RUVB1_SYNJA
ID RUVB1_SYNJA Reviewed; 378 AA.
AC Q2JTM7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB 1 {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN Name=ruvB1 {ECO:0000255|HAMAP-Rule:MF_00016}; Synonyms=ruvB-1;
GN OrderedLocusNames=CYA_1812;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC cruciform structure in supercoiled DNA with palindromic sequence,
CC indicating that it may promote strand exchange reactions in homologous
CC recombination. RuvAB is a helicase that mediates the Holliday junction
CC migration by localized denaturation and reannealing.
CC {ECO:0000255|HAMAP-Rule:MF_00016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00016};
CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; CP000239; ABC99965.1; -; Genomic_DNA.
DR RefSeq; WP_011430641.1; NC_007775.1.
DR AlphaFoldDB; Q2JTM7; -.
DR SMR; Q2JTM7; -.
DR STRING; 321327.CYA_1812; -.
DR EnsemblBacteria; ABC99965; ABC99965; CYA_1812.
DR KEGG; cya:CYA_1812; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_3; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 874197at2; -.
DR Proteomes; UP000008818; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041445; AAA_lid_4.
DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008824; RuvB-like_N.
DR InterPro; IPR008823; RuvB_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR42848; PTHR42848; 1.
DR Pfam; PF17864; AAA_lid_4; 1.
DR Pfam; PF05491; RuvB_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00635; ruvB; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; SOS response.
FT CHAIN 1..378
FT /note="Holliday junction ATP-dependent DNA helicase RuvB 1"
FT /id="PRO_0000235419"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ SEQUENCE 378 AA; 41945 MW; 839DC154B8FC83F2 CRC64;
MAIISSRDTG QNAEGPKRRQ QKSSAWRKEG RELSFAGERG ADPSALLQPQ AHPGEAQEES
LRPRTLAEYI GQTELKEVLS IAIAAARARQ EPLDHLLFYG PPGLGKTTVA AVLAAEMGSQ
FYMTTAPALE SPRDIAGYLV RLKRGDVLFI DEIHRLPKVT EELLYPAMED FRLDITIGKG
RSARITSLPL ERFTLIGATT RIGALTSPLR DRFGHVQRLR FYEPHELVQI VLRTARLLNV
STDPEGAAEI ARRSRGTPRI ANRLFKRVRD YAQVRGDGHI SQEVAAAALE LFQVDPMGLD
WIDRKLLTVL VEQFGGGPVG LETMAAVTGE DPQTIEEVYE PYLLQIGYLQ RTPRGRVVTP
AALRHLGYEA QSPLPLWS
