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Database: UniProt/TrEMBL
Entry: D7APE6_THEM3
LinkDB: D7APE6_THEM3
Original site: D7APE6_THEM3 
ID   D7APE6_THEM3            Unreviewed;       681 AA.
AC   D7APE6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
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   OrderedLocusNames=Tmath_1348 {ECO:0000313|EMBL:ADH61062.1};
OS   Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS   53645 / CIP 108742 / A3).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61062.1, ECO:0000313|Proteomes:UP000002064};
RN   [1] {ECO:0000313|EMBL:ADH61062.1, ECO:0000313|Proteomes:UP000002064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11426 / CIP 108742 / A3
RC   {ECO:0000313|Proteomes:UP000002064};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT   mathranii str. A3.";
RL   Submitted (MAY-2010) 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}.
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DR   EMBL; CP002032; ADH61062.1; -; Genomic_DNA.
DR   RefSeq; WP_013150379.1; NC_014209.1.
DR   AlphaFoldDB; D7APE6; -.
DR   STRING; 583358.Tmath_1348; -.
DR   KEGG; tmt:Tmath_1348; -.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   Proteomes; UP000002064; Chromosome.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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}.
FT   DOMAIN          270..431
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          454..610
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   681 AA;  77288 MW;  198F40D2347AC862 CRC64;
     MPLNLDIQYV KGVGPKRAKL LKKLGIQTVE DLLFYFPKDY ENRSSILKIE DLTVGEKQTF
     KGYIVGSPRE IKTSRVIITK VPVKDGTGAV ELVWYNQPYI KNNLKIGEEY IINGKLRFKY
     GQLIVENPVI EKSEDFKLNT GRIVPIYGLT EGLTQNAIRK IMFNALKEYV QEVEEFFDEE
     FLSEKRLMDI KSALININFP QNEAYLEQAK YRFKYQELFL LQMALFLMKG SAKEKKGIKF
     ERVDLKPFIM GLPFKLTQAQ VKVLKEIIAD MNSHKVMNRL VQGDVGSGKT VVAACSMYIA
     VKNGYQVAMM APTEILAKQH YSTLKELFKN TDIKIGLLSG SLSPSNKKEV LEKIKKGDYD
     IIVGTHALIE DDVVFNNLGL CITDEQHRFG VRQRALLTQK GKNPDVLVMT ATPIPRTLAL
     ILYGDLDISI IDQLPPGRKK VKTYVISSSV RKKAYEFAMK EVKKGRQVYV VCPLIEESDK
     ISAMSAEIVY REIYKDAFKE AKVGLLHGKM ADSEKEKVME EFVNGKIDIL VSTTVIEVGV
     NVPNATVMII ENAERFGLAQ LHQLRGRVGR SEFQSYCILI SYSNSDVAKK RLGVLAQTSD
     GFKIAEKDLE IRGPGEFLGL RQHGLPEFKI ANIVEDIDIL KIVQKDVEEL LKKDPKLENY
     PKIKNILLNQ FYQKLEGIIL N
//
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