ID A0A2C9ZIA6_BACTV Unreviewed; 682 AA. AC A0A2C9ZIA6; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 29-SEP-2021, entry version 11. 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=BK784_12490 {ECO:0000313|EMBL:OUC01763.1}; OS Bacillus thuringiensis subsp. medellin. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=79672 {ECO:0000313|EMBL:OUC01763.1, ECO:0000313|Proteomes:UP000195160}; RN [1] {ECO:0000313|EMBL:OUC01763.1, ECO:0000313|Proteomes:UP000195160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30001 {ECO:0000313|EMBL:OUC01763.1}; RA Zheng J., Gao Q., Liu H., Peng D., Ruan L., Sun M.; RT "Comparative genomics of Bacillus thuringiensis reveals a path to pathogens RT against multiple invertebrate hosts."; RL Submitted (OCT-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|ARBA:ARBA00003447, 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|ARBA:ARBA00001665, CC 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:OUC01763.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MOOV01000091; OUC01763.1; -; Genomic_DNA. DR EnsemblBacteria; OUC01763; OUC01763; BK784_12490. DR Proteomes; UP000195160; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.300; -; 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; IPR033454; RecG_wedge. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF17191; RecG_wedge; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00643; recG; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363016}; KW DNA damage {ECO:0000256|RuleBase:RU363016}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, KW ECO:0000256|RuleBase:RU363016}; DNA repair {ECO:0000256|RuleBase:RU363016}; KW Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:OUC01763.1}; KW Hydrolase {ECO:0000256|RuleBase:RU363016}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363016}. FT DOMAIN 271..432 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 451..611 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" SQ SEQUENCE 682 AA; 77626 MW; D4D93F3E32B08727 CRC64; MNDVVQVPVT DVKGIGGETS ELLHEMGIYT VSHLLEHFPY RYEDYAMKDL AEVKHDERVT VEGKIHSAPL LQYYGKKKSR LTVRVLVSRY LITAVCFNRP YYKQKLKLDE TVTITGKWDQ HRQTIAVSEL HFGPVVRQQE VEPVYSVKGK LTVKQMRRFI AQALKEYGDS IVEVLPDGLL GRYKLLPRYE ALRALHFPVG QEDLKQARRR FVYEEFFLFQ LKMQTLRKME RENSKGTKKE IPSVELQEFI DALPFPLTGA QRRVVDEILK DMTSPYRMNR LLQGDVGSGK TVVAAIGLYA SKLAHYQGAL MVPTEILAEQ HYQSLAETFS HFGMKVELLT SSVKGARRRE ILAKLEQGEI DILVGTHALI QDEVIFHRLG LVITDEQHRF GVAQRRVLRE KGESPDVLFM TATPIPRTLA ITAFGEMDVS IIDEMPAGRK VIETYWAKHD MLDRVLGFVE KEIKKGRQAY VICPLIEESE KLDVQNAIDL HSMLTHHYQG KCQVGLMHGR LSSQEKEEIM GQFSENKVQI LVSTTVVEVG VNVPNATVMV IYDAERFGLS QLHQLRGRVG RGSEQSYCLL IADPKSETGK ERMRIMTETN DGFVLSEKDL ELRGPGDFFG SKQSGLPEFK VADMVHDYRA LETARQDAAI LVDSEAFWHN DQYAALRTYL DGTGVFQGEK LD //