ID A4J5B5_DESRM Unreviewed; 930 AA.
AC A4J5B5;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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 OrderedLocusNames=Dred_1743 {ECO:0000313|EMBL:ABO50268.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50268.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50268.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50268.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exonuclease. {ECO:0000256|HAMAP-Rule:MF_02206,
CC ECO:0000256|RuleBase:RU364106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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; CP000612; ABO50268.1; -; Genomic_DNA.
DR RefSeq; WP_011878082.1; NC_009253.1.
DR AlphaFoldDB; A4J5B5; -.
DR STRING; 349161.Dred_1743; -.
DR KEGG; drm:Dred_1743; -.
DR eggNOG; COG1199; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_012117_1_0_9; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; PF00270; DEAD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 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.
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:0000256|ARBA:ARBA00022806};
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}; Nucleotidyltransferase {ECO:0000313|EMBL:ABO50268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Transferase {ECO:0000313|EMBL:ABO50268.1}.
FT DOMAIN 244..517
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 266..508
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT MOTIF 459..462
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 279..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 930 AA; 104930 MW; E1DB3FE04BF99A7E CRC64;
MLNFVALDLE TSGLDCLQDE IIEIGLVKMV DGKEIDSFST LIRPKGILPV KIKRLTGIKD
HELQDAPKLQ EVLPVILQFI ADLPLVGHNV KFDYDFLSTA VQSPLANPLY DTLELSKYLM
PGASNHRLGY LCSYLGIDIP NQHRALDDAR GAAMLLIHLL NQCEEMEPEL IWQLSQFLSK
SGSLWHSVLE TLSSRMIKMF PDRKITATIP GATEEDSNQS ERIPQPKTTL DFEQCLAVLG
PEGILATTLP RFRYRSQQCD MMEQVTKGLN GDKTVLVEAG TGTGKSLAYL VPAIAWAKQN
HERVLISTHT INLQEQLWNK DIPLLAKLPE YEFKSAIMKG RGNYICLRRW HSFMKEDNHT
PDEAAFLAKI LIWIYQTNTG DKGELVLNYS DFEYWYRVCS ESDGCLGNRC QYFKEKCYFM
AAKRKAERAD IVIVNHSLLL SDANADNMIL PSYGPLIIDE AHHLENCATD HLGRAVTRVG
VLRWLAVATK LLSKLEKIAF LTIDGRWEKL LLQSSETKQR TREAATSFFE MALSWIKSID
RNGEGRCSMR FDRGGNIDGI PSIPVAVDAE LDNLLVNLRT LCQALVKISD QLEEGTVITG
GGPGIIRDLA AWASVGQELS DNLEWICRHQ EESQVYWVEG GGDSPEVVFR SAPIDVGPLL
YEKLFSENRP VVLTSATLSV DGNFKHYINS VGLDFLPQEN ILEKHLNSPF NYNEQAILCV
ARDILPPGQV SNKEYHDELS KAIFHISMAA EGRSLVLFTS HRSLRETYQR LKDQYENEDI
CLLGHELDGS RRRLVEQFME GRRTVLFGAS SFWEGVDIPG EALSCVIIVK LPFAPPNHPV
TEARLQKLSR QGRNGFMEHQ IPQAVIKFKQ GFGRLIRGPE DRGVVVVLDG RLVEKRYGYK
FFNSLPIAQH IRDSWLGISK KARFWLTTGK
//
