ID A0A368WAZ2_9BACL Unreviewed; 967 AA.
AC A0A368WAZ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DFP97_102263 {ECO:0000313|EMBL:RCW51070.1};
OS Paenibacillus prosopidis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW51070.1, ECO:0000313|Proteomes:UP000252415};
RN [1] {ECO:0000313|EMBL:RCW51070.1, ECO:0000313|Proteomes:UP000252415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW51070.1,
RC ECO:0000313|Proteomes:UP000252415};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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:RCW51070.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QPJD01000002; RCW51070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368WAZ2; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000252415; 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; 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; 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 NCBIfam; TIGR00573; dnaq; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 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.
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:RCW51070.1};
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:UP000252415}.
FT DOMAIN 253..517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 275..511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 754..946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 948..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 469..472
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 288..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 967 AA; 109727 MW; A6421DCCD235C2A4 CRC64;
MKFAVLDLET TGHGSEDDIL QVGLVIVSDE LEIIDTFSSF VRPNIPIPAF ITQLTGIDDT
VVAEAPELNE VLVKLIPQLD DAVLVAHNVG FDAGFLNQAL DRSGYHMFAG RRLDTIELLR
ILYPTITTYQ LGAVSELFGI THDQHHRADS DAMATALLFI ETVKKLRKMP LLTLQRLSAL
IDDGSDLSWF IKLTQQKMEF HTVFESNEFD YFNQFALKAR EWTDEQPPRS GSGTEEPLKD
VAFDSYLADV KQRFEQKFEN YEEREAQAAM FQEVYSALNS NKHLLIEAGT GTGKSLGYLI
PALYYSIQNG KKVVVSTHTI NLQEQLRQRD LPLLEEVLPF DFKASIFKGR GNYLCLRKFE
GKVNTKDLVS PIEDTVTAAQ MVVWLGETET GDQEELNFGN KGADFWSTVE SDADSCLNRA
CPWFKRCYYH RAKHEANIAD VCITNHSMLF TDIQADHRLL PSYTHLVIDE AHHVEEVAGK
HLGMQINYFS LTQAVLRLFK DNRSGLLPAL RQKLLHEDND HQTAWIETID TVIPIFQEVK
EHWDKLFEMF YSFTSTSSDG QTDNGQAVCR LKNNLLPAGW EDAVTVEANV HTELNRVVRT
VDKMVTDIKD RIDDSAVQAI ITDLNGAVRD LTRVKDELRT FIKLELADSV FWIEASSIYR
YRSVQLYGMP VDVSAQLQKH FFDVKESIVL TSATLSVQKS FQYAEEQLGL NGYEEQGRLK
TVQLPSPFNY REQALVVIPR NFPVLKGASV DTAYLEMLVK SLADSAKETK GRMLVLFTSY
RMLKQVYEPL KDQLSEAGIG VLGQGIDSSN RTKLTRRFRQ TPESVLLGTS SFWEGVDIPG
EALICLAIVR LPFQPPNHPL AEAKAEMLQR LKQNPFMKLS IPQAVIRFKQ GFGRLVRTAQ
DKGIVIIYDT RVIDTYYGKH FLYSLPGPKI ETMHTDQMVP RMREWLEAKQ EEPMGVQAAP
SSEEEKR
//