ID A0A081P5T0_9BACL Unreviewed; 950 AA.
AC A0A081P5T0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=ET33_36335 {ECO:0000313|EMBL:KEQ26053.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ26053.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ26053.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ26053.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEQ26053.1}.
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DR EMBL; JNVM01000008; KEQ26053.1; -; Genomic_DNA.
DR RefSeq; WP_036680584.1; NZ_JNVM01000008.1.
DR AlphaFoldDB; A0A081P5T0; -.
DR eggNOG; COG1199; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000028123; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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; 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; 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; PS51192; HELICASE_ATP_BIND_1; 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:KEQ26053.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT DOMAIN 251..522
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 273..511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..949
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 467..470
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 286..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 950 AA; 108536 MW; FDBACD3CAFA77F50 CRC64;
MKFAVLDFET TGSTATDRII QVGLFLINDH EMTDRYTSLV NPGISIPSSI TTLTGIDDEM
VKDAPAMEEV IAEMVPLLQD AVLVGHNIAF DLAFLQRALD DNGYFPFDGR VLDTMDALRV
LFPGLSSLQL SMVCHAFGIE HERPHQADSD AEVTALIWLR CMERFQSLPL LTLQRLELVF
TDSAGDFGWF VSEMRQYKEL HQPLDPDLDR YFRQFALNVG EWGEEEPVRE EEDVLRLPDD
FPSFYVQLKQ ELQQRFAAYE DRESQVQMLS EVETAFEDGK HLMIEAGTGT GKSLGYLIPS
LYYGLKQDKK VLVSTHTINL QEQLRERDVP LLHELFPVGF RAAVLKGRSH YLCLRKFEHK
MNMLDFEHGK EDRITAGQML VWLGETKHGD EEELHFANKG KQFWQSVESD TDSCLNRACP
WFKKCFYHRA RHEANTADVI ITNHSLLFTD MKAENRLLPG YKHLVIDEAH HFEEVAGKHL
GIELHYHGLS NTLLWLYKDA RSGQLSNLRI RLQRFEDERA QGWCISIDRV VEKLLQLKEE
WDQLTELLYQ LLASRSDPSQ SEGNGLVYRV KKDSLPTGWD KLEVLEENMQ LNFGEALKPL
DKLISEIKEV QDEYDVQSLI TDLSGTVKEL YRHRDSLHFF MTMPDANYVY WLEAGTYSKN
RSLQLFCVPI DVSEMLKQHF FGPKDSVILT SATLSVGKSF DYTCDQLGLR ENGADGKLKT
VQLPSPFNYR DQALVAIPRD FPTLRGASGE KEFVDRLVPS LAEVALETRG RMLVLFTSNR
MLKLVHGALK EMLSPFGIGV LGQGVDSSNR SKLTRLFQNS PNCVLLGTSS FWEGVDIPGN
ALTCLAIVRL PFQPPNHPLI EAKTEMIKQR NQNPFMKLSV PQAVIRFKQG FGRLVRTATD
KGIVIIYDTR VIDTNYGKYF LYSLPGPKIE HMNSNQLVPR IKQWMGENQA
//
