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Entry: A0A1M5W4X7_9BACT
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ID   A0A1M5W4X7_9BACT        Unreviewed;       202 AA.
AC   A0A1M5W4X7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05720761_12918 {ECO:0000313|EMBL:SHH82536.1};
OS   Fibrobacter sp. UWCM.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896208 {ECO:0000313|EMBL:SHH82536.1, ECO:0000313|Proteomes:UP000184289};
RN   [1] {ECO:0000313|EMBL:SHH82536.1, ECO:0000313|Proteomes:UP000184289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWCM {ECO:0000313|EMBL:SHH82536.1,
RC   ECO:0000313|Proteomes:UP000184289};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQWR01000029; SHH82536.1; -; Genomic_DNA.
DR   RefSeq; WP_073116259.1; NZ_FQWR01000029.1.
DR   AlphaFoldDB; A0A1M5W4X7; -.
DR   Proteomes; UP000184289; Unassembled WGS sequence.
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; 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   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   ATP-binding {ECO:0000313|EMBL:SHH82536.1};
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:SHH82536.1};
KW   Hydrolase {ECO:0000313|EMBL:SHH82536.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:SHH82536.1}.
FT   DOMAIN          73..92
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          108..127
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   REGION          1..64
FT                   /note="Domain I"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
FT   REGION          148..202
FT                   /note="Domain III"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00031"
SQ   SEQUENCE   202 AA;  21080 MW;  E06A4F186C2A4E77 CRC64;
     MIERIRGILA EKSPTFVVVD VNGVGYGVNI SAYTAGKLPE EGSEVTLYTN LVVREDSMTL
     FGFADKTEKN IFLMLLDVNG VGPKMAQRIL SGVTPADLLN MIASDNKAAL SKIKGLGKKT
     CEQMTLSLKE KAGALLQALG DVEGSGITGM GALTGAKMEA VLALHTLGVK DPAAEKAVVK
     AAEILGDSAD AAALIPEALK YL
//
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