(data stored in SCRATCH zone)

SWISSPROT: Q145H8_PARXL

ID   Q145H8_PARXL            Unreviewed;       768 AA.
AC   Q145H8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|RuleBase:RU363016};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363016};
GN   Name=recG {ECO:0000256|RuleBase:RU363016};
GN   ORFNames=Bxe_A3988 {ECO:0000313|EMBL:ABE29011.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29011.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29011.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29011.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Critical role in recombination and DNA repair. Helps
CC       process Holliday junction intermediates to mature products by
CC       catalyzing branch migration. Has a DNA unwinding activity
CC       characteristic of a DNA helicase with a 3'- to 5'- polarity.
CC       Unwinds branched duplex DNA (Y-DNA).
CC       {ECO:0000256|RuleBase:RU363016}.
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|RuleBase:RU363016};
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000256|RuleBase:RU363016}.
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DR   EMBL; CP000270; ABE29011.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A3988; -.
DR   EnsemblBacteria; ABE29011; ABE29011; Bxe_A3988.
DR   KEGG; bxe:Bxe_A3988; -.
DR   eggNOG; ENOG4105CB5; Bacteria.
DR   eggNOG; COG1200; LUCA.
DR   HOGENOM; HOG000036617; -.
DR   KO; K03655; -.
DR   OMA; RETNDGF; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR004609; ATP-dep_DNA_helicase_RecG.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033454; RecG_wedge.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF17191; RecG_wedge; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00643; recG; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145H8.
DR   SWISS-2DPAGE; Q145H8.
KW   ATP-binding {ECO:0000256|RuleBase:RU363016};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   DNA damage {ECO:0000256|RuleBase:RU363016};
KW   DNA recombination {ECO:0000256|RuleBase:RU363016};
KW   DNA repair {ECO:0000256|RuleBase:RU363016};
KW   Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:ABE29011.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU363016,
KW   ECO:0000313|EMBL:ABE29011.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN      354    524       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      557    703       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
SQ   SEQUENCE   768 AA;  83628 MW;  CAD14DE1501E8ACC CRC64;
     MDREKAAREG EKSGIHPADK PADKPADEPT DKPTDKPTDK PDNIFGDKPA GRSAAKAAAK
     AAAKSATKPA AKSTDKPAAK PAEKTADKLA KLGLTRDIDL VLHLPMRYED ETSLTPIGHL
     LPGGIAQTEG VVFDNEIAYR PRRQLLVKLR DDAGDELVLR FLNFYGSQVK QMAIGARLRV
     RGDVRGGFFG MEMVHPAVRV VDEDTPLPQA LTPVYPSTAG VTQAYLRKSI DNALSRTSLP
     ELLPEPVART WLEPLGVPSL MDAVRTLHHP GVQSDETALI DGTHPAWVRI KFEELLAQQM
     SLKRAHEERR TRAAPAMPRR KLGDESALVA RLLKALPFSL TAAQERVGGE IALDLTQPHP
     MQRLLQGDVG SGKTIVAALA AAQAIDAGYQ AALMAPTEIL AEQHARKLRG WLEPLGVSVA
     WLAGSLKTRE KRAAIEAAAL GTAQLVIGTH AIIQDAVEFA RLGLVIVDEQ HRFGVAQRLA
     LRAKAQNAAD GARDFQPHQL MMSATPIPRT LAMTYYADLD VSTIDELPPG RTPILTKLVS
     DARREEVIGR VREAALTGRQ VYWVCPLIEE SETLQLQTAV ETYETLVAAL PELKVGLVHG
     RLAPAEKAAV MDAFTRNEVQ LLVATTVIEV GVDVPNASLM VIEHAERFGL AQLHQLRGRV
     GRGSAASVCV LLYTGPLSMT ARARLQTMRE TTDGFEIARR DLEIRGPGEF LGARQSGAAM
     LRFADLENDQ WLIEPAREAA AALLEKYPEV VMQHLARWLG AREQYLKA
//

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