ID F9HIC4_9STRE Unreviewed; 823 AA.
AC F9HIC4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=HMPREF9182_1971 {ECO:0000313|EMBL:EGP66976.1};
OS Streptococcus sp. oral taxon 056 str. F0418.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP66976.1, ECO:0000313|Proteomes:UP000004514};
RN [1] {ECO:0000313|Proteomes:UP000004514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL Submitted (MAY-2011) 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:EGP66976.1}.
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DR EMBL; AFQU01000001; EGP66976.1; -; Genomic_DNA.
DR RefSeq; WP_009754568.1; NZ_AFQU01000001.1.
DR AlphaFoldDB; F9HIC4; -.
DR eggNOG; COG1199; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR Proteomes; UP000004514; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR006310; DinG.
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; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR PANTHER; PTHR30231:SF41; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR Pfam; PF00270; DEAD; 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:EGP66976.1};
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 235..494
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 257..494
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 626..810
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 441..444
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 823 AA; 95446 MW; 26B775B4B65D22B8 CRC64;
MKRKNVKYAV VDLEATGTGS SAKIIQVGIV ILENGQISQT YQTDVNPHEV LDEHIKQLTG
LSDQRLSQAP DFSQVAREIY ELIEDAVFVA HNVKFDANLL AESLFWEGYD LLSPRVDTVE
LAQVFFPTYE KYGLSSICEL LEIPLEQAHT AISDAKATAL LFLKIQEKIQ SLPKSLLERL
LDLSDNLIYE SRLVLEDCFS QMSQESTGDL LDCHGIYLRK KRKIAKEKHL SADFTKNLSL
LVLEERSEQE KFATMVEQAI ENHHPSFLQA QAGLGKTYGY LLPLLAKTKE QIVVSVPTKI
LQEQIVSGEG KAIKEVFQVS FHSLKSPHSY IKLDTFYQSL TRMDDHRLLN RCKMQLLVWL
TETETGDLEE IRQAYRYQAY FEELAHDGQI SKKSLFYGYD FWQLNQENAR ASRVLVTNHA
YLLTRLEDDK SLIEGKTLVV DEAQRLFLTL DNFSQKSIRV TQLLQEIQQE ISQATSLLNR
RLLESIQFEL SQAVEQFHRG SQREIKEDLI QKLRQDLSEL PAPYLQELRE LLDQKYEQFW
LEDDHFEQNR VTSLHGARIS LVNFQDFLPE KVRLFFISAT LEISRKVSLA QLLGFQNVRF
YHLPPQDYHQ QKIWVDKDFP DLIGLPLTQH AQLIVERIER LFHTKLPILV LFTSKELLLE
VSERLSLPHL AQYKNGDATN IKRRFDKGEV TVLLGTGSFW EGTDFSTQNK MIQIITRLPF
DNPQNIFTQK MNRQLRQNGQ NPFYDYSLPV AILRLKQAFG RTMRHHNQRS AVLILDNRVY
TKRYSRQIRE ALAESTPVEQ ASFKQIQDEI TNFLKKKTSK KKK
//