ID A0A494XFS6_9BURK Unreviewed; 795 AA.
AC A0A494XFS6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:RKP48712.1};
GN ORFNames=D7S86_21605 {ECO:0000313|EMBL:RKP48712.1};
OS Pararobbsia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pararobbsia.
OX NCBI_TaxID=1792498 {ECO:0000313|EMBL:RKP48712.1, ECO:0000313|Proteomes:UP000270342};
RN [1] {ECO:0000313|EMBL:RKP48712.1, ECO:0000313|Proteomes:UP000270342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHC34 {ECO:0000313|EMBL:RKP48712.1,
RC ECO:0000313|Proteomes:UP000270342};
RA Gao Z.-H., Qiu L.-H.;
RT "Robbsia sp. DHC34, isolated from soil.";
RL Submitted (OCT-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:RKP48712.1}.
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DR EMBL; RBZU01000011; RKP48712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XFS6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000270342; 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; 3.
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:UP000270342}.
FT DOMAIN 339..551
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 584..730
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 85730 MW; 1540402DB564B218 CRC64;
MHPEPGDAAP SARPEGSARA IGRGAKAAEN APKTPKAEDG PKAPEAPKAA KAAKAPKAPK
AAKVPRKPET TADKLARMGL SRDIDLVLHL PMRYEDETAI VPIDDLLPGQ SAQVEGVVVD
NEIAFRPRRQ MVVKIVDDAR GELTLRFLNF YGSQTKQLAV GTRVRARGDV RGGFFGMEMV
HPAYRVVAEG DPLPQSLTPV YPSTAGVPQA YLRKAIDRAL EHTSLPELLP AAIAAAYLDP
MNVPPLAQAV RMLHHPGTAE NEHALMDGSH PAWLRIKFEE LLAQQLSLQR AHAARRARSA
PLLARRQDAP DSLVARFERA LPFALTEAQQ RVWREIGAEL EAAHPMQRLL QGDVGSGKTI
VAALAAAQAI DAGYQAALMA PTEILAEQHA RKLRSWLEPL GVQVAWLAGS LKAREKRAAV
EAAANGTAQL IIGTHALVQD TVDFARLGLV IVDEQHRFGV AQRLALRSKA KGARASNADD
TGHARSDEAR ATAVGSDKRH ASPDPRTATR RDADPDADSD AFQPHQLMMS ATPIPRTLAM
TYYADLDVST LDELPPGRTP VLTKLVSDAR RDEVIARVRQ AALGGRQVYW VCPLIEESEA
LQLQTAVDTH ATLVAALPEL AVGLVHGKLA PADKAAVMSG FIDNRIQLLV ATTVIEVGVD
VPNASLMVIE HAERFGLAQL HQLRGRVGRG TAASVCVLVY ANPLSLTARA RLSTMRETAD
GFEIARRDLE IRGPGEFLGA RQSGAAMLRF ADINEDGWMI EPARSAATRL LSDFPAAAQA
HLDRWLGGRE HFLKA
//
