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Database: UniProt
Entry: M1NZN4_DESSD
LinkDB: M1NZN4_DESSD
Original site: M1NZN4_DESSD 
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};
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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
//
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