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Database: UniProt
Entry: F9HIC4_9STRE
LinkDB: F9HIC4_9STRE
Original site: F9HIC4_9STRE 
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
//
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