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Database: UniProt
Entry: RUVA_FRATT
LinkDB: RUVA_FRATT
Original site: RUVA_FRATT 
ID   RUVA_FRATT              Reviewed;         216 AA.
AC   Q5NH17;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Holliday junction branch migration complex subunit RuvA {ECO:0000255|HAMAP-Rule:MF_00031};
GN   Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; OrderedLocusNames=FTT_0658;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_00031}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00031}.
CC   -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00031}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG45291.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ749949; CAG45291.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003020417.1; NZ_CP010290.1.
DR   RefSeq; YP_169675.1; NC_006570.2.
DR   AlphaFoldDB; Q5NH17; -.
DR   SMR; Q5NH17; -.
DR   STRING; 177416.FTT_0658; -.
DR   DNASU; 3191358; -.
DR   EnsemblBacteria; CAG45291; CAG45291; FTT_0658.
DR   KEGG; ftu:FTT_0658; -.
DR   eggNOG; COG0632; Bacteria.
DR   OrthoDB; 5293449at2; -.
DR   Proteomes; UP000001174; 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   Cytoplasm; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..216
FT                   /note="Holliday junction branch migration complex subunit
FT                   RuvA"
FT                   /id="PRO_0000224869"
FT   REGION          1..64
FT                   /note="Domain I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00031"
FT   REGION          65..143
FT                   /note="Domain II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00031"
FT   REGION          144..163
FT                   /note="Flexible linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00031"
FT   REGION          164..216
FT                   /note="Domain III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   216 AA;  23577 MW;  43108364BF923DF5 CRC64;
     MISFIKGVLI EKDPTALLID VNGIGYEVFV PMTTFYTLGD IDSQVSLYTH FVVREDAQQL
     YGFKSKVDKK VFQELIKVNG IGARTAIAIL SGMDSKTLLH CIENKDYALL ATVPGIGKKT
     AERLVVEIYD KLLKMANEIY AQTSGTTTTS QDSQAQQAPT SVVLANSIFN ESVDALLALG
     YKQKDAEKMA RSAMGDATTV AEVIRKALQG SIKSKR
//
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