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Database: UniProt
Entry: A0A368WAZ2_9BACL
LinkDB: A0A368WAZ2_9BACL
Original site: A0A368WAZ2_9BACL 
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}.
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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
//
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