ID A0A0H4P0D3_9BACI Unreviewed; 935 AA.
AC A0A0H4P0D3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BSM4216_2311 {ECO:0000313|EMBL:AKP47551.1};
OS Bacillus smithii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP47551.1, ECO:0000313|Proteomes:UP000036353};
RN [1] {ECO:0000313|EMBL:AKP47551.1, ECO:0000313|Proteomes:UP000036353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP47551.1,
RC ECO:0000313|Proteomes:UP000036353};
RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA van Kranenburg R.;
RT "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT 4216T.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; CP012024; AKP47551.1; -; Genomic_DNA.
DR RefSeq; WP_048623550.1; NZ_CP012024.1.
DR AlphaFoldDB; A0A0H4P0D3; -.
DR STRING; 1479.BSM4216_2311; -.
DR KEGG; bsm:BSM4216_2311; -.
DR eggNOG; COG0847; Bacteria.
DR eggNOG; COG1199; Bacteria.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000036353; Chromosome.
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; IPR006935; Helicase/UvrB_N.
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; PF13307; Helicase_C_2; 1.
DR Pfam; PF04851; ResIII; 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:AKP47551.1};
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 248..511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 462..465
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 935 AA; 107907 MW; ED2C576BBFE2A34C CRC64;
MLPQRFVVVD LETTGNSPKK GDRIIQASLV IIEREQIIDQ YTTFINPETA IPAFIEELTG
IHEDLVKQAP LFSEAAQNIR PLLDHSIFVA HNTAFDLTFL QTELEKANFP LFNGQTVDTV
ELARFLYPTQ DSYKLSDMAE ELGVLHSRPH QADSDAYVTA EILLLMLKKL KSLPYVTLKK
LHQLSSHLKS DISTVIQAVL DEKEQSIESL PEDLEVYRNI ALKKKKIQKR EDLLYDVMYP
SSPNEKAEYM KEFPQFQIRE AQFEMMDCVY ETLDSSNHAF IEAGTGIGKS LAYLLPAAFY
SKQHKVPIVI STYTTVLQEQ LMNKDLVLLK AILPFSVQTA VLKGRSHYID LFQFENSLND
ETSNYDEALT KMQILVWLTE TTTGDKNELN LSSGGELYWA RIKQEDIFLN RSKNPWMEKD
FYLHARKQAQ QADIIVTNHA ILAKDLFSDQ NLISDYNQVI IDEAHHFGNV LGDQMGTEID
LRALKWMYQQ IGTMEQKQLF FQCEELLKKH GKEATIHFFE TDHDLHQIAF EMNEWMNAAS
AFFLHLAKKK PNSWNKVQIR VGEQERKMKY WKELLYSTER LYELMKMIHH SLQERLMLAK
KLETDLTLDE AAMIEKLYDL LESWKKWMND LKNVIIEGSK QPAVIWMEGD VRMPQNHLKI
KCRPAGLDRI RMEQFIDGKK SVIFTSATLS VNRSFQHFAE ELGIPEKRFR QAIFPSPFHY
EKNCKLIIPN DVPEIQDVTS EKYVEVLADY LSAVAQATNG RMLVLFTSYD MLKNTYLLMK
ESGLLEDFVL IAQGITNGSK VRLTRHFQKF EKAILFGTSS FWEGVDIPGE DLSCLVLVRL
PFTPPDDPLF QAKGEALRAE GKNPFYHSSL PQAVIRFKQG FGRLIRTERD RGIIIVFDRR
ITTARYGKAF IQSIPKVPIL HASLPEVIQV IEDWL
//
