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Database: UniProt
Entry: A0A0R1VVI7_9LACO
LinkDB: A0A0R1VVI7_9LACO
Original site: A0A0R1VVI7_9LACO 
ID   A0A0R1VVI7_9LACO        Unreviewed;       936 AA.
AC   A0A0R1VVI7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=FD16_GL001807 {ECO:0000313|EMBL:KRM09423.1};
OS   Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM09423.1, ECO:0000313|Proteomes:UP000051820};
RN   [1] {ECO:0000313|EMBL:KRM09423.1, ECO:0000313|Proteomes:UP000051820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM09423.1,
RC   ECO:0000313|Proteomes:UP000051820};
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:KRM09423.1}.
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DR   EMBL; AZGF01000042; KRM09423.1; -; Genomic_DNA.
DR   RefSeq; WP_010622153.1; NZ_BACO01000044.1.
DR   AlphaFoldDB; A0A0R1VVI7; -.
DR   STRING; 1423807.FD16_GL001807; -.
DR   PATRIC; fig|1423807.3.peg.1851; -.
DR   eggNOG; COG0847; Bacteria.
DR   eggNOG; COG1199; Bacteria.
DR   OrthoDB; 9803913at2; -.
DR   Proteomes; UP000051820; 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:KRM09423.1};
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}.
FT   DOMAIN          246..536
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   MOTIF           460..463
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT   BINDING         283..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ   SEQUENCE   936 AA;  106559 MW;  92595047529D3440 CRC64;
     MKSSKIYSVV DLETTGTSYK NGDRIIQVGC VLFSDGKMIN KFESIINPQT SIPQTIEQLT
     GITNHDVKNA PLFDDIAPTL FSLLSDTVFV AHNVGFDFPF LNAEMERAGY PSLDIKAIDT
     VTLSQILLPN EPSFRLRDLT NYLSIDHDSP HTADSDAQAT GELLVQLFDK LHQLPTTTLQ
     SIIKLRLSLP YDTDNVFKKE LEERSSTNKL PNNLNVVGGL VLQKPVNFEI VENRSSAKFP
     RSKAAKIKSY GQFLSYRPSQ AKMMNAIHNN YTHDDVKNMI VEAGTGTGKT LGYLLPAIYL
     AYPNQRIIVS TATNILQKQL SATGIGQLNN ILPFKINSVV LKGSRHYIDI AKFMHSLSVI
     EDSKPIQLVK AKLLVWLTET KSGDLDELNL NSYRLPYFSE IRHEGILSLN QQSRYYDDDF
     LVRQQKALKH ASIIVVNHAY LASHAQELGS NIDKPYLIID EAQHLSDSIL KRSRQKIDFP
     LINAAIHIMQ SLVNANHDRN LRNVFNDLPL GTYNIDLLRN DLLNLDEAFK QFEQALYRQF
     MLNVNTSREQ QIIEETIDNH KLANMLQPAN RILSDLEQSL GSLHLHFNTL FRMFEKNQIH
     WLTSDRYLVT QFQSQLLIIT QAYDTLHHFS EVLQKQLNES VFWLTVHQSS EKSNLQLSGG
     LLTTSGFLAE QIYPYFKKAT FVGATLFSSG RSRYLYDQLD IKAEKTRVKK YHSPFDFANQ
     ASLMIANDAP IISSENYRDY ISYLSQTIYQ IAKDNPRQTM ILFNSLLTIE QVYSQLHSTD
     LFLQRDILAQ GVTGNKEKIM KQFVTGSQSI LLGASSFWEG IDLPKDQLQL LIITRLPFDF
     PDAILQRAEN NWLKQNHKNP FYSSALPKTT LRIRQGIGRL IRTPDDYGVA IILDRRIHER
     KYGQSILNTL PSELPVSSIP TSEILSETKA FFKKHD
//
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