ID A0A369BUL7_9BACL Unreviewed; 952 AA.
AC A0A369BUL7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DFP94_101901 {ECO:0000313|EMBL:RCX23304.1};
OS Fontibacillus phaseoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX NCBI_TaxID=1416533 {ECO:0000313|EMBL:RCX23304.1, ECO:0000313|Proteomes:UP000253090};
RN [1] {ECO:0000313|EMBL:RCX23304.1, ECO:0000313|Proteomes:UP000253090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8333 {ECO:0000313|EMBL:RCX23304.1,
RC ECO:0000313|Proteomes:UP000253090};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
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:RCX23304.1}.
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DR EMBL; QPJW01000001; RCX23304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369BUL7; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000253090; 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:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 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; 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:RCX23304.1};
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:UP000253090}.
FT DOMAIN 253..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 762..937
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 469..472
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 288..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 952 AA; 107907 MW; 65849DA0FF7B2D77 CRC64;
MKYAVLDFET TGNQSSDEII QVGLAIIDED MKVSRVYSSY VKPGVPIPPF ITGLTGITED
DVRDAPELDE VMMEMVPLLD DAVLVGHNVA FDFNFLQSAL DKTGYLPFTG RILDTMDFLK
IFFPSLTTYQ LGLVASEFGV EHDRPHQADS DALATALIFL KCHEELADLP LLVLQRLSDL
FAGEDNDLGW FFDAMLQERE READQNPDGY TYYRQFALQV EDWMDIDPPR NSMLGNPLRE
ISFEQFMEQV RERLRAKLPE YEEREAQNLM LGEVTRAFEE DKHLLIEAGT GTGKSLGYLL
PAIYHSVKQD EKVMVSTHTI NLQEQLRERD VPLLTEVIPF PFRAAVFKGR QHYLCLRKFE
HKINRRDFAT PKEEVMTAAQ MIVWLAQTET GDDEELNLGN RGGDFWETVA SESDSCLGRS
CPWFRKCYYH KAKHEAGVAD VVITNHSKLF TDIQAGHQLL PGYERLVIDE AHHLEEVAGK
HLGLQMKYFT VVHTLTRLFK DSKTGQFPNL RMILQQSGSE KSAEWCSIID GLYPSLIEVK
DDWDRLAEQL FTLMPERSDA ASGDPGQFVL RLLPQKKPKA WDALAALENQ IHVTLGDVLR
KGERLLNELR EDDNDYGSES LMTDISGLLK DLGSERDALR FFIKLEDPGT VYWIEGNGNY
RSRSLQIFAV PIDVSAQLKG YFFDKKKSVV MTSATLSVDK SFQYMIEQLG LGEAAAEDKL
ITSLLPSPFN YRDQALLVIP RDFPSVKGSV GDDHFVSTLV KSLADTAIVT KGRMLVLFTS
YRMLRQVYDP LKELLATEGI TVIGQGMDSG SRTKLTRRFQ GQNASVLLGT SSFWEGVDIP
GEALTSLAIV RLPFQPPNHP LVEAKSERLQ QEKKNPFMKL SVPQAVIRFK QGFGRLVRSS
QDRGIVVVYD TRILESYYGK YFLYSLPGPK MEHMPLGQMV PRISEWLNAD EQ
//