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Database: UniProt
Entry: A4G1Z1_HERAR
LinkDB: A4G1Z1_HERAR
Original site: A4G1Z1_HERAR 
ID   A4G1Z1_HERAR            Unreviewed;       711 AA.
AC   A4G1Z1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 97.
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   ECO:0000313|EMBL:CAL60528.2};
GN   OrderedLocusNames=HEAR0301 {ECO:0000313|EMBL:CAL60528.2};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60528.2, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL60528.2, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL60528.2; -; Genomic_DNA.
DR   AlphaFoldDB; A4G1Z1; -.
DR   STRING; 204773.HEAR0301; -.
DR   KEGG; har:HEAR0301; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_4; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; 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|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363016};
KW   DNA recombination {ECO:0000256|RuleBase:RU363016};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363016};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:CAL60528.2};
KW   Hydrolase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:CAL60528.2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT   DOMAIN          296..467
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          490..646
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  78327 MW;  CD364DE53EC80606 CRC64;
     MKKKPVASAK TATQTAAKST AKAAAPAAAT RAAKIDDKLI KLGLRSDMDK VLHLPLRYED
     ETEIRSISEA GFIFGRSVQV EGVVTACEVA FRPRRQLVVT ISDDSGQLVM RFLNFYGSQV
     KQMAEGNRVR ARGEVRHGFF GAEMVHPSYK MVTEGAPLPS ALTPVYPAGE GLSQTLLRKT
     IIDAMARIEW RDTLSEQLRS SLDLMSFEPA VRLLHNPPPD IDESVLADRS HAAWVRMKFD
     ELLAQQLSMK RAQIARREKG AAVLPTIGKL SKAFLKQLPF SLTAAQQRVL EEVRADLKQS
     FPMQRLLQGD VGSGKTVVAA IAAAQAIDSG FQAVLMAPTE ILADQHFRKI AGWMEPLGVN
     VAWLTGSLKK KEKLEAKARI ESGVAQLIIG THALIQEDVQ FSKLGLVIVD EQHRFGVGQR
     LVLRNKGLDA SAAAAQQKIP HQLMMSATPI PRTLAMTYYA DLEVSVIDEL PPGRTPIVTR
     VIDQNRRDEV IERVHAAALE GRQVYWVCPL IEESEALQLQ TATDTHQTLV AALPDLQVGL
     VHGRMKPADK QQVMDAFTRG DIHVLVATTV IEVGVDVPNA SLMVIEHAER FGLSQLHQLR
     GRVGRGSTAS VCLLLYQGPL GMVAKQRLRI MRESTDGFEI ARKDLEIRGP GEFLGARQSG
     QAMLRFADLE TDQWLVDRAR DLAQTLLRDD PATVGAHLAR WLGAREDYLK V
//
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