ID   RECG_AQUAE              Reviewed;         792 AA.
AC   O67837;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=aq_2053;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Critical role in recombination and DNA repair. Helps process
CC       Holliday junction intermediates to mature products by catalyzing branch
CC       migration. Has a DNA unwinding activity characteristic of a DNA
CC       helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-
CC       DNA) (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07804.1; -; Genomic_DNA.
DR   PIR; A70476; A70476.
DR   RefSeq; NP_214406.1; NC_000918.1.
DR   RefSeq; WP_010881342.1; NC_000918.1.
DR   AlphaFoldDB; O67837; -.
DR   SMR; O67837; -.
DR   STRING; 224324.aq_2053; -.
DR   EnsemblBacteria; AAC07804; AAC07804; aq_2053.
DR   KEGG; aae:aq_2053; -.
DR   PATRIC; fig|224324.8.peg.1583; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_0; -.
DR   InParanoid; O67837; -.
DR   OMA; DNGFQAC; -.
DR   OrthoDB; 234717at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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; IPR045562; RecG_dom3_C.
DR   InterPro; IPR033454; RecG_wedge.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF19833; RecG_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;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..792
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102137"
FT   DOMAIN          375..538
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          557..719
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           489..492
FT                   /note="DEQH box"
FT   BINDING         388..395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   792 AA;  91180 MW;  EFE1DC8BBAF38045 CRC64;
     MDTAFVKDFI DNLLENDGLK LKRAIGVGIF LFNKLKEDAP DYILESLKEV DKLPFEKKKA
     VLREVRKFLS EYEKRKKEGN FLEKTKRKPI DVFFNPIEKV KILTKTQIST LKALGIETVY
     DALFYFPEKY EDKRLNTSIK TAKVGEKVAL KVKVKEVKIK ENERYTLEVV CTDGTGYITL
     KYRYKNPHFA LKAFRKGMEI VVYGKLKSFK GEKYMVHPEV KSPSSEELGK IIPVYYVRKR
     GELQEISSKT KQKRVRTALT ALSESLYRYF PEYMPDYLIE KYNFPDIALC IKELHNPKDI
     SVNALNSFTD LYHKRVIYDE LFLFQLALLL KKQEIKKEKA PKVNVDEKFL RKAIEKLPFK
     LTRAQERAIK EILEDLSRDV PMNRLLQGDV GSGKTIVAIL TSLAVVKSGY QVAVMVPTEI
     LAHQHYKKFS EMLKDYGVNV ALLTGSLTPS QKKSVYKHVK EGNIHVLVGT HALIQDKVEF
     KNLGYVIIDE QHRFGVMQRK LLLEKGKGLY PHCLVMSATP IPRTLALSIY GDLDISIIDE
     LPPGRKEVIT KLYFESQKEE VYKKVEEELK KGNKVYVIYP LIEESEKLNL KAATEEYERW
     KKLFPDRKVL LLHGKMPDKE KLAVMEEFKR EGDILVSTTV IEVGIDVPEA TVMVIEDAHR
     FGLSQLHQLR GRVGRSDKEA YCLLVVPDEI KNEKNESLKR LRVFVKTTDG FKIAEEDLKL
     RGPGEIIGVS QSGYFGFRVA NLARSQDRAL LGVARKDAEE LLKNNPNLEN LQDLKKLLIK
     KYGDKMELSF VA