ID M1NZN4_DESSD Unreviewed; 478 AA.
AC M1NZN4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Exodeoxyribonuclease I {ECO:0000256|ARBA:ARBA00019900};
DE EC=3.1.11.1 {ECO:0000256|ARBA:ARBA00012108};
DE AltName: Full=DNA deoxyribophosphodiesterase {ECO:0000256|ARBA:ARBA00031220};
GN OrderedLocusNames=UWK_00156 {ECO:0000313|EMBL:AGF76743.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF76743.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000563};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000977-2};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000256|PIRSR:PIRSR000977-
CC 2};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003985; AGF76743.1; -; Genomic_DNA.
DR RefSeq; WP_015402442.1; NC_020304.1.
DR AlphaFoldDB; M1NZN4; -.
DR STRING; 1167006.UWK_00156; -.
DR KEGG; dsf:UWK_00156; -.
DR PATRIC; fig|1167006.5.peg.173; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_7; -.
DR OrthoDB; 9763470at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd06138; ExoI_N; 1.
DR Gene3D; 1.10.287.1240; -; 1.
DR Gene3D; 3.30.1520.20; Exonuclease ExoI, domain 2; 1.
DR Gene3D; 1.20.1280.70; Exonuclease ExoI, domain 3; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR023607; Exodeoxyribonuclease_I.
DR InterPro; IPR034748; EXOI_C.
DR InterPro; IPR034747; EXOI_SH3.
DR InterPro; IPR038649; EXOI_SH3_sf.
DR InterPro; IPR013620; Exonuc_1_C.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08411; Exonuc_X-T_C; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51785; EXOI_C; 1.
DR PROSITE; PS51784; EXOI_SH3; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000313|EMBL:AGF76743.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGF76743.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000977-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000977-2}; Nuclease {ECO:0000313|EMBL:AGF76743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 196..350
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51784"
FT DOMAIN 353..476
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51785"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
SQ SEQUENCE 478 AA; 55175 MW; 6BE715F14CDCFCE9 CRC64;
MTTTLYWHDY ETWGADPRRD RPAQFAGIRT DINLNIIGKP MMNYCKPALD MLPQPEACLI
TGITPQTAME EGLCEAEFMA EIYHEFIQPG TCGVGYNSIR FDDEFTRYGL YRNFYDPYAR
EWRNGNSRWD IIDMLRLTRA LRPEGIEWPT NEEGVTSFRL EDLTRANSIS HEGAHDALSD
VHATIELARL IRTRQPKLYN YLFDMRDKRK VGSNLNIQEQ LVVLHVSSMY PAKQGCISPV
IPLAAHPINK NGIIVYDLRH DPSPLLTLAV DEIKKRLFTR SEDLPEGVER IPLKTIHLNK
SPVVVPMSTL TPEAAECWGI NLKNIETHAK QLRGLPDLSR KLQQVHGDQQ FPPITDPDQN
LYGGGFFSDR DRALMEDIHD MSINDLAKTR MKFEDPRLSE MLFRYRARNW PHSLSQEERV
RWNTFRHNRV TNPDADCGIT LSEYRKQLAK KVMQPDVKER ERKIISALAD WPTLLGLS
//