ID A0A1G5UW87_9FIRM Unreviewed; 678 AA.
AC A0A1G5UW87;
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=SAMN02910343_00012 {ECO:0000313|EMBL:SDA37045.1};
OS Allisonella histaminiformans.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Allisonella.
OX NCBI_TaxID=209880 {ECO:0000313|EMBL:SDA37045.1, ECO:0000313|Proteomes:UP000199689};
RN [1] {ECO:0000313|EMBL:SDA37045.1, ECO:0000313|Proteomes:UP000199689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15230 {ECO:0000313|EMBL:SDA37045.1,
RC ECO:0000313|Proteomes:UP000199689};
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; FMXA01000003; SDA37045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5UW87; -.
DR STRING; 209880.SAMN02910343_00012; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000199689; 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 CDD; cd04488; RecG_wedge_OBF; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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:UP000199689}.
FT DOMAIN 273..434
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 453..613
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 678 AA; 76979 MW; 2FFE0192B5044626 CRC64;
MELKDKVTAV KGVGPKMEEK LGRLGIHTVE DLISYFPRKY QDWTDITPMD ALDTEDEHVV
YGRIVDVREV RPRPRLSIIT VVLTDGRGAV NLTYFNQPWK RQAFDRGQGI LAYGKVEYVY
GKYQMSNAET ISARPEEIQS LKKLVPVYPL TEGIRLQQMQ KMIAYALQHM DTIEENLPSR
VRMKYHLMER KEAVYAMHFP RSWEEQKRAR YRLAFEELFF MQAGIWLLRK KREQGHTGIK
CSPDGKLMLS VMKNIPFELT DDQKQVLVDI ESDMEGLVPM QRLIQGDVGS GKTVIAALAL
AKIVENGYQG ALMAPTEILA AQHYKTLSEL YDGTGICTEL LTGQTRASEK KEILSRLASG
KIDILVGTHS LIEDPVEFAH LGMVVTDEQH RFGVKQRERL ETKGDNPHIL VMTATPIPRT
MALSVYGDLD VSSIRHLPPG RQPVGTYAVG RNMLARIYRF MKKEMNMGHQ VYVVCPLVEE
SEKADLAAAV SVYEELRTKQ FPEFCLGLVH GQMKAREKDE VMEAFVQGKI QMLVATSVIE
VGVNVPNATI MFIYGADRFG LSQLHQLRGR VGRGKAKSYC ILYSDNTSEA AEFRLSLMTK
IQDGFTLAEK DLLLRGSGEF FGTRQHGMDD LKVANVIRDL PILEEARKAA REEISHGLDV
KEELARRFHG EFFSRIYH
//
