ID A0A0R1M7U5_9LACO Unreviewed; 930 AA.
AC A0A0R1M7U5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=FD46_GL001343 {ECO:0000313|EMBL:KRL04223.1};
OS Liquorilactobacillus oeni DSM 19972.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL04223.1, ECO:0000313|Proteomes:UP000051686};
RN [1] {ECO:0000313|EMBL:KRL04223.1, ECO:0000313|Proteomes:UP000051686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL04223.1,
RC ECO:0000313|Proteomes:UP000051686};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRL04223.1}.
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DR EMBL; AZEH01000039; KRL04223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1M7U5; -.
DR STRING; 1423777.FD46_GL001343; -.
DR PATRIC; fig|1423777.3.peg.1388; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000051686; 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; 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: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; 2.
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}; Helicase {ECO:0000313|EMBL:KRL04223.1};
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:UP000051686}.
FT DOMAIN 245..533
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 457..460
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 282..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 930 AA; 106155 MW; B2B5B012405EE1C5 CRC64;
MSPAPIYAVV DIETTGTAMD GSNRIIQFSC VLVKDNKIAN IFNTMVNPLM KIPEEVQQLT
GITPKDVRKA PLFDDLAGTI YELLQGTVFV AHNINFDYRF LNTELERCGY PSLEIDGIDT
VQLSQILLPT LPSYRLAYLG SYLNIVHSHP HRADSDASVT AQLLLFLLKQ IENLPIQLLE
QAVRFRSSLL FQTGECFLNA LRLKQKNANV VPDYLENVSG MLLRRIEKNI KFDQSSKFPR
TDAEKKKLFL NFLNWRKAQS EMMNRVFAIL SQSGSERAIL EAPTGLGKTL GYMIPAAYAS
QAGKGTVIST ATTALQTQLL EQVIPLMRQI LPFEFEVAVF KGSQNYIDLG KFARTLKQVQ
NSQTRLLQLR LLVWLTITKT GDLTELHLTK YQNPLFDEIR HHGPASLDSS DTFYSVDFVH
RQQLLEKNAD LIITNHAYLV RHAAELGGLK KRDLIVDEAQ HLGEIALKNN RDVIDFDELK
ILCDTLLVKM ESKVSFSLKN LSAQHFLTIA ESKEIIKKVQ LIDQRIPKLR DKLYKRFVNE
TLFTTGFYEE TLRLDKFFGF VKENLGDIKQ ISKAAFSLQR IFKQLTIRFS NFKAENRIDR
TAEEFLYDFC SQLQGLIESL KTWERLSLDE LEELSTEILV SISLPLHQPG AHLRLRFSLF
RTKNFLEPNV YANFKHVLFV GASLVLPSSP YYMLDQLDLA HETQVISFKG IFDYRKQALA
LLVADAPDVS QNASEYTEYI GKTLENIILH NKRRMMVLFN SLTMIQKIYD HLKETGITEK
RLVLAQGITG SNEKVVKSFK LAESAILLGS GAFWEGIDLP KDKLELLVIT RLPFQSPDTL
LNRAKYSLIE KQGLNSFTEI ALPETMMRLK QGFGRLIRTP EDKGVLIVLD SRVISRTYGS
RLRTAFPEEL PVRIVETKEL ETYLHSFWQK
//
