ID   RECG_ACIFR              Reviewed;         652 AA.
AC   O50224;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG;
OS   Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9603897; DOI=10.1128/jb.180.11.3007-3012.1998;
RA   Oppon J.C., Sarnovsky R.J., Craig N.L., Rawlings D.E.;
RT   "A Tn7-like transposon is present in the glmUS region of the obligately
RT   chemoautolithotrophic bacterium Thiobacillus ferrooxidans.";
RL   J. Bacteriol. 180:3007-3012(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF032884; AAC21662.1; -; Genomic_DNA.
DR   PIR; T45499; T45499.
DR   AlphaFoldDB; O50224; -.
DR   SMR; O50224; -.
DR   STRING; 380394.Lferr_2795; -.
DR   PRIDE; O50224; -.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.565.60; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025831; RecG_C.
DR   InterPro; IPR038475; RecG_C_sf.
DR   InterPro; IPR033454; RecG_wedge.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13749; HATPase_c_4; 1.
DR   Pfam; PF17191; RecG_wedge; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..652
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102160"
FT   DOMAIN          300..461
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           414..417
FT                   /note="DEQH box"
FT   BINDING         313..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   652 AA;  73043 MW;  5C48328A517253E9 CRC64;
     MSTSTNFSQS GHVARPCRAR NSMAGAKAGL YLQSSVSALR GVGPALVPRL QHMDLWRVQD
     VLFHLPSRYQ DRRHIASMAT LQAGQECAIL GEIVRVDHQR GGREQWLVTV SDGSGRLQIR
     LFHMTVALRA QWQVGRRLWC FGELRGGFHG LEMIHPEWQM ADVPQFQAPR HLTPFYPSSE
     GITQAQWRRW MAQALTLLDQ LPDYLENRLP PQWPGLREGL RLLHESADEI PSPQHPAWQR
     LALEELLANH LAVRRMRQSG MMQNAPCLRS KGQLWHRFLA HLPFSPTMAQ ERVIAEINAD
     LVRHRPMRRL LQGDVGSGKT LVAAAATLTA LEAGYQVAMM APTEILAEQL HARFQQWLEP
     LGLEVGYLVG SRSPRARRET AETLAGGSLR LVIGTQSLFQ EGVVFACLGL VIIDEQHRFG
     VEQRRQLLEK GAMPHLLVMT ATPIMVEDGI TVSGILLFGR TPNRFLPQAG IDAVAFPGVD
     KDYAARERAA LRGPMTPLLN DAGDIVEAGL VEQAIAFVQR NTAIGGQLEE GGARRENLPA
     YPREAIREAI VNALIHRDYL LSSTDIELSI YEDRLEITSP GRLPNGITPA RMLTGCRATR
     NQLIKDVMRD YRYLEHSGMG VPRKIVKCMR EHNGTEPQLI EDGELFTVRL LR