ID A0A1S2HQH5_9MICO Unreviewed; 246 AA.
AC A0A1S2HQH5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Exonuclease {ECO:0000313|EMBL:OII13325.1};
DE Flags: Fragment;
GN ORFNames=BIV00_16415 {ECO:0000313|EMBL:OII13325.1};
OS Curtobacterium sp. MCBA15_012.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898738 {ECO:0000313|EMBL:OII13325.1};
RN [1] {ECO:0000313|EMBL:OII13325.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_012 {ECO:0000313|EMBL:OII13325.1};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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:OII13325.1}.
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DR EMBL; MJGP01000060; OII13325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S2HQH5; -.
DR STRING; 1898738.BIV00_16415; -.
DR OrthoDB; 9803914at2; -.
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 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; 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 Exonuclease {ECO:0000313|EMBL:OII13325.1};
KW Hydrolase {ECO:0000313|EMBL:OII13325.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2};
KW Nuclease {ECO:0000313|EMBL:OII13325.1}.
FT DOMAIN 2..233
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT SITE 136
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 203
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT SITE 233
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OII13325.1"
FT NON_TER 246
FT /evidence="ECO:0000313|EMBL:OII13325.1"
SQ SEQUENCE 246 AA; 27818 MW; 98051E5E33EEC4FA CRC64;
EDVDVLGMQE IKCKPEQFPV EAFEAAGYQV EAHGLNQWNG VAFASRLPME DVTRDFPGQP
GFLKGHEGPD LPVEARAIGV TVEDVRLWSL YVPNGRELGD PHYTYKLDWL ARLADRTTEW
LTADPSLKLA LMGDWNVAPF DRDVWDVRVF EGATHVSEPE RAAFRAFEER GLQDVVRPIV
PEGYTYWDYK SLRFPRNEGM RIDFVMGSEA FADVVTDASI HRDERKGDAP SDHVPVVVDL
DLETAL
//
