(data stored in ACNUC7421 zone)

SWISSPROT: D4YX51_SPHJU

ID   D4YX51_SPHJU            Unreviewed;       202 AA.
AC   D4YX51;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000256|HAMAP-Rule:MF_00031, ECO:0000256|SAAS:SAAS01087591};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_00031, ECO:0000256|SAAS:SAAS01087580};
GN   Name=ruvA {ECO:0000256|HAMAP-Rule:MF_00031,
GN   ECO:0000313|EMBL:BAI94933.1};
GN   OrderedLocusNames=SJA_C1-00990 {ECO:0000313|EMBL:BAI94933.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94933.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94933.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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
CC       homologous recombination. RuvAB is a helicase that mediates the
CC       Holliday junction migration by localized denaturation and
CC       reannealing. RuvA stimulates, in the presence of DNA, the weak
CC       ATPase activity of RuvB. {ECO:0000256|HAMAP-Rule:MF_00031,
CC       ECO:0000256|SAAS:SAAS01087604}.
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:0000256|HAMAP-Rule:MF_00031,
CC         ECO:0000256|SAAS:SAAS01122358};
CC   -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000256|HAMAP-
CC       Rule:MF_00031, ECO:0000256|SAAS:SAAS00881025}.
CC   -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00031, ECO:0000256|SAAS:SAAS01087593}.
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DR   EMBL; AP010803; BAI94933.1; -; Genomic_DNA.
DR   RefSeq; WP_013038759.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-00990; -.
DR   EnsemblBacteria; BAI94933; BAI94933; SJA_C1-00990.
DR   GeneID; 29271811; -.
DR   KEGG; sjp:SJA_C1-00990; -.
DR   eggNOG; ENOG4105KA4; Bacteria.
DR   eggNOG; COG0632; LUCA.
DR   HOGENOM; HOG000057115; -.
DR   KO; K03550; -.
DR   OMA; DCHGVGY; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   HAMAP; MF_00031; DNA_helic_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   PANTHER; PTHR33796; PTHR33796; 1.
DR   Pfam; PF07499; RuvA_C; 1.
DR   Pfam; PF01330; RuvA_N; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF46929; SSF46929; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YX51.
DR   SWISS-2DPAGE; D4YX51.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087601};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS00881019};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087577};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS00881020};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087589, ECO:0000313|EMBL:BAI94933.1};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087596};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087608};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS01087598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00031,
KW   ECO:0000256|SAAS:SAAS00880989}.
FT   DOMAIN       73     92       HhH1. {ECO:0000259|SMART:SM00278}.
FT   DOMAIN      108    127       HhH1. {ECO:0000259|SMART:SM00278}.
SQ   SEQUENCE   202 AA;  20516 MW;  49AA74DB706095D0 CRC64;
     MIAKLKGRLD STGLDHAIID VGGVGYLVGA SSRTLAALGP VGEAVTVHTE MLVSDDAIRL
     VGFARAEERD WFRLLTGVQG VGSRVALAIL SALEPVELHR AVAAGDKAMI ARANGVGPKL
     AQRIANELKD KIGAAPMPAG AVGAGFAALP TGGHSADAIS ALQNLGFKPA EASIAVAAAE
     EELGEDASLD ALVRLALRKA AK
//

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