ID A0A1I0QL87_9FIRM Unreviewed; 694 AA.
AC A0A1I0QL87;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846, ECO:0000256|RuleBase:RU363016};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU363016};
GN Name=recG {ECO:0000256|RuleBase:RU363016};
GN ORFNames=SAMN05421659_108114 {ECO:0000313|EMBL:SEW27856.1};
OS [Clostridium] fimetarium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=99656 {ECO:0000313|EMBL:SEW27856.1, ECO:0000313|Proteomes:UP000199701};
RN [1] {ECO:0000313|EMBL:SEW27856.1, ECO:0000313|Proteomes:UP000199701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9179 {ECO:0000313|EMBL:SEW27856.1,
RC ECO:0000313|Proteomes:UP000199701};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|ARBA:ARBA00024832, 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|ARBA:ARBA00007504, ECO:0000256|RuleBase:RU363016}.
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DR EMBL; FOJI01000008; SEW27856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QL87; -.
DR STRING; 99656.SAMN05421659_108114; -.
DR Proteomes; UP000199701; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd17992; DEXHc_RecG; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047112; RecG/Mfd.
DR InterPro; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR NCBIfam; TIGR00643; recG; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_dom3_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363016};
KW DNA damage {ECO:0000256|RuleBase:RU363016};
KW DNA recombination {ECO:0000256|RuleBase:RU363016};
KW DNA repair {ECO:0000256|RuleBase:RU363016};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363016};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363016};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363016};
KW Reference proteome {ECO:0000313|Proteomes:UP000199701}.
FT DOMAIN 271..434
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 456..622
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 694 AA; 79162 MW; 9DD3677E3B097ABF CRC64;
MQLKDLKGIG AKTSDLLNKL SIFSVEDLVD FYPRDYDVYE NTIFVNDIND YLDKPAIAID
GIVANTPDMK RISNLMIIST IIKDEKGQGI KATWFNMPYL KTTLRMGYRF VFRGRVIFKN
GAYVMEQPVM YTMSDYAKLL NEMQPIYALT KGLSNKIVTK AVAQALEIFS LQKDYIPQYV
REKYKLTEYN FAIKNIHFPK NMEIFCEARK RLVFEEFFMF IMSIRQLKDN NDLQPNHFHI
QNDDRTDKMI ERLPYRLTNA QLKAWAEVKQ NMSSDKLMNR LIQGDVGSGK TIIATLALMN
TVYKGYQAAM MVPTEVLAKQ QYASIRQLFA EYNIDIKLSL LTGSLTAKEK TLEYERIQSG
EAQIVIGTHA LIQEKVQYDN LALVITDEQH RFGVNQREAL SNKGKEPHIL VMSATPIPRT
LAIIIYGDLD ISIIDEMPSN RLPIKNCVVG ESYRPKAYQF ISEQVSQGRQ AYVICPMVEE
SENVEAENVV DYSMMLKEGM PKIMTSDGTF KTVSIEYLHG KMKSSMKNEI MEKFTAGQID
VLVSTTVIEV GVNVPNSTVM LIENADRFGL AQLHQLRGRV GRGGDQSYCI FVSDSRSKKT
KERLDILNKS NDGFKIAEED MKLRGPGDFF GIRQSGIMEF GIGDIFTDAL ILKDASDAVN
EIMTIDPELL RDENQILKEK LLKQTEKLIN KLNI
//
