ID A0A0F4RK28_9RHOB Unreviewed; 266 AA.
AC A0A0F4RK28;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:KJZ20283.1};
GN ORFNames=TW80_05550 {ECO:0000313|EMBL:KJZ20283.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20283.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ20283.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ20283.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR604808-2};
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000256|ARBA:ARBA00007092}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJZ20283.1}.
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DR EMBL; JXYE01000002; KJZ20283.1; -; Genomic_DNA.
DR RefSeq; WP_045996295.1; NZ_JXYE01000002.1.
DR AlphaFoldDB; A0A0F4RK28; -.
DR STRING; 579483.TW80_05550; -.
DR PATRIC; fig|579483.3.peg.1132; -.
DR OrthoDB; 9803914at2; -.
DR Proteomes; UP000033741; Unassembled WGS sequence.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd09086; ExoIII-like_AP-endo; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR037493; ExoIII-like.
DR NCBIfam; TIGR00195; exoDNase_III; 1.
DR NCBIfam; TIGR00633; xth; 1.
DR PANTHER; PTHR43250; EXODEOXYRIBONUCLEASE III; 1.
DR PANTHER; PTHR43250:SF1; EXODEOXYRIBONUCLEASE III; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT DOMAIN 4..257
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 158
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 227
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 257
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ SEQUENCE 266 AA; 29848 MW; 5DD25DC107E4ABA9 CRC64;
MKIATFNING VKARINALTD WLDDANPDVA ILQEIKSIDE NFPREIIEDK GYNVETHGQK
GFNGVAILSK LPLEDVTRGL PGAQGAGREG VDDEEARYIE ATVVGDVAIR ICGLYLPNGN
PAPGPKYDYK LRWMERLYLR AQELMLAEQP ALMAGDYNII PQAEDAARPD SWRDDALFRP
ESRAAFRKIL NLGFTEAFRA REAGAGHYSF WDYQAGAWEK NNGIRIDHFL LTPQCADLMN
NCWIESEVRG KEKPSDHVPV WVELAA
//