ID RECG_MYCBO Reviewed; 737 AA. AC P64323; P95122; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 19-MAR-2014, entry version 61. DE RecName: Full=ATP-dependent DNA helicase RecG; DE EC=3.6.4.12; GN Name=recG; OrderedLocusNames=Mb2998c; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- FUNCTION: Critical role in recombination and DNA repair. Help CC process Holliday junction intermediates to mature products by CC catalyzing branch migration. Has a DNA unwinding activity CC characteristic of a DNA helicase with a 3' to 5' polarity. RecG CC unwind branched duplex DNA (Y-DNA) (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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; BX248344; CAD96685.1; -; Genomic_DNA. DR RefSeq; NP_856643.1; NC_002945.3. DR ProteinModelPortal; P64323; -. DR SMR; P64323; 2-700. DR STRING; 233413.Mb2998c; -. DR EnsemblBacteria; CAD96685; CAD96685; Mb2998c. DR GeneID; 1093419; -. DR KEGG; mbo:Mb2998c; -. DR PATRIC; 18008326; VBIMycBov88188_3295. DR eggNOG; COG1200; -. DR HOGENOM; HOG000036618; -. DR KO; K03655; -. DR OMA; PHVLTMT; -. DR OrthoDB; EOG6FNHKW; -. DR ProtClustDB; PRK10917; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC. DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. 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 Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50249; SSF50249; 2. 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; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding. FT CHAIN 1 737 ATP-dependent DNA helicase RecG. FT /FTId=PRO_0000102147. FT DOMAIN 302 477 Helicase ATP-binding. FT DOMAIN 514 673 Helicase C-terminal. FT NP_BIND 315 322 ATP (Potential). FT MOTIF 427 430 DEQH box. SQ SEQUENCE 737 AA; 80361 MW; 97BAC1C8C4A0732F CRC64; MASLSDRLDR VLGATAADAL DEQFGMRTVD DLLRHYPRSY VEGAARVGIG DARPEAGEHI TIVDVITDTY SFPMKKKPNR KCLRITVGGG RNKVTATFFN ADYIMRDLTK HTKVMLSGEV GYYKGAMQLT HPAFLILDSP DGKNHGTRSL KSIADASKAI SGELVVEEFE RRFFPIYPAS TKVQSWDIFK CVRQVLDVLD RVDDPLPAEL RAKHGLIPED EALRAIHLAE SQSLRERARE RLTFDEAVGL QWALVARRHG ELSESGPSAA WKSNGLAAEL LRRLPFELTA GQREVLDVLS DGLAANRPLN RLLQGEVGSG KTIVAVLAML QMVDAGYQCA LLAPTEVLAA QHLRSIRDVL GPLAMGGQLG GAENATRVAL LTGSMTAGQK KQVRAEIASG QVGIVIGTHA LLQEAVDFHN LGMVVVDEQH RFGVEQRDQL RAKAPAGITP HLLVMTATPI PRTVALTVYG DLETSTLREL PLGRQPIATN VIFVKDKPAW LDRAWRRIIE EAAAGRQAYV VAPRIDESDD TDVQGGVRPS ATAEGLFSRL RSAELAELRL ALMHGRLSAD DKDAAMAAFR AGEVDVLVCT TVIEVGVDVP NATVMLVMDA DRFGISQLHQ LRGRIGRGEH PSVCLLASWV PPDTPAGQRL RAVAGTMDGF ALADLDLKER KEGDVLGRNQ SGKAITLRLL SLAEHEEYIV AARDFCIEAY KNPTDPALAL MAARFTSTDR IEYLDKS //