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Database: UniProt
Entry: S2KTQ4_HALAF
LinkDB: S2KTQ4_HALAF
Original site: S2KTQ4_HALAF 
ID   S2KTQ4_HALAF            Unreviewed;       271 AA.
AC   S2KTQ4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:EPC03908.1};
GN   ORFNames=L861_01010 {ECO:0000313|EMBL:EPC03908.1};
OS   Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC03908.1, ECO:0000313|Proteomes:UP000014463};
RN   [1] {ECO:0000313|EMBL:EPC03908.1, ECO:0000313|Proteomes:UP000014463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35
RC   {ECO:0000313|Proteomes:UP000014463};
RX   PubMed=23868129; DOI=10.1128/genomeA.00497-13;
RA   Tahrioui A., Quesada E., Llamas I.;
RT   "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT   Halomonas anticariensis FP35.";
RL   Genome Announc. 1:31-31(2013).
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:EPC03908.1}.
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DR   EMBL; ASTJ01000011; EPC03908.1; -; Genomic_DNA.
DR   RefSeq; WP_016414642.1; NZ_KE332377.1.
DR   AlphaFoldDB; S2KTQ4; -.
DR   STRING; 1121939.L861_01010; -.
DR   PATRIC; fig|1121939.11.peg.184; -.
DR   eggNOG; COG0708; Bacteria.
DR   OrthoDB; 9803914at2; -.
DR   Proteomes; UP000014463; 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; 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; PS00727; AP_NUCLEASE_F1_2; 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:UP000014463}.
FT   DOMAIN          4..262
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        152
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-1"
FT   ACT_SITE        262
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         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   SITE            154
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            232
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            262
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ   SEQUENCE   271 AA;  31688 MW;  EFE8D4FDD479CF39 CRC64;
     MRLVSFNING LRARLHQLEA LIDTHRPAVI GLQETKVQDS EFPEDAIKSL GYHVYYHGQK
     GHYGVALLCR EAPEAVFYGL PDDGEDAQRR MIGARLALTN GKTMTIWNGY YPQGENINHA
     TKFPYKRTFY DQFSRMLETQ HHQDERIAVM GDFNISPEDI DIGIGEANRK RWLREGKTSF
     QPIEREWLSR IKNWGFKDSY RHCHPDIDDR FSWFDYRSRG FERDPKRGLR IDYILVTASL
     CEHVSDAGID YELRSMERPS DHAPVWTELS F
//
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