ID A0A0R1UL30_9LACO Unreviewed; 939 AA.
AC A0A0R1UL30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=FC21_GL001489 {ECO:0000313|EMBL:KRL94017.1};
OS Limosilactobacillus equigenerosi DSM 18793 = JCM 14505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL94017.1, ECO:0000313|Proteomes:UP000051084};
RN [1] {ECO:0000313|EMBL:KRL94017.1, ECO:0000313|Proteomes:UP000051084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL94017.1,
RC ECO:0000313|Proteomes:UP000051084};
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:KRL94017.1}.
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DR EMBL; AZGC01000039; KRL94017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1UL30; -.
DR STRING; 417373.GCA_001570685_00580; -.
DR PATRIC; fig|1423742.4.peg.1543; -.
DR Proteomes; UP000051084; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_02206,
KW ECO:0000256|RuleBase:RU364106}; Helicase {ECO:0000313|EMBL:KRL94017.1};
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:UP000051084}.
FT DOMAIN 253..537
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT COILED 490..543
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 468..471
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 939 AA; 105439 MW; 24C86C3606096195 CRC64;
MMGKQAATTS PVYAIVDLET TGTNWKNQAR IIQIGCVLVQ DNQIIHQFET KVNPGVAIPS
AVQQLTGIHQ RDLQSAPTFD ELAPSICAML TDTTFVAHNV NFDFSFLNME LVKAGYPELT
IPAIDTVTLS QILMPTAPSF RLRDLTSYLG IEHDNPHSAS SDAEATAILL MDLMRRLHEL
PTLTLTKLAE LNLKLPEQTA VMFARELAMR EAAPVNLDNA HYVSNGIVLH KIRPRTVEHP
HRKFPYPRTK KQKATFFGDK YQYRPVQAKL MNSIYNQFRQ PDGSQQLVIE AGTGTGKTLG
YLVPLSYLAY PHGQIIISTV TNVLQKQLAQ VVNEQLGELL PFQLQAVIVK GNQHYIHLGK
YVRSLSMNED GANVQLLKAR LLVWLTQTTT GDLDELNLNS MRSPYFATIQ HHGLHTVTPD
EPFYRDDFLI RRQQALQTAN IVITNHAYLV EHAAELTNDQ QASYLVVDEA QHLSHSVMRH
SRLTIEFAKL STALNQLKNL VSQRDEHNLR AVFAKLPLGS YNIELLQTDL GAVEQALEEF
QTALLNLLPA SQATTGYVEA MVPVAAIAEI LDFTQPLMIG LEQALASVQL HFNALQRLFD
GRRDSWLSLD RYQMNQFSSH FAVLAQANDE LHRLANGVDD EAAAFWVSYI EGNELGNLKL
SGGLLAQNHY LSTHVYPHFK AMVFTGATLF TSQRSAYLYQ QLDLDPETVK TKHFGSPFDY
EHQMELLIAS DAVEPSLESE YLDYLATTIA EITTQNPCQT MILFNSLVTI EQVYSRLRKT
SLFDQRDILA QGINGNRDKL LKQFATGTDS VLLGAASFWE GIDLPEDQLQ LLIVTRLPFD
SPDDVLVKAQ HEHLKRQGKS PFYQVDLPQM IMRMRQGIGR LLRTDRDYGT VVILDPRLIT
RRYGKSVLKM LPQGMPVAAI PTSQLAGRVK KFLKTHGAV
//
