ID A0A098F0F0_9BACI Unreviewed; 928 AA.
AC A0A098F0F0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BN1002_02498 {ECO:0000313|EMBL:CEG27628.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG27628.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG27628.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG27628.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02206}.
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DR EMBL; CCXR01000001; CEG27628.1; -; Genomic_DNA.
DR RefSeq; WP_048825238.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098F0F0; -.
DR STRING; 1476857.BN1002_02498; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000042335; 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; 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; 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; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 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:CEG27628.1};
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:UP000042335}.
FT DOMAIN 250..512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT BINDING 285..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 928 AA; 103927 MW; AF8E172B21740388 CRC64;
MAKKFVVVDL ETTGNSPKKG DRIIQIAAVV IEGGKISDTY TSLLNPLQPI PPFISELTGL
SDDDVSEAPL FSEIAPKISS LLKDAYFVAH NVLFDLGFLQ EELILCGEES FAGPVLDTVE
MARFLKPSAD SYKLADLAAG EGLSHDRPHQ ADSDATVTAE LFLLFLDKLK KLPEKTLGQL
ALLSEGLKSD IHLLLHSIGS IKVTDRGTLP DSIVYVNGLA IKKQERQMGD KTSTEASLEY
PWSDSDKQKF FSQSPYRLVK REGQFEMMDE VFHSFQNGTH ALIEAGTGIG KSLGYLFPAV
YFSRLHAVRV IISTYTIQLQ EQLLAKEIPL LSGMVPFSFK SAMLKGKNNY ISLSRFAKSL
EEENDNYDIV LAKMQILIWL LDTDHGDRDE LNLSSGGQLY WNTIRNEKGI LREQDPWHEH
DFYNKARKKA DEADILITNH SLLLSDVESG GNVLPAYSFA ILDEGHHFEK ASAGHLGIRL
DYLSIRLALN QFGLYEQRQL FYKTVSALSQ FQNGKKMQIQ HINDLFADTL YDLDEFFKIS
IAYASKAAKK NSSKKLKAVI YRHEHNREWQ ALNNASERLI FRLRDLSGIV QSMYDKAIVL
PGRSSATLGT ELAAYKEELE GLRAKFTGVF TSGDEFVKWV ETDLRVPQNA TEIFAMPVTV
SETLSKKFFS LKKSVVLTSA TLTVNQSFSY MIEALGLEPR YVNTISIPSP FNYKDNVKLF
ISSDVPEINS VSQDSYIAEV SARIISICEA AKGRLLVLFT SHDMLKKTFE LVKESGLLPE
YALIAQGITG GSRSRLTRNF QKYDKAVLFG TNSFWEGVDI PGEGLSCLIV VRLPFSSPDE
PLTKAKCEQI EKNGGRPFSE YSLPEAVLRF KQGFGRLIRT DEDRGVIVIF DKRIGASSYG
KVFLQSIPEI PIKKADIEEL VNEIEKWL
//
