ID A0A1M6X4D6_9FLAO Unreviewed; 701 AA.
AC A0A1M6X4D6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05443634_105106 {ECO:0000313|EMBL:SHL00776.1};
OS Chishuiella changwenlii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chishuiella.
OX NCBI_TaxID=1434701 {ECO:0000313|EMBL:SHL00776.1, ECO:0000313|Proteomes:UP000184120};
RN [1] {ECO:0000313|Proteomes:UP000184120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27989 {ECO:0000313|Proteomes:UP000184120};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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|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; FRBH01000005; SHL00776.1; -; Genomic_DNA.
DR RefSeq; WP_072931102.1; NZ_FRBH01000005.1.
DR AlphaFoldDB; A0A1M6X4D6; -.
DR STRING; 1434701.SAMN05443634_105106; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000184120; 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; 2.
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 285..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 466..633
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 701 AA; 79832 MW; B4D7227DD0F9AE6C CRC64;
MYQNPLKKTI EYLKGAGPER AKALQSEFGI FRYEDLLQHF PFRYVDKSKF YKVSEISSTD
AEIQLKGKIV ELEEINQGKV KRLKGKFQDT SGTLELVWFK ISTWQKDKLK SDLFKEIVIY
GKPSVFNGTY SITHPEIELI EDAKSVSLGL FPVYPSTEKL TKRGITNRVM QKMMQNLFAE
NIAIAENLPE NVLDHFKLIG RNEALKAIHF PKDLNELNAA VRRLKFEEFF FLNLANLSQK
AVNKQKNKSN PFPIIGDYFN TFYNEYLPFE LTNAQKRVIK EIRTDLRQPA QMNRLLQGDV
GSGKTMVALL TMLIAIDNGF QAALIAPTEI LAQQHFESIT ELLNDLDVSV KLLTGSVTKK
KRQPILEDLE SGELKIIVGT HALLEDNVVF KNLGLAVIDE QHRFGVAQRA KFWRKATLPP
HVLVMTATPI PRTLSMTMYG DLDVSVIDEL PKGRKPIKTV HKTDAYRLSV FKFIKDEIAK
GRQIYIVYPL IEESDKLELK DLMDGYESIS RAFPLPEYAI SIVHGRQKPA DKEFEMNRFK
NNETQILVAT TVIEVGVNVP NASVMIIENS ERFGLSQLHQ LRGRVGRGAE QSFCILMTGK
KLNDVSRRRI QTMCETNDGF KVAEVDLELR GPGDMMGTQQ SGVLNFKIAD LAKDKEILYA
ARKCVEKILE YDPTLSLPIN IPTKNFFLEN HKDKVGWSQI S
//
