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Database: UniProt
Entry: G9YJE9_9FIRM
LinkDB: G9YJE9_9FIRM
Original site: G9YJE9_9FIRM 
ID   G9YJE9_9FIRM            Unreviewed;       677 AA.
AC   G9YJE9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=HMPREF0080_01798 {ECO:0000313|EMBL:EHM38666.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM38666.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM38666.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM38666.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:ARBA00024832, 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:EHM38666.1}.
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DR   EMBL; AGCJ01000076; EHM38666.1; -; Genomic_DNA.
DR   RefSeq; WP_006790763.1; NZ_JH417605.1.
DR   AlphaFoldDB; G9YJE9; -.
DR   STRING; 861450.HMPREF0080_01798; -.
DR   GeneID; 85019907; -.
DR   PATRIC; fig|861450.3.peg.1662; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000005481; 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; 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; 2.
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:UP000005481}.
FT   DOMAIN          269..430
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          448..609
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   677 AA;  74389 MW;  BA6B9021AF63FCDA CRC64;
     MTVAITEIKG IGAQKGKLFA KVGIRTVTDL LQYFPRAYED RSHIVPIGEA AAAEGLSVLI
     NGTVSSVTEV RPRRGMTILK VFISDSTGAV ELIWFNRPFK KRMFRKGMEV HAFGKIEHRY
     GRLQMNSPEA EPGVAAPGGL VPVYALTDGL YQNDFRKAVT AAFAYAKEYG DVLPACLSAE
     VTGRAVTAEM YKAIHFPPDF EVLKKARKIL AFEELFSLQA GLLLKRQENK AGRAVKFGPN
     GKLVKGLLNN LPFTLTQGQI DAFSDIQNDV ETESPMQRLI QGDVGSGKTV VAALALAKTV
     ENGYQGALMA PTGILAVQHY EEFTRLFTGL PVTVALLTGR STAKERAELL RGLANRDIDI
     LVGTHALIQE DVVFADLALA VTDEQHRFGV KQRVKLRDKG KAPHSLYMTA TPIPRTLALS
     VYGDLDVSTI REVPPGRKPV KTYAVGEGMR ARVYAFMKKR IAEGQQVYVV CPLVEESESA
     DLQAASALYE DLSRHAFKEY RCGLVHGRMS GKEKDAVMDA FRQGDLNILS ATSVIEVGVN
     VPNATIMLID GAERFGLAQL HQLRGRVGRG ILQAYCILLA KSGSEETRQR MKWMETIHDG
     FKLSEKDLLL RGSGQLFGYM QHGLPDLRVA DIVGDAALLV PAREAAQHYL REPGRKEIIV
     KALKHRFGDS FAKILNN
//
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