ID A0A432LEH7_9BACI Unreviewed; 939 AA.
AC A0A432LEH7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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, ECO:0000313|EMBL:RUL55500.1};
GN ORFNames=EK386_04010 {ECO:0000313|EMBL:RUL55500.1};
OS Lysinibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2498145 {ECO:0000313|EMBL:RUL55500.1, ECO:0000313|Proteomes:UP000287910};
RN [1] {ECO:0000313|EMBL:RUL55500.1, ECO:0000313|Proteomes:UP000287910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYSU K30002 {ECO:0000313|EMBL:RUL55500.1,
RC ECO:0000313|Proteomes:UP000287910};
RA Narsing Rao M.P., Zhang H., Dong Z.-Y., Niu X.-K., Zhang K., Fang B.-Z.,
RA Kang Y.-Q., Xiao M., Li W.-J.;
RT "Lysinibacillus antri sp. nov., isolated from a cave soil.";
RL Submitted (DEC-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:RUL55500.1}.
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DR EMBL; RYYR01000004; RUL55500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432LEH7; -.
DR Proteomes; UP000287910; 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: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:0006139; P:nucleobase-containing compound metabolic process; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006935; Helicase/UvrB_N.
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 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; PF04851; ResIII; 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; 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:RUL55500.1};
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 248..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 739..924
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 459..462
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 283..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 939 AA; 107911 MW; 22BF78A8137E007B CRC64;
MMESQKYAIV DLETTGHSPA SGDRMIQIAI VIMKDWCIEK TFTSFIHPGK PIPLFIQDLT
NITDADVKDA LPFEAHADYI YELLQDSIFV AHNTDFDLSF LQAEFQRAGL PKWFGKKIDT
VELAKILFPT SLSYKLGDLA ADLNIPLDNA HRADDDARAC AHLLKKCWEE LISLPLTTLE
QLHKKSFRLK SNLSQLFFDA LQTKRRSVID TENIIYYNKI ALQQPVARSK TNEKPLQYPM
SKEEKIKLFT EKIPAFEERV QQFQMMDSIW ESLNRKSEIA IEASTGIGKT IGYLFPALIY
AIQNNRKICI STYTSHLLEQ LLINEIPKME EILGRQINVT LLKGKQNYVD IGTFEQLIKF
EDLSYDETLT VLQVLVWLSK TKTGDVTELN VSGGGQLFID KIRKSNEKSQ TIDPHFDFYD
RAIRESEEAD LIVTNHSMIL VDLVRKEPIF EKIDGWIIDE AHQFIQAAVN QDESIFTYTN
WKYLFGQIGL ATDNGIFTRF QKIALKKQRV PLQLFNQLEK KYIRVTNLFN KAMQELVHQM
KNYTIQTKQD TKHTVFLSQI ELDNGLMKSV SHAIQNWIDL AERIATTFKN DVEEIAPEHQ
LVLEQWEYWI REFKMKVAQW EELFLQGETD STTWIEIDRR NVPGSIRVLK KPINITASIH
QLFEPFRKSG AVIWTSGTLS VPNNERFIAD QLGIDKNVPI LSLQAPANYY AGAKAYIVTD
MPDIQSVSQT DYIESVALAI TRIVRTTNGR CFVLFTSQDM LRKTVELITE SELLHDYMLF
AQGVTNGSRM RLLKSFQKFS HSVLFGTNSF WEGVDVPGDG LSSVIIVRLP FSSPEEPTFK
AKSSLIQQQG RNSFTELSLP EAILRFKQGF GRLIRSSHDK GVFIVLDRRI ETKSYGVEFL
RALPQISVNK LPLQDMVLEI EHWYNSNDKD RKQVGNNEK
//
