ID Q2Z0D2_9BACT Unreviewed; 965 AA.
AC Q2Z0D2;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=3'-5' exonuclease DinG {ECO:0000256|HAMAP-Rule:MF_02206};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_02206};
GN Name=dinG {ECO:0000256|HAMAP-Rule:MF_02206,
GN ECO:0000313|EMBL:CAI78468.1};
OS uncultured Latescibacteria bacterium.
OC Bacteria; Candidatus Latescibacteria; environmental samples.
OX NCBI_TaxID=199737 {ECO:0000313|EMBL:CAI78468.1};
RN [1] {ECO:0000313|EMBL:CAI78468.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309397; DOI=10.1111/j.1462-2920.2005.00918.x;
RA Nesbo C.L., Boucher Y., Dlutek M., Doolittle F.W.;
RT "Lateral gene transfer and phylogenetic assignment of environmental fosmid
RT clones.";
RL Environ. Microbiol. 7:2011-2026(2005).
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206}.
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}.
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DR EMBL; AJ937760; CAI78468.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2Z0D2; -.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; 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}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_02206};
KW Helicase {ECO:0000313|EMBL:CAI78468.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02206};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_02206};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02206}.
FT DOMAIN 277..549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 299..568
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..493
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 965 AA; 105140 MW; C51616E6F91971CC CRC64;
MRHQEDDRRP EGRGRMTEAG TNAYPRTFVG LDLETTGVDS RVDRIIEVGA VRVVDGRVAD
TFESFVNPGC PIPSDIVHLT GISDADVAGA PTIDEVLPRI IEFIGGSPIV AHHAPFDTGF
LDEAAGGRPG LLVGRGGVFD TLPLTRALLP RLPNHRLATA ARFFDIPTGR SHRATDDARA
VSDLFLALLG VLDQIGATVL DRMYRLADTA TRTLIEAARE RAEATIDPLA VPDHGEKERE
LQRLDTARGL GVPRTPAEEI REIDLDEIES LFGTDGPIGR ELRGYEVREQ QLQMLRAVGD
SLMGGVHLVV EAGTGVGKSL AYLTPAVYFA VENGERVVVS TNTKNLQEQL FLKDVPFLER
VLDIDFSVAL LKGRGNYICQ ARWRQVLEKG LSSSERSQLL PVALWEQETR SGDISENAAF
RQYGYVWNRI SADGGPCLGQ KCPMRETCYL LKARKASQAA HLVIVNHSLL FSDTEADNRI
LGEYSYLICD EAHNMEQVAT EHLGKRSNVW RARAMLDNLY RNEGGPSGDL GEVMGALSGT
DGALLESATA GVERLASDVT AASAAVETFF TALAARHIDL NDGREVEFGK LRYRQEAPVS
ALLEEELAGV LAALSTVARG AESVADLITD SELDRAESFV QNLTFHAARV REFAADLEYV
AEAADPGSVF WLDVRTFRDV FECELRSAPV SVAEMMGDFL YSRVDSLIAT SATMTVDGSF
DFVMERMGLD LIPDWKVLTL DVGSPYDYDA QSIAVVAGYL PQPSSSGFNQ TVSRLVVKLA
ERAQGGTLVL FTARSALDAV FKSVLDPLTS RGKLVLAQGH GGASSALLEQ FAREVDSVLL
ATSSFWEGVD VPGRSLEQLV IVKLPFPVPR DPVVEAHCER YEADGENSFG RYMIPRTAIR
LRQGFGRLIR STTDSGAVIF LDSRLSTRAY GERLLEQLPT RTVIADSEAG LMTALAGIHA
DRSVV
//
