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Database: UniProt
Entry: A0A285P6B8_9PSED
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ID   A0A285P6B8_9PSED        Unreviewed;       472 AA.
AC   A0A285P6B8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Exodeoxyribonuclease I {ECO:0000256|ARBA:ARBA00019900, ECO:0000256|PIRNR:PIRNR000977};
DE            EC=3.1.11.1 {ECO:0000256|ARBA:ARBA00012108, ECO:0000256|PIRNR:PIRNR000977};
GN   ORFNames=SAMN05660463_03494 {ECO:0000313|EMBL:SNZ16797.1};
OS   Pseudomonas sp. URIL14HWK12:I9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ16797.1, ECO:0000313|Proteomes:UP000232228};
RN   [1] {ECO:0000313|EMBL:SNZ16797.1, ECO:0000313|Proteomes:UP000232228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ16797.1,
RC   ECO:0000313|Proteomes:UP000232228};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000563,
CC         ECO:0000256|PIRNR:PIRNR000977};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000977-2};
CC       Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000256|PIRSR:PIRSR000977-
CC       2};
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DR   EMBL; OBEM01000007; SNZ16797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285P6B8; -.
DR   OrthoDB; 9763470at2; -.
DR   Proteomes; UP000232228; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd06138; ExoI_N; 1.
DR   Gene3D; 3.30.1520.20; Exonuclease ExoI, domain 2; 1.
DR   Gene3D; 1.20.1280.70; Exonuclease ExoI, domain 3; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR023607; Exodeoxyribonuclease_I.
DR   InterPro; IPR034748; EXOI_C.
DR   InterPro; IPR034747; EXOI_SH3.
DR   InterPro; IPR038649; EXOI_SH3_sf.
DR   InterPro; IPR013620; Exonuc_1_C.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF08411; Exonuc_X-T_C; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51785; EXOI_C; 1.
DR   PROSITE; PS51784; EXOI_SH3; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR000977};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR000977};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR000977};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000977};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000977-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000977-2};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000977};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232228}.
FT   DOMAIN          195..348
FT                   /note="ExoI SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51784"
FT   DOMAIN          351..467
FT                   /note="ExoI C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51785"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
SQ   SEQUENCE   472 AA;  54121 MW;  78C409678FD1A0AB CRC64;
     MTASIFWYDY ETTGIDPRCD RPLQVAGLRT DHQLNVIDEP LNLYCRPSDD ILPHPAACRI
     TGITPQILQA RGLSEAAFMA RVHEQLSRPG TCGAGYNTLR FDDEVTRYSL YRNFYDPYAR
     EWQGGNSRWD LIDIVRAAYA LRPDGIEWPE RDGQVSLKLE ALTAANRLEH GQAHDALSDV
     YATIALAKLI RARQPKLFDW FFQLRGKRAV TQQIHLMQPL VHISGRFSAA RSYLGVVLPL
     AWHPVNRNAL IVCDLHLDPA VLWELTPEAL AKRLYTRREE LAEGERPVPL KLIHVNRCPV
     IAPMSVLREQ DRRRLGLDME QLKQHAQALA EAACDWPSLL AQVYRDSDFA TSEDPEQQLY
     NGFIAERDRR LCDQVRSASA SALGNSEWIF DDARLTELLW RYRARNFPEA LDALERQRWQ
     SFCRARLSEP KHGAPHTVAQ FEAALADYDM EAEPVLQQWA EYVHGLRERF GL
//
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