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Database: UniProt
Entry: C4Z9X3_AGARV
LinkDB: C4Z9X3_AGARV
Original site: C4Z9X3_AGARV 
ID   C4Z9X3_AGARV            Unreviewed;       688 AA.
AC   C4Z9X3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=EUBREC_1670 {ECO:0000313|EMBL:ACR75414.1};
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR75414.1, ECO:0000313|Proteomes:UP000001477};
RN   [1] {ECO:0000313|EMBL:ACR75414.1, ECO:0000313|Proteomes:UP000001477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990 {ECO:0000313|Proteomes:UP000001477};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR75414.1; -; Genomic_DNA.
DR   RefSeq; WP_012742512.1; NC_012781.1.
DR   AlphaFoldDB; C4Z9X3; -.
DR   STRING; 515619.EUBREC_1670; -.
DR   PaxDb; 515619-EUBREC_1670; -.
DR   KEGG; ere:EUBREC_1670; -.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   Proteomes; UP000001477; 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   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          274..437
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          456..616
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   688 AA;  77632 MW;  3EA90144E3776432 CRC64;
     MDIASPITAV KGIGEKTQKA FAKMGVYTVG DILLHFPRDY VKFPEITDID ELNNVNVSST
     YAIYAVIKKA PVVKNTARMQ ITLQDIGSPG HMIQLVWYRM PYLKAQLVQG RHLIFYGHIK
     PKGGRYVMEQ PVVYEVQKYE AIRDTLQPVY SVTSGVTNNL IVKTIKETLS HDTLLSDYLP
     KDIRHRYGFC EYNYAMKQIH FPDDFDALVE ARRRLVFDEF FLFIMGMRYQ NKKQQKDKNE
     FEFTDDAFID GLIDKLPYEL TGAQKKTIDE IKQDIKSPYV MQRLIQGDVG SGKTIVAFLL
     MAWASKCGYQ SAIMAPTEVL ANQHYETFCS LVSQFGLDSP VVLLTGSMTA KQKREAYASL
     ENEKNALIIG THALIQEKAD FSNLSLVITD EQHRFGVKQR ESFSDKGRKP HILVMSATPI
     PRTLAIIIYG DMDISVINEV PAKRLPIKNC VVGTAFRPKA YSFIEEQVRA GHQAYVICPL
     VEETENSEGE NVTDYADVLK AALPKDITVD VLNGRMKSKA KDEVMQRFAN NESQVLVSTT
     VVEVGVNVPN ATVMMIENAD RFGLAQLHQL RGRVGRGDAQ SYCIFINSSN SKKSKKRLEI
     LNKSNDGFYI ASEDLKLRGP GDFFGIRQSG DLAFALADVY QDSDVLKEAS EMVDEVLEAD
     PALCTPENRI LKKKMDEFAK EQLKRMNL
//
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