ID A0A2A8CXI5_9BACT Unreviewed; 700 AA.
AC A0A2A8CXI5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CRI94_10620 {ECO:0000313|EMBL:PEN13098.1};
OS Longibacter salinarum.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longibacter.
OX NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN13098.1, ECO:0000313|Proteomes:UP000220102};
RN [1] {ECO:0000313|EMBL:PEN13098.1, ECO:0000313|Proteomes:UP000220102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN13098.1,
RC ECO:0000313|Proteomes:UP000220102};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longibacter Salinarum.";
RL Submitted (OCT-2017) 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:PEN13098.1}.
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DR EMBL; PDEQ01000005; PEN13098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8CXI5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000220102; 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 CDD; cd18811; SF2_C_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:UP000220102}.
FT DOMAIN 286..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 466..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 659..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 79504 MW; 3E6B45C4756B6F0E CRC64;
MSDDFLQESV RYLKGVGERR AEVWDDQFGV RTVRDLLHFY PRRYLDRSTI TPVGQLRESS
DPVTVVGTVR AKDIVPGKRS KRFELILEGE RGAKMKCTWF QGIWFIPKVF EVGERVAFHG
KVQKYGRWFS MTHPDYDKLE GESALLDTGR IVALYPGSEA MDKVGLNSRS IRRVVYNLFK
EHGLKLEEPL PDWMTDRFEL MEGRVALRAI HFPKSQSELS RARTRLKFEE LFYIQLLLAD
MRQSRSEIAG PMFDEPGDYT RQFVREVLPF ELTGAQKRAL KDVIADTQTG TQMNRLVQGD
VGSGKTVVAV AAMMHALDSG YQSAFMAPTE ILAEQHYTNL RKYLNPLGIE PRLLIGSQSK
SEREEALRAV RSADAPVAVG THALIQEEVQ FDRLGLAIVD EQHRFGVAQR ATIFDKGDRP
HMLLMTATPI PRSLAMTLYG DLDVSIMDEM PAGRKPVKTV LRAEKRRGEV YAFVQDQLEK
GQQAYVVYPL VEESEKVDLK DAVSGYEKLQ KQFSNHTVGL VHGQMKSDEK DATMRRFKNG
EIDLLVSTTV IEVGVDVANA TLMIIEHAER FGLSQLHQLR GRVGRSDIQS YCILMAGYKR
SAEAKERLQA MVDTNDGFEI SERDLQIRGA GDFFGTRQSG LPDLKIADIT EDEDLIEEAR
EGAQELVERD PELDAPEHSR IRDRYDAEYR PRQDSFARVG
//
