ID A0A3M8HE84_9BACI Unreviewed; 937 AA.
AC A0A3M8HE84;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:RND00774.1};
GN ORFNames=EC501_03615 {ECO:0000313|EMBL:RND00774.1};
OS Lysinibacillus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1368476 {ECO:0000313|EMBL:RND00774.1, ECO:0000313|Proteomes:UP000279909};
RN [1] {ECO:0000313|EMBL:RND00774.1, ECO:0000313|Proteomes:UP000279909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12703 {ECO:0000313|EMBL:RND00774.1,
RC ECO:0000313|Proteomes:UP000279909};
RX PubMed=24814335; DOI=10.1099/ijs.0.061465-0;
RA Kong D., Wang Y., Zhao B., Li Y., Song J., Zhai Y., Zhang C., Wang H.,
RA Chen X., Zhao B., Ruan Z.;
RT "Lysinibacillus halotolerans sp. nov., isolated from saline-alkaline
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 64:2593-2598(2014).
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:RND00774.1}.
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DR EMBL; RHLQ01000005; RND00774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8HE84; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000279909; 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; 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; 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; 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:RND00774.1};
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:UP000279909}.
FT DOMAIN 248..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 458..461
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 937 AA; 107754 MW; 9689884A16FB4492 CRC64;
MMESQKYAIV DIETTGHSQA NGDRMIQIAI VIMKDWCIEK TFTSFIHPGK SIPLFIQDLT
NITDDDVKDA LPFEAHADTI YELIQDAIFV AHNTDFDLSF LQGEFKRVGL PKWNGKKIDT
VELAKILFPS ALSYKLGDLA AELNIPLTNA HRADDDAKAC AFLLKTCWEE LLVLPLSTLE
QMHKKSFRLK SNLSQLFFEA LQISRSTVSN EDDFIYYKKL ALKKPYATNK KIRHQIDFPA
TSAEKSTLFK KALSHFEERP KQYQMMDIIW EHLNNKSEVM IEASTGIGKT IGYLIPSIIY
AKQNNRKVCI STYTTYLLEQ LLSSEIPKVE KILGCPINVT LLKGRRNYVD VVVFEQLMKS
NDLSYDETLT TLQVLVWLSK TETGDLSELN CSGGGQLFID KIRKNAEYGK KKQLFDYYDR
AIQESEHADL IITNHSMLLA DLVRHEPVFN QIDAWIIDEA HQFVQAAVQR DQAIFSYTNW
KYLFGQIGYA SDHQLFSIFQ KIALKKQRVP LTYFQQLEKK FMQMVELFDK TIQEILYHMQ
KTSLPSKFES KQIAFVHNIL TNRETMNNFS IALQGWVDLA EQISVMFKKD IEQIAPEHQL
ILEQWDFFVR EYKMKATEWD EIFLQTDNDY TAWIEIDRRN LPGSIRVLKK PISITATIQQ
LFESIRKTSA VIWTSGTLTV PKNERFIANQ LGIDERVPMI VLQAPASYYK GAKAYVVNDM
PDIQSVSQTD YIESVALAIT RIVRATEGRC FVLFTSQDML KKTVELIQES ELLYDYMLFA
QGVTSGSRMR LLKSFQKFSH SVLFGTNSFW EGVDVPGDGL SSVVIVRLPF SAPEEPTFKA
KSISLQQQGR NAFTELSLPE AILRFKQGFG RLIRASQDKG VFVVLDRRID TKSYGVEFLR
ALPQISVNKL PLQDMVLEIE HWYNNKDGKR KQVDKNE
//
