDNESREM FAVLQTVSGL GPRLALACES VLSPLEIAQA IGNGDSKTLQ RVPGVGKRMA
     DRLIVELKDK VAAFSAGVVD PNQPQLSLGD TPVASVVVVE QVTQALIGLG FSEKQSEEAV
     TFVLSVDPGL DTSGALRAAL AKLSGK
//
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