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Database: UniProt
Entry: Q47ZA1_COLP3
LinkDB: Q47ZA1_COLP3
Original site: Q47ZA1_COLP3 
ID   Q47ZA1_COLP3            Unreviewed;       268 AA.
AC   Q47ZA1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AAZ26006.1};
DE            EC=3.1.11.2 {ECO:0000313|EMBL:AAZ26006.1};
GN   Name=xth {ECO:0000313|EMBL:AAZ26006.1};
GN   OrderedLocusNames=CPS_3173 {ECO:0000313|EMBL:AAZ26006.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ26006.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ26006.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ26006.1};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ26006.1; -; Genomic_DNA.
DR   RefSeq; WP_011043956.1; NC_003910.7.
DR   AlphaFoldDB; Q47ZA1; -.
DR   STRING; 167879.CPS_3173; -.
DR   KEGG; cps:CPS_3173; -.
DR   eggNOG; COG0708; Bacteria.
DR   HOGENOM; CLU_027539_0_3_6; -.
DR   Proteomes; UP000000547; Chromosome.
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; IPR020847; AP_endonuclease_F1_BS.
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; PS00726; AP_NUCLEASE_F1_1; 1.
DR   PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR   PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AAZ26006.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR604808-2};
KW   Manganese {ECO:0000256|PIRSR:PIRSR604808-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2}.
FT   DOMAIN          4..260
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        260
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         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-2"
FT   BINDING         260
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            230
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
FT   SITE            260
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604808-3"
SQ   SEQUENCE   268 AA;  31184 MW;  C5BECD745BE603EC CRC64;
     MKIISFNING LRARLHQLQA IIDKHQPDII GLQEIKVHDE AFPLEAVEAM GYHVYFHGQK
     AHYGVAMLCK KEAESVQRGF PTDDDEAQRR MIMVTTTNDK GEKVTVLNGY FPQGENISHE
     TKYPYKRKFY KDLMTYLNDN HVNDENVVVM GDINISPQDL DIGIGDVNSK RWLKSGKCSF
     QPEEREWLTR LMDWGFVDTF RQLHPDTTER YSWFDYRSRG FDDNRGLRID VVLATKNMAE
     QCIEADIDYE LRAIEKPSDH APIWSTFS
//
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