ID F6B4T3_DESCC Unreviewed; 929 AA.
AC F6B4T3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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=Desca_1336 {ECO:0000313|EMBL:AEF94195.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94195.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|EMBL:AEF94195.1, ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF94195.1, ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
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}.
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DR EMBL; CP002736; AEF94195.1; -; Genomic_DNA.
DR RefSeq; WP_013810124.1; NC_015565.1.
DR AlphaFoldDB; F6B4T3; -.
DR STRING; 868595.Desca_1336; -.
DR KEGG; dca:Desca_1336; -.
DR eggNOG; COG1199; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_012117_1_0_9; -.
DR OMA; VVTNHAM; -.
DR Proteomes; UP000009226; Chromosome.
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: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: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; IPR001650; Helicase_C.
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:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 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.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02206}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:AEF94195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009226};
KW Transferase {ECO:0000313|EMBL:AEF94195.1}.
FT DOMAIN 244..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 266..507
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 738..913
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 929 AA; 104390 MW; 4957ECC43400EE68 CRC64;
MFSFVALDLE TTGLDCWSDD IIEIGMVKVI DGQERDFFQS LVRPGGPLPV KIKQLTGLKD
DDFQSAPLFQ TIIPKILTFI GDLPLVGHNI KFDRDFLAAA CGHQLPNDLY DTFELARILQ
PSAPSHRLGE LCKIAGVEVN VEHRALDDAR SSARLMLKLL SNLTDTEPEV VWQLSHLLRE
AGSAWHPVFQ EISNQLLKKF PDKKLGQRIP GAPPLEPTTG DRQKQDKTAI SLTDCLNILG
PQGAMESTMP RFQYRPQQCD MMGEVVKAFN EDKILLVEAG TGTGKSLAYL VPAIVWARQN
DERVLITTHT INLQEQLWHK DLPLLANLPD FEFKAALMKG RSNYLCLRRW FALMAEPNHQ
PEEAHFLARL LVWLHQTITG DKSELFIPYQ ESEYWYRVCS ESDGCLGSRC RFFAEKCFFA
AARRAAEQAD VVIVNHSLLL SDVNTDNMVL PSYGPLIIDE AHHLENTATE HLGYTSGRSE
VSRWLTATGR QLQKLEQLVV SVDPEGWQKL LKQSIAAKQT CMDSVTVLFE MLHRWAGQSA
VNSDFGRYNL RFDRPENPDG VCSLPLAIDT ELDNLLVNIR TFNQLLIKLS ARLEEVITLT
EDAAGVIKDM ASAISLGQEL ANKLEFIGRS QGDGYVYWLE GSSETDILLR AAPIDVGPLL
QEKLFSAKRP VVLTSATLSV NGSFDYFIKS IGLDLLPKDS INEKQLDSPF NYSEQVLLCA
ARDIPQPGDL GDKAYHDVIS SIIYRLSLAA GGRTLVLFTS HRSLREVYHR LKEDFEEQDI
CLLGHELDGS RGRLVEQFKE GHRTVLFGAA SFWEGVDIPG ETLSCVIIVK LPFSPPNQPV
VEARLQRIAR QGGNGFHDYQ IPQAVIKFKQ GFGRLIRDPE DKGAVVILDS RLVEKRYGVK
FFNSLPVTEH FRGSWQQILS KVYIWLNPN
//