ID A0A1I6DM37_9FIRM Unreviewed; 949 AA.
AC A0A1I6DM37;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05660706_11360 {ECO:0000313|EMBL:SFR06437.1};
OS Desulfoscipio geothermicus DSM 3669.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=1121426 {ECO:0000313|EMBL:SFR06437.1, ECO:0000313|Proteomes:UP000199584};
RN [1] {ECO:0000313|Proteomes:UP000199584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3669 {ECO:0000313|Proteomes:UP000199584};
RA Varghese N., Submissions S.;
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 -!- 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}.
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DR EMBL; FOYM01000013; SFR06437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6DM37; -.
DR STRING; 39060.SAMN05660706_11360; -.
DR Proteomes; UP000199584; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; 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; 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; IPR006554; Helicase-like_DEXD_c2.
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; PF00270; DEAD; 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; SM00488; DEXDc2; 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.
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:SFR06437.1};
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:UP000199584}.
FT DOMAIN 252..548
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 468..471
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 949 AA; 107722 MW; 036051142044ACF3 CRC64;
MHRGSEILQN FVVCDLETTG FDHEQDKIIE IALVKVIDGE IIETFDTLIN PHTQIPLKIK
RLTGITGEQL ASSPTLDQVL PQIQRFLQNV PLVGHNIAFD RSFLSANIDY LPFTFYLDTL
ELARITLPDI PGHSLASLVQ YLQLPQRPQH RALNDALSTT ELLFALLQKV SSFEIGVLHR
LVSLLRQGRS PLTEVVENVS KNKIQNFSWE KISRRIPVKE PVSEPEPESL EMPKHINEPG
FQLDYLLGVD SPLAGLMPNY SYRPEQVRMA QTVKDTLEGQ KILLVEAGTG TGKSIAYLLP
ALLWTLQNEQ RAVIATNTIN LQEQIWHKDI PLLQRLLNLP FKGALLKGRS NYLCLHRFIS
LLNNSAGLTR GEALLTARVL VWLQNTDSGD KTELNLFGPD NESWLQLCSE SESCLGNGCR
WSSGYCFVNR ARRRAEDAHL VIINHSLLFS DIVSDIKILP PHGALIIDEA HNIDETAYKH
LGKKITRTEI IQWLSLAGKN LKKLTELAPP QDGQRWLAAV NKAEEAKNKL MEKVNVFFKS
LVQHLKTNNR GSYSQTRVRL HREPNTLENI EADYQNLLFH MRHFITNLHS ITQWLEIWTV
SNDSLTDILQ DINNNITTGT GYLKDIDFII KAPEDNYVCW VEVSALPGYD KKYNCDLHAT
PIDISEILHE RLFDTSRAII LTSATMTVNN RFDHFIKQCG LDRMPKEMVN AGIIQSPFNY
DQQCLLCIAD NVPNFNETDS QVYLDTLADT IFSLALETEG RTLVLFTSHK LLKEAYLKTK
PAFDEVDICL LGHNIDGSRT KLIEQFTMNR RSVLFGAFSF WEGVDIPGEA LVNVIIVKLP
FAPPDDPVLE ARNEKIAALG YNGFYTLSLP SAVIRFKQGF GRLIRSERDR GVVVILDKRI
LEKRYGKIFL NSLPVKSHLR GDVALIRKKL SYWILHAHSH PPLNNIIYR
//
