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Database: UniProt
Entry: A0A1H9P5G2_9BACI
LinkDB: A0A1H9P5G2_9BACI
Original site: A0A1H9P5G2_9BACI 
ID   A0A1H9P5G2_9BACI        Unreviewed;       939 AA.
AC   A0A1H9P5G2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN05518684_101153 {ECO:0000313|EMBL:SER43428.1};
OS   Salipaludibacillus aurantiacus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=1601833 {ECO:0000313|EMBL:SER43428.1, ECO:0000313|Proteomes:UP000198571};
RN   [1] {ECO:0000313|EMBL:SER43428.1, ECO:0000313|Proteomes:UP000198571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S9 {ECO:0000313|EMBL:SER43428.1,
RC   ECO:0000313|Proteomes:UP000198571};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOGT01000001; SER43428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9P5G2; -.
DR   STRING; 1601833.SAMN05518684_101153; -.
DR   Proteomes; UP000198571; 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:UniProtKB-KW.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; PF06733; DEAD_2; 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.
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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SER43428.1};
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}.
FT   DOMAIN          251..526
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   DOMAIN          273..489
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   MOTIF           466..469
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   939 AA;  107088 MW;  02981F1346F4C48F CRC64;
     MNRFVVLDVE TTGVSFSRGD RIIQLAYSVV ENEQIIHRYS TYINPERSIP PFIKSLTNIH
     EKHVSEAPVF SEIAPGLLEE LEGAYFVAHN VEFDLKFIND ELVNAGYVPF EGPVIDTVEL
     SRIVFPTQDS FKLSQLTESF EMDHFEPHRA DSDAEATALL LIEIFQRLSA LPLLTLQQLE
     KLQGRLKSDT GSILREWIEL SKSSPEDFPE IDAFRGLAVK EPAGYSGEVT AGAVPESVTD
     FLHSTLENVN FMKEKIPSYE RREGQMDMIR FIDEVFKNDS IGLIEAGTGT GKTLGYLIPA
     ALYSRTESGP VVISTETVQL QDQIVSKELP ALQQLLPFKI KAALLKGRSH YLCLQKFENI
     LINDPIDSYD RTLSKAQILV WLTETDTGDV EELSLASGNS RFWEEVASDP RSCSTPQCPW
     FSRCFYQRAR KQSKKADLII TNHSLLFTDM AAEHQILPSY STLIVDEAHH LEDSATRQFG
     GKLDYLTMTQ LLNDLVREKE GWVPENIWRL MGSGLKENSK EFFELSGQFK QEWNDLFLLL
     NQYAGKGMAG KNETGRLSKI INSADKFWDT VRETAGRCDN LFKALLKKLN YIIRETDLLL
     EDKETSDHHQ REAEWMAALL FKIEEQYLSF HELILNHEDS SVYWLELETK GPKQSIAVHG
     SPIQIADKLA DNFFAKKDRV ILTSATLTVN NQFKYMIHRL GLEDFQVETK QVDSPFSWDK
     QVSFMVPEDM PLIQEAGEEA YIEAAALQIY RIAHVTKGKM LVLFTSYDML RKTYFQLKKM
     LDESFMLIAQ GIQTKSRSKL TKNFQQFDQA ILFGTSSFWE GVDIPGSDLS AIVMARLPFS
     PPNDPVFKKR SDTLKEEGHS PFMKLALPQA VIRFKQGFGR LIRSSTDRGI VVVLDRRLTT
     TRYGKSFTRS LPDIPMIEEP MSEMEERIAD WFNQPLIDK
//
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