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Entry: A0A0G3H8W4_9CORY
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ID   A0A0G3H8W4_9CORY        Unreviewed;       273 AA.
AC   A0A0G3H8W4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AKK09779.1};
DE            EC=3.1.11.2 {ECO:0000313|EMBL:AKK09779.1};
GN   ORFNames=CTEST_11860 {ECO:0000313|EMBL:AKK09779.1};
OS   Corynebacterium testudinoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK09779.1, ECO:0000313|Proteomes:UP000035540};
RN   [1] {ECO:0000313|EMBL:AKK09779.1, ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK09779.1,
RC   ECO:0000313|Proteomes:UP000035540};
RX   PubMed=26227591;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT   DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL   Genome Announc. 3:e00784-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT   recovered from necrotic lesions in the mouth of a tortoise.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011545; AKK09779.1; -; Genomic_DNA.
DR   RefSeq; WP_047253885.1; NZ_CP011545.1.
DR   AlphaFoldDB; A0A0G3H8W4; -.
DR   STRING; 136857.CTEST_11860; -.
DR   KEGG; cted:CTEST_11860; -.
DR   PATRIC; fig|136857.5.peg.2342; -.
DR   OrthoDB; 9803914at2; -.
DR   Proteomes; UP000035540; Chromosome.
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:SF2; 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   Hydrolase {ECO:0000313|EMBL:AKK09779.1};
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:UP000035540}.
FT   DOMAIN          5..256
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        157
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        256
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         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         255
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   SITE            159
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            226
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            256
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ   SEQUENCE   273 AA;  30919 MW;  E11BAF253F5643D6 CRC64;
     MRIVNWNVNS VRTRAERVVE FLHRHDVDVL AMQETKCSDD KFPYLAFEEA GYEVAHMGLS
     QWNGVAIASR VGLADVDKHF PGQPGFDKDP SQPQDVEARA IGATCNGVKV WSLYVPNGRE
     IADPHYDYKL RWLYNLKFHI ADTLREDPSH RAVYLGDFNV APLDIDVWDP AFFEGKTHVT
     EPERQAFDGL IDVGLTEVTR PLTAERFTYW DYKSLRFQKG EGMRIDFQLA TPALAGQARA
     AFVDIEERAG KGASDHAPVV VDYVPTADYD EVR
//
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