ID A0A2A2G7T5_9BACT Unreviewed; 689 AA.
AC A0A2A2G7T5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CK503_14185 {ECO:0000313|EMBL:PAU93064.1};
OS Aliifodinibius salipaludis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=2032627 {ECO:0000313|EMBL:PAU93064.1, ECO:0000313|Proteomes:UP000218831};
RN [1] {ECO:0000313|EMBL:PAU93064.1, ECO:0000313|Proteomes:UP000218831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN023 {ECO:0000313|EMBL:PAU93064.1,
RC ECO:0000313|Proteomes:UP000218831};
RA Liu D., Zhang G.;
RT "Aliifodinibius alkalisoli sp. nov., isolated from saline alkaline soil.";
RL Submitted (AUG-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:PAU93064.1}.
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DR EMBL; NSKE01000011; PAU93064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2G7T5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000218831; 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:UP000218831}.
FT DOMAIN 276..437
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 456..621
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 689 AA; 78641 MW; 5536DA69BE1A13E5 CRC64;
MKLVDLPNLS TKRLKALSES GIDSLLDLLN WFPHRYLDRT TVLPIRQVKG QGEEVTVVGR
IQKIRQKGYG KKKRLEVILQ DDTASLKGVW FKGGHYIKKQ FSEDDAVAFF GKAKQYGRYV
SMAHPEWDKI DDTSDIQDLK QIVPIYPSNK TFSKRRITSK LIHQWQKVIL KHERPPEFLP
AKIRDQHNLP KRHESYRMIH FPESQSEYKQ AFKRFKFEEL FLFELSVAKT KHEIIERNEG
ALFTDLDQYT QPFFNEHLPF ELTEGQKSAL ADIKKDVRSG KQMNRLIQGD VGSGKTIVAL
GAILMALDNG YQAAFMAPTE ILAEQHYRTL SNFLDPLDVN VRLLVGNQKT SLRTDILTDI
EGGNCDIVVG THAVIQDEVN FNNLGLAVID EQHRFGVKQR AEILTKGSHP HVLVMSATPI
PRSLAMTLYS DLDISIIKGL PGGRKPVKTA VRHQSKHDDI YNFVEQELRE GGQAYVVYPL
VEESEKMDLK DATAGYKKLK KRFSDFEVGL LHGQMKSEEK DAVMQQFINN DIQVLVSTTV
IEVGVDVPNA SIMIVEHAER FGLSQLHQLR GRIGRGKRQS YCILVHGQKV SKEGKFRLRK
MAQTSDGFEI AEADLKLRGP GDFLGTKQSG LPEFRVADIV EDQWILEQAK SAAWEIMNDD
PDLQKPEYQK LKEVFIPYYK EKSKFYGMG
//
