ID A0A0R2LB01_9LACO Unreviewed; 935 AA.
AC A0A0R2LB01;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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, ECO:0000313|EMBL:GEK27708.1};
GN ORFNames=IV55_GL000824 {ECO:0000313|EMBL:KRN96949.1}, LSI01_00190
GN {ECO:0000313|EMBL:GEK27708.1};
OS Furfurilactobacillus siliginis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN96949.1, ECO:0000313|Proteomes:UP000051139};
RN [1] {ECO:0000313|EMBL:KRN96949.1, ECO:0000313|Proteomes:UP000051139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN96949.1,
RC ECO:0000313|Proteomes:UP000051139};
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).
RN [2] {ECO:0000313|EMBL:GEK27708.1, ECO:0000313|Proteomes:UP000321429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101315 {ECO:0000313|EMBL:GEK27708.1,
RC ECO:0000313|Proteomes:UP000321429};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus siliginis NBRC 101315.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:KRN96949.1}.
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DR EMBL; BJUD01000001; GEK27708.1; -; Genomic_DNA.
DR EMBL; JQCB01000002; KRN96949.1; -; Genomic_DNA.
DR RefSeq; WP_057808848.1; NZ_JQCB01000002.1.
DR AlphaFoldDB; A0A0R2LB01; -.
DR STRING; 348151.IV55_GL000824; -.
DR PATRIC; fig|348151.3.peg.849; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000051139; Unassembled WGS sequence.
DR Proteomes; UP000321429; 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; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
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; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR PANTHER; PTHR30231:SF4; PROTEIN NEN2; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 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:KRN96949.1};
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:UP000051139}.
FT DOMAIN 247..522
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 461..464
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 284..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 935 AA; 104328 MW; 49C054B6B65D9262 CRC64;
MNKDTTYAVV DIETTGTSVK DGDRVIQIGC AFVKHGKVIN HYSTKINPGR QIPANITHLT
SITNREVAKA PYFDDVAGAL YAMLQGTVFV AHNVNFDFPF LNAEFSRVGY PPLQIEAIDT
VTLTQILFPT LTSFRLRDLS AHFQIEHDQP HTADSDADAT AVLLLKLLDQ VATLPINTLR
QLVNLNLSLP ADTTKVFDVA LAAARKQPAQ LPAGQYVRSR LVLHEATPPQ AIDLGQPRAY
PKSKAAKLKA WGDQVEWRDS QAKMMNHIFN NYSHEDTKNL IIEAPTGIGK TLGYAVPFAF
LSQTGKATVI STQTTLLQEQ FMTDTLPKLR AMVPFAINAV AVKGSQHYLD LSRFAATLTV
PEHSQQSQFL KARILVWLLQ TQTGDLDELH LNSYRAQLFE EICHRGLQSL NPKDPFYEDD
YLRRMDQRIR QANMVVVNHA YLTQHAAQLD TLLGRPYLLV DEAQHLPTVA TSDHRNTVKF
HELASALHHA QATIFNQHEH HLTEMFSEDG TATAALQQLA SVLLKLDADL DQFEQGLYRQ
FLLAAQVNSH GQRILEQLVD NEQLQKLLQA GNPIFSALIT EADLLPNALH KVQTRFEKQQ
NKWLNSDVAL MHEFTQTVAD VQTKLAQLAQ FADELGDAET TNVYWLRQNQ YGDSASLELS
GGLLMATGWL KEHVYAHFQL PTFTGATLFT STRANYLMTQ LDLDKATTVT KRLPERFNYE
QQARLFVATD APVANLRKPD VQYRYWADTI AKLAKKTHRQ TLVLFNSLAA VSGVYTALTH
GLVNDNQTVF AQGETGSREK NLKRFSTESN GILLGAASYW EGIDLPKDAL ELVIITKLPF
DSPTDLLVAA TNARLEAAGH NAFYASALPK ATLRLRQGIG RLIRTPTDRG VIVVLDSRLV
NKRYGGTMQK ALPKGLTVIS KPTAEIITQT NNFFR
//
