ID A0A1D9DZ03_9MICO Unreviewed; 189 AA.
AC A0A1D9DZ03;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=A4Z71_03425 {ECO:0000313|EMBL:AOY56035.1};
OS Candidatus Rhodoluna planktonica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=535712 {ECO:0000313|EMBL:AOY56035.1, ECO:0000313|Proteomes:UP000243784};
RN [1] {ECO:0000313|EMBL:AOY56035.1, ECO:0000313|Proteomes:UP000243784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Dar1 {ECO:0000313|EMBL:AOY56035.1,
RC ECO:0000313|Proteomes:UP000243784};
RX PubMed=27659506; DOI=10.1016/j.bbabio.2016.09.006;
RA Nakamura S., Kikukawa T., Tamogami J., Kamiya M., Aizawa T., Hahn M.W.,
RA Ihara K., Kamo N., Demura M.;
RT "Photochemical characterization of actinorhodopsin and its functional
RT existence in the natural host.";
RL Biochim. Biophys. Acta 1857:1900-1908(2016).
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; CP015208; AOY56035.1; -; Genomic_DNA.
DR RefSeq; WP_070954545.1; NZ_CP015208.1.
DR AlphaFoldDB; A0A1D9DZ03; -.
DR STRING; 535712.A4Z71_03425; -.
DR KEGG; rpla:A4Z71_03425; -.
DR OrthoDB; 5293449at2; -.
DR Proteomes; UP000243784; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 NCBIfam; TIGR00084; ruvA; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF01330; RuvA_N; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000243784}.
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 145..189
FT /note="Domain III"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ SEQUENCE 189 AA; 19818 MW; 3FB81BA662D59A26 CRC64;
MIASVSGSVQ SIGKSAVVVR AGNFGVSVLA TATTLRSLRI GQEVELLTSL QVREDSLTLY
GFSDDGQLST FELLLTVSGI GPKVALSIID SLTPAQIANA IQQDDDSVFR SVSGVGPKTA
KLIILALSGK VTQVSSSKEP SNQENDLVEA IANLGWPSAK IRDAISQGDI SKLTPAEAIR
EILRRLAAK
//
