ID   RECG_PASMU              Reviewed;         693 AA.
AC   Q9CMB4;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, 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=PM0919;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03003.1; -; Genomic_DNA.
DR   RefSeq; WP_010906918.1; NC_002663.1.
DR   AlphaFoldDB; Q9CMB4; -.
DR   SMR; Q9CMB4; -.
DR   STRING; 747.DR93_1064; -.
DR   EnsemblBacteria; AAK03003; AAK03003; PM0919.
DR   KEGG; pmu:PM0919; -.
DR   PATRIC; fig|272843.6.peg.929; -.
DR   HOGENOM; CLU_005122_7_1_6; -.
DR   OMA; DNGFQAC; -.
DR   Proteomes; UP000000809; 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; 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; 3.40.50.300; -; 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..693
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102148"
FT   DOMAIN          283..448
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          482..628
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           397..400
FT                   /note="DEQH box"
FT   BINDING         296..303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   693 AA;  78025 MW;  5AB96E4B5BA54DB3 CRC64;
     MTIQFLDAVP LTTLSGVGAA ISDKLGRIGI HNLQDLLFHL PIRYEDRTRI TPIHDLRPDA
     YATIEGLVQT CEVQFGKRPI LNVSLSDGTS KIMLRFFNFN AGMKNSLQPG ARVKAFGEVK
     RGRFMAEIHH PEYQIIRDNA PLILEETLTP IYSTTEGIKQ NSLRKLTDQA LAVLENIQIA
     EILPNEFNPH PFSLKEAIRF LHRPPPDVSL EALEKGTHPA QQRLIFEELL AHNLAMQKVR
     IGTQQFSAYP LSYQTDLKQR FLAQLPFTPT DAQVRVTQEI EQDLTHPFPM MRLVQGDVGS
     GKTLVAALAA LLAIDNGKQV ALMAPTEILA EQHATNFRRW FESLGIEVGW LAGKVKGKAR
     QTELEKIRTG QVQMVVGTHA LFQDEVEFSD LALVIVDEQH RFGVHQRLML REKGKQADHY
     PHQLIMTATP IPRTLAMTVY ADLDTSIIDE LPPGRTPITT VAISEERRAE VIARVNHACV
     NEKRQAYWVC TLIDESEVLE AQAAEAIAED LRKILPHLRI GLVHGRMKPA EKQDIMQAFK
     QAEIDLLVAT TVIEVGVDVP NASLMIIENA ERLGLSQLHQ LRGRVGRGTT ASFCVLMYKP
     PLGKISQKRL QVLRDTQDGF VISEKDLEIR GPGEVLGTKQ TGVAEFKVAN LMRDRKMIPT
     VQYYARRLIV EQPEVATKLI QRWINQREIY THV