ID A0A2T4UAC0_9BACI Unreviewed; 931 AA.
AC A0A2T4UAC0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C6Y45_00060 {ECO:0000313|EMBL:PTL40340.1};
OS Alkalicoccus saliphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL40340.1, ECO:0000313|Proteomes:UP000240509};
RN [1] {ECO:0000313|EMBL:PTL40340.1, ECO:0000313|Proteomes:UP000240509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6AG {ECO:0000313|EMBL:PTL40340.1,
RC ECO:0000313|Proteomes:UP000240509};
RA Zhao B.;
RT "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PTL40340.1}.
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DR EMBL; PZJJ01000001; PTL40340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4UAC0; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000240509; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PTL40340.1};
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 245..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 267..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT MOTIF 460..463
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 280..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 931 AA; 105817 MW; 114ABA9CCEF18F45 CRC64;
MSRYVVLDLE TTGVSYAEGD RIIQLAYTVI EEKKIVKTFN TLINSETTIP AFVQQLTQIQ
TEDLAKAPSF EEIVPELMED LNNSCFVAHN VDFDLHFLNE TLEDTGYTPY EGPVLDTVEL
SRIAFPSESG YRLSELAENL SLHHVVPHQA DSDAYATAEL FLKISEVFRK LPRPALKHLL
GIEHMLKSSL RPLLEEWFEQ AEDAAGELEV YRGIALRKIN YEAAENENIE ADFNEVFADF
QTGETISKVM PGFIRRSGQE EMINFVHQIF TGSKIGLVEA GTGTGKTLAY LLPAAYYAAV
YKEKVVISTE TIQLQEQLLK KEVPLVEKLL PFPVKPALLK GRTHYVCLQK VENLLDLSFQ
ESYERMVSKA QIVVWLTITG TGDVEELNLA DASDRFLREV SSDIQSCAGP DCPWFSRCFY
QRAKKAAKAA DVVITNHAML LSDIVHESQI LPSYSSVIID EAHHLEEAAT RHFGTQLDYA
SMAQLLNDFT TRGQDNVLEP WLSLYTPEMW KRCKEKIQQA REEWNDLFLS IYSYADKGAG
RGETGDVSKV IVRDESWNYV LEAAHRFHAV FTEAVDELKK IELEISSDTS TGPAYKNEQT
ALDRYIHEMD DLHRKFMDLI THQQEDNVYW MERALKGPKQ SITIFSSPTE VSQLLADRFF
QKKKRVILTS ATLTVNQSFN FVIRQLGLED FEVETKVVAS PFNWSEQVAL MIPNDIPLIQ
EAGEDAYIHS IAQAIYQTAE VTEGKMLVLF TSYDMLRKTY HLVSNLLDDS YMLIGQGIQS
KSRTKLVKMF QQFDRTILFG TSSFWEGVDI PGEDLSVIVM ARLPFSPPSD PVFKAKSDKL
KQEGASPFIK LALPQAVLRF KQGFGRLIRR ETDRGIVIVL DRRIDTARYG KQFVKSLPDM
PVHRGSIYDL ETEIDAWLHK PLKESVYDGD H
//
