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Database: UniProt
Entry: E4THX5_CALNY
LinkDB: E4THX5_CALNY
Original site: E4THX5_CALNY 
ID   E4THX5_CALNY            Unreviewed;       756 AA.
AC   E4THX5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
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=Calni_0994 {ECO:0000313|EMBL:ADR18905.1};
OS   Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Calditerrivibrionaceae.
OX   NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18905.1, ECO:0000313|Proteomes:UP000007039};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA   Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Calditerrivibrio nitroreducens DSM
RT   19672.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADR18905.1, ECO:0000313|Proteomes:UP000007039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC   {ECO:0000313|Proteomes:UP000007039};
RX   PubMed=21475587; DOI=10.4056/sigs.1523807;
RA   Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT   (Yu37-1).";
RL   Stand. Genomic Sci. 4:54-62(2011).
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}.
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DR   EMBL; CP002347; ADR18905.1; -; Genomic_DNA.
DR   RefSeq; WP_013451118.1; NC_014758.1.
DR   AlphaFoldDB; E4THX5; -.
DR   STRING; 768670.Calni_0994; -.
DR   KEGG; cni:Calni_0994; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_0; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000007039; 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   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:UP000007039}.
FT   DOMAIN          344..504
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          523..688
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   756 AA;  87264 MW;  194EDD584767F5E3 CRC64;
     MSLDLSILKQ LNNILKNKGY YYKNFKSYLL PLKDKLPLEI SQKIDNIITK ENPETSELDD
     IVNDILLEIY SIKRGDYNRL KEPLVIKFSN FVKTLEQLKK IGIETAEDII FHFPYKYDIL
     SSSSNDRCVL TGTFEDSKIV KTKNGKKILE AVFKGDTGYF YGVWFNFNNR YPLLLLKKGE
     NYNLYGKLQN FNGLPAIVHP EFLSTDELGK IRPVYLLPEN VKDNLYLSLL KKVYMEYSEH
     IVETLPLRLI IKYGFLDLKN SLRYIHFPDN INEFKKYNLL SHRRFVYEEL FYLQLGLFIR
     KNSYGEVRGI KFDIDKDILL TLKPYIPFKL TDAQKKALKD IFNDMKSSKQ MNRLLQGDVG
     SGKTVVAFIS GVLAVKNGYQ VAFISPTEIL AEQHYNNFKK LFKDDFSSCL ITGSLKQKDK
     KYLKALVESG DISFIFGTHA ILQEDTIFKN LGFVVIDEQH RFGVMQRKIL IEKGYTPDIL
     LMSATPIPRT LSLTFYGDLE ISIIDQLPPG RKPITTKAFR QKEIGKVFDL VKEQIEKGFS
     AYFVYPLIDE SDTLDLKAAT QAYEQVAEFF GEDNVGILHG RMKAEEKNYL MNRFKNREIK
     ILVSTTVIEV GVDVPHATVM VIENAERFGL SQLHQLRGRV GRGGDQSFCY LVYSDKISED
     GLKRIKAMIN YNDGFKLSEI DLEMRGPGDF FGTRQSGLPD LKFSNIIKDT DILLSAREDA
     FEILKEDPYL NKPENRILKE MLKFKWKDAY ELVNIG
//
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