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Database: UniProt
Entry: A0A0F2CA81_9MICO
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ID   A0A0F2CA81_9MICO        Unreviewed;       281 AA.
AC   A0A0F2CA81;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:KJQ55762.1};
DE            EC=3.1.11.2 {ECO:0000313|EMBL:KJQ55762.1};
GN   Name=xthA {ECO:0000313|EMBL:KJQ55762.1};
GN   ORFNames=RS85_00343 {ECO:0000313|EMBL:KJQ55762.1};
OS   Microbacterium sp. SA39.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ55762.1, ECO:0000313|Proteomes:UP000033425};
RN   [1] {ECO:0000313|EMBL:KJQ55762.1, ECO:0000313|Proteomes:UP000033425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA39 {ECO:0000313|EMBL:KJQ55762.1,
RC   ECO:0000313|Proteomes:UP000033425};
RA   Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJQ55762.1}.
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DR   EMBL; JXRU01000022; KJQ55762.1; -; Genomic_DNA.
DR   RefSeq; WP_046011697.1; NZ_JXRU01000022.1.
DR   AlphaFoldDB; A0A0F2CA81; -.
DR   STRING; 1263625.RS85_00343; -.
DR   PATRIC; fig|1263625.4.peg.353; -.
DR   OrthoDB; 9803914at2; -.
DR   Proteomes; UP000033425; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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; IPR020848; AP_endonuclease_F1_CS.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR037493; ExoIII-like.
DR   NCBIfam; TIGR00633; xth; 1.
DR   PANTHER; PTHR43250; EXODEOXYRIBONUCLEASE III; 1.
DR   PANTHER; PTHR43250:SF2; EXODEOXYRIBONUCLEASE III; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR   PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KJQ55762.1};
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:UP000033425}.
FT   DOMAIN          4..258
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        158
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        258
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         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         160
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   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   SITE            160
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            228
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            258
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ   SEQUENCE   281 AA;  31200 MW;  BFD67553FCAC81B3 CRC64;
     MRLATWNVNS IRTRVTRTVE FAVREDLDVL AMQEVKCKPE QFPYGPFEEA GYHVEVHGLN
     QWNGVAIASR LPITDVRTAF DGMPGFAKGH EGPDAPLEAR ALGAMVEGVR VWSLYVPNGR
     SLDDPHLAYK LHWLEELKKS TAAELAANPE LPLALVGDFN IIPFDHDNGD PDIVVGRSTH
     VSPTERAAFF ALEDAGVTDV VRPLLPEGYT YWDYQRLKFP RNEGIRIDFV LGSRTFADAV
     TGASIHRNER KGEQPSDHVP VVVDVNLGAA DEDDDLPMIF S
//
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