ID A0A1I0YX54_9BACL Unreviewed; 1049 AA.
AC A0A1I0YX54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05216312_104231 {ECO:0000313|EMBL:SFB17627.1};
OS Cohnella sp. OV330.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB17627.1, ECO:0000313|Proteomes:UP000198686};
RN [1] {ECO:0000313|EMBL:SFB17627.1, ECO:0000313|Proteomes:UP000198686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV330 {ECO:0000313|EMBL:SFB17627.1,
RC ECO:0000313|Proteomes:UP000198686};
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; FOKE01000004; SFB17627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0YX54; -.
DR Proteomes; UP000198686; 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:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 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; PS51192; HELICASE_ATP_BIND_1; 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:SFB17627.1};
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:UP000198686}.
FT DOMAIN 257..554
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 279..540
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..949
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 955..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 473..476
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT COMPBIAS 978..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 1049 AA; 115782 MW; A3FE83E67EE2AC44 CRC64;
MKFAVLDFET TGTSSQHDEI IQIGIAVVDD TGTVSSVYQS LVKPSRAIPS FITTLTGIAD
ADVADAPAIE DAIAEMVPLL HDAVLVAHNA GFDAAFLQAA LDKSGYLPFS GRVLDTVELA
RLVFPFLPSY RLTAITHGLG IAHDRPHQAD SDALATAEVL TACIGRLRAL PTLTLERLCE
LTDGERSDLG WLLTSLRAER DTTWFEEPDG YQYYRQFAMR IADWTDDDEG REAQRLQAER
MLSGMPFETY LDTVADRMKE LFPGYEPREG QRIMYDEVHQ ALADDSHLLV EAGTGTGKSL
GYLLPSLYYG LKENKKIVVT THTIQLQEQL RQRDLPLLQD VLPVPFKAAV FKGRSNYMCL
RKFEQQMQTP AFALSREEAV ARGQLAVWLS ETERGEAEEL NLGSRSKEEW NAVASDADSC
LNRQCPWFRK CFYHRARQDA LKADLVITNH AMVFTDMRAE HRLLPAYDRL IVDEAHHMEE
VASNHLGRRI GYGALPSALA RLAKDARTGQ LPSLISQLTG TAESASGTWA EKLEELLPRV
QELRESWEQW TDRLFGLLAS GAAADETGGL SYRLKPDALP RDWESIRVDG DNVVLRLSDL
VRPLEKLLAE IRDRSEDIAL QSLLTDMNGS VKELSGVRSD LQSFVSMSET ECVYWIEGHT
QYKSRSLWMY IVPADVSGLL KDGLFGQKES VVLTSATLTV DKSFQYVKEQ LGLDEAEQQG
RLRTAQLPSP FNYRQQALLL IPRDFPSIKG RDGEAAFLQA LTASLAEVAT ETRGRMLVLF
TSHKMLKTVY EPLKSALAPV DIQVLGQGMD GSSRSRLTSQ FMEQPRSVLL GTSSFWEGVD
LPGDALTCLA IVRLPFQPPN HPVTEAKSER LTAQRKNPFM KLSLPQAVIK FKQGFGRLVR
TASDKGIVIL YDTRVIDTSY GKYFLYSLPG PKMEHLPLAG LVPRVREWLH PAHAAGAEAA
ADAERPPSAA PAADASPTPD TEPAPVPDTE PMPDASGRPA SGEAGQTASV PSGEAGAPAE
PAPEKVKVKR TRAKKPKQET DAREGGVSS
//