ID A0A0U2VGZ0_9LACT Unreviewed; 934 AA.
AC A0A0U2VGZ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=NY10_389 {ECO:0000313|EMBL:ALV21009.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV21009.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV21009.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV21009.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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; CP010796; ALV21009.1; -; Genomic_DNA.
DR RefSeq; WP_058918389.1; NZ_CP010796.1.
DR AlphaFoldDB; A0A0U2VGZ0; -.
DR STRING; 1564681.NY10_389; -.
DR KEGG; carc:NY10_389; -.
DR PATRIC; fig|1564681.3.peg.386; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000064734; 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: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; 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:SF47; FANCONI ANEMIA GROUP J PROTEIN; 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; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 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:0000313|EMBL:ALV21009.1};
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:UP000064734}.
FT DOMAIN 248..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT MOTIF 463..466
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
FT BINDING 285..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02206"
SQ SEQUENCE 934 AA; 107827 MW; 07DFC375CD07B6EF CRC64;
MKEKVTYAVV DIETTGGNAA TGDRMIQFGC ALIEEGKIVQ QYAIDINPLV SIPKQIEHLT
GISNQTVANA PYFEDVAPMI YNLLEGCIFV AHNIQFDYKF LSEELVRCGL PPLNSIGMDT
VELAQILLPT EPSFRLNDLA TRFGFLHDNP HQADSDAYVT AELFLLLKQK LKKLPLVTVE
KLVELAEHCT MQTNLFFKET LSDMLTMRQL LSDDLLVKEG LAIRKKTVTY EQRTHRETEH
YPVGIEAKEQ LFQKKLTTRK LQIQMMDEVY RYFSEKDSEH FVIEAATGIG KTLGYLIPLA
YVATPQEPVI ISTYTTLLQK QLLEKDSIQL NTILPFAVQA AILKSKHHYI HLAKFQEVLK
DPIEHQMDAI LKMRTLTWLT ETVTGDLDEL NLTNYLQPFW NKIRHRGWMD NAQEDLFYEQ
DFYLHAQEKV KQASIIITNH AFLCHDLQRE EPVLPNVQKI IIDEAHHLAD VATTASSEVF
SYYRNQQLMK LIGKRADDKS FLSRLSALAE KSNSIQLTQI NMIEMSVVAF EEELAAFFDK
LISYCRSELP ERQQMSDQLD VQFSKTENWT LDLKKKTKIL LALMEDIVFL GYEITRQALI
HREQFTHRER HLIDDFFELI GTVESQKGIF QKIFRESEQN EVTWFSFKQK SPKNSFVIKR
SRIDSSEFLR TKLAEQTTSI LYTGATLELN GDFSYFEKQL GEKKLRKMVI PSPYDYQKQA
RLWIPKELKP LKQLTKKQYA EMIVEHLETV IQHSNENMMV LFNANETLQD VFSLLQQHPA
FTGRELLAQG LSGSRDRILK RFFHSTGGIL LGADSFWEGV DLPGKSLRII VVTRLPFESP
DRPFTKAKYK WLESQQLSPF KMDTLPKATV RLKQGLGRLV RSEKDKGVMI VLDDRLIKTN
YGQQMLASLP HDLVKEVVAK EELQRNLSLF LEED
//
