ID A7GN79_BACCN Unreviewed; 929 AA.
AC A7GN79;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=3'-5' exonuclease DinG {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
GN Name=dinG {ECO:0000256|HAMAP-Rule:MF_02206,
GN ECO:0000256|RuleBase:RU364106};
GN OrderedLocusNames=Bcer98_1265 {ECO:0000313|EMBL:ABS21587.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21587.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS21587.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
CC -!- FUNCTION: Involved in the transposition of the insertion sequence.
CC {ECO:0000256|ARBA:ARBA00002286}.
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|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 2 sub-
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
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DR EMBL; CP000764; ABS21587.1; -; Genomic_DNA.
DR RefSeq; WP_012093754.1; NC_009674.1.
DR AlphaFoldDB; A7GN79; -.
DR STRING; 315749.Bcer98_1265; -.
DR GeneID; 56416848; -.
DR KEGG; bcy:Bcer98_1265; -.
DR eggNOG; COG0847; Bacteria.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_1_0_9; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd06127; DEDDh; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_02206; DinG_exonucl; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR006310; DinG.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR01407; dinG_rel; 1.
DR NCBIfam; TIGR00573; dnaq; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02206};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_02206,
KW ECO:0000256|RuleBase:RU364106}; Helicase {ECO:0000313|EMBL:ABS21587.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02206};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_02206, ECO:0000256|RuleBase:RU364106};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02206}; Nucleotidyltransferase {ECO:0000313|EMBL:ABS21587.1};
KW Transferase {ECO:0000313|EMBL:ABS21587.1}.
FT DOMAIN 249..515
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 744..923
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 463..466
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 284..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 929 AA; 107335 MW; 8E5329CF79EC31AE CRC64;
MSKRYVVVDL ETTGNSWKDG KDKITQIAAV VVEGGEILEI FSSFVNPKRE IPPFITELTG
IDENLVKQAP LFQDVAPMIV ELLQGASFVA HNVHFDWNFL KEELKQAGYA DIHCPKIDTV
ELAQILLPTA DSYKLRDLAK KHELEHDQPH RADSDALATA ELFLQFLTQI EKLPLVTLQS
LYELSDVFQS DMSHILSENI LKKMTAGKEE SEEYDIYRNI ALRKRSYSLH LGENQTSKFS
IFLHKSMEQL EKKVPKFEKR ETQQQMMKEI YAALQDARFS LIEAGTGTGK TLAYLLPSIY
FAKKKEEPVV ISTQTVQLQQ QILEKEIPLL QSVLPFPFEV ALLKGRKHYL CLHKFEYALQ
EDEKNYDIAL TKAKILIWLL KTETGDCDEL NIPEGGKLLW NRICSDAYSP NGVQSSWFSR
CFYQRAKNRA LFADIVITNH TLLFQDFISE ESLFSSYKYI IFDEAHHIEE AASRTLGERF
SCMYFQMVLS RLGTLDTDDV LAKVYKMMKE SGQASRSTFR KISHRLKEMK FDADELFQML
RAFIFQKTKQ EKSSNNNIPL IYRYHTEREN GKLWSGIIEL TSRLIFELKD LCTDLEKQVD
LLQSGMKWNM HVVTGEFFHL ITALRKMTHS LQVLLLEANT YVTWMETETK GTIHSTMLYA
QPIHIGERLA DEFFAEKRSV IFTSATLTVN HTFDYIKEEL GLEDFAPHTL TVPSPFRYEE
QVKLMVPTDI PLIKEVKEEE YIREISQQLK KIAQATNGRI LVLFTSYEML KETYAKLKNE
AALEEYILLT QSVHNRSRSR LIRKFQEFDK AILLGTSSFW EGIDIPGAAL SHLVIARLPF
TPPHQPMMEA KSEWLKRNGE DVFTKLALPQ AILRFKQGFG RLIRSTSDTG TVFVLDRRLT
TSFYGEKFLQ SIPNVPLYEE SLDELLRRL
//
