ID A0A1H9WHJ3_9BACI Unreviewed; 918 AA.
AC A0A1H9WHJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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};
GN ORFNames=SAMN05518872_10834 {ECO:0000313|EMBL:SES33396.1};
OS Psychrobacillus sp. OK032.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1884358 {ECO:0000313|EMBL:SES33396.1, ECO:0000313|Proteomes:UP000199084};
RN [1] {ECO:0000313|EMBL:SES33396.1, ECO:0000313|Proteomes:UP000199084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK032 {ECO:0000313|EMBL:SES33396.1,
RC ECO:0000313|Proteomes:UP000199084};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGY01000008; SES33396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9WHJ3; -.
DR STRING; 1884358.SAMN05518872_10834; -.
DR Proteomes; UP000199084; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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; SM00487; DEXDc; 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; PS51193; HELICASE_ATP_BIND_2; 1.
DR PROSITE; PS51194; HELICASE_CTER; 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:SES33396.1};
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 246..519
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 729..880
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 457..460
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 918 AA; 105120 MW; B15852CA881B5936 CRC64;
MENHKYAVVD IETTGHSSTS GDRIIQLAIV FIENSKIVDT FTTFINPEKP IPFFIQDLTK
IKDKDVEHAP LFETIGSNVL DLLQDHIFVA HNIHFDLPFL QNELKRVGLP KLVCKTMDTV
EFAKLMFPNL YSYKLQDIAT ELHIPLDVAH RADDDALATA YLLLKCIERL ESLPLKTIEL
LHKRSFQLKS NLSIIFFDVL AEKRKQYNAT NYPMYRGIPL KEIEKEHAGI DTSISYPKTK
ELKMALFQKG LTHFEERQGQ FAFMDEIQHS LEKKAETVCE AETGIGKTLG YLLPATIYGL
GRQKPVIIST YTTHLIDQLV LEEIPKLNRV LGTSIRVAKL KGMHHYIDLY RFWQHVQLDD
ESYDETFTIM QMLVWLTITD EGDLTELNVS GGGQLFVDKI RKTSLSKILE EREMDFYERA
LRKSEQCDIL VTNHAMIMAD REREKKLLSH GCVTIIDEAH QVIHASMSRK ERIFSYTTWK
YVLGQFGTLD TDQLLSKLTL LNIPLALRIR LEKQYVDVVE SFDQAISSII HSIPSTKGHS
KSTKRMATLE DLNLNPAIFR EVATLLQTYI LSAKSILATY AKNKLDDPAT VLLNEWEYWI
RELEIKVSEW DEIFLIDEAV EAKWLEIDTR SIPGSLTIIK RPLNYQKDIK EAVDPLRLSG
AVIWTSGTLT VPSNRHFITS QLGLSTSIPI HQYRAAYDYY NGAELLIMED MPDIKQVSQS
DYIEAVAEAI VQTVLITEGR CFVLFTSQDM LRKTVEIIQD TNLLEDYMLF AQGMTSGSRM
RLLKSFQRFS KSVLFGTNSF WEGVDVPGDA LSVIIMVRLP FSSPDDPLYK KRAELLSVNG
QNPFTAYSLP EAVLRFRQGF GRLIRSSNDK GVFIVLDRRI ETKSYGSDFL QAIPNIPIKK
VTLENMVLEL ENWYTNEG
//
