ID A0A399ESF2_9DEIN Unreviewed; 770 AA.
AC A0A399ESF2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 ECO:0000313|EMBL:RIH86908.1};
GN ORFNames=Mlute_01109 {ECO:0000313|EMBL:RIH86908.1};
OS Meiothermus luteus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=2026184 {ECO:0000313|EMBL:RIH86908.1, ECO:0000313|Proteomes:UP000265800};
RN [1] {ECO:0000313|EMBL:RIH86908.1, ECO:0000313|Proteomes:UP000265800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52599 {ECO:0000313|EMBL:RIH86908.1,
RC ECO:0000313|Proteomes:UP000265800};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus luteus KCTC 52599 genome sequencing project.";
RL Submitted (AUG-2018) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIH86908.1}.
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DR EMBL; QWKZ01000027; RIH86908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399ESF2; -.
DR Proteomes; UP000265800; 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; 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}.
FT DOMAIN 358..517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 536..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 770 AA; 85907 MW; 1D05C14AFF4FF1B4 CRC64;
MEELRTRLLR PLERELADGA RDRVVAGGLE KLVQNLARPF PEVQRTLSGY RGMDLQTRLE
RLKKAIALLG GQAKVPSEPC PSATPPLGPD LDAPLGVLEL GPGGRKKLAE LGLRSLRDLL
HYYPRRYEDR RTLGSIRDAE DGSKATVVGK VLSRELVKTP KKGMQLVQVR FMDAWGWKFT
GVWFNQPWVL KQVPEGASLV LTGRVQRRGG AISMVVEYFE DEGGESLSTG RIVPVYGAKE
GVGQAFLRRL VWRALQAFPH LPDPLEAYVK DQGLPSLDFA LRQAHFPDTE EKLEQALYRL
KFDEYLLLEL KVMITSGGSA LLGRMFKVTP GMLERFRATL PFQLTRAQER VLGEILSDMQ
SERQMARLVQ GDVGSGKTVL AAAALYIAAE NGAQGALMAP TEILAKQHFE NLTRYLYPLG
VRVDLLVGSL SQGEKKTVLE RLRTGQTQVV VGTHALIQDG VEFHDLGLAV IDEEHRFGVL
QRRRLLGQRP DVLVMSATPI PRSLALTMYG DLEVSQIDEL PPGRIPVRTK LLTQKTRLQA
YAFARQEIQK GHQVFVVTPM IEEGASEATL ELAAATRLRE ELESLLPEAR IDLLHGRMKP
EEKDAVMERF RRGEFDLLVS TTVIEVGVDI PRATLMVIEN AERFGLAQLH QLRGRVGRGG
LEAYCILIAG ETSKRTLERL RVIEGSNDGF YIAEQDLRLR GPGELRGLRQ SGMPDLRLGD
LASDQEIIER SRALAQAILE TDPYLDKPEH ALLKRELQAR AEAVGFREVI
//
