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Database: UniProt
Entry: A0A1H1LN74_9PSED
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Original site: A0A1H1LN74_9PSED 
ID   A0A1H1LN74_9PSED        Unreviewed;       477 AA.
AC   A0A1H1LN74;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SAMN05216221_0211 {ECO:0000313|EMBL:SDR75339.1};
OS   Pseudomonas oryzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1392877 {ECO:0000313|EMBL:SDR75339.1, ECO:0000313|Proteomes:UP000243359};
RN   [1] {ECO:0000313|Proteomes:UP000243359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32247 {ECO:0000313|Proteomes:UP000243359};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; LT629751; SDR75339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1LN74; -.
DR   STRING; 1392877.SAMN05216221_0211; -.
DR   OrthoDB; 9763470at2; -.
DR   Proteomes; UP000243359; Chromosome i.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
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; IPR022894; Oligoribonuclease.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11046:SF11; EXODEOXYRIBONUCLEASE I; 1.
DR   PANTHER; PTHR11046; OLIGORIBONUCLEASE, MITOCHONDRIAL; 1.
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:UP000243359}.
FT   DOMAIN          195..348
FT                   /note="ExoI SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51784"
FT   DOMAIN          351..471
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   477 AA;  54278 MW;  496EDC0683FD2C4D CRC64;
     MTASIFWYDY ETTGIDPRRD RPLQVAGIRT DEALNEIGAP LNLYCRPSDD ILPHPMSCLI
     TGIDPARLEQ QGLGEAEFMT RLHAELARPG TCSAGYNSLR FDDEVTRYSL YRNFFDPYAR
     EWQGGNSRWD LIDLVRTAYA LRPQGIEWPQ EEGRVSLRLE KLTAANGIEH GQAHDALADV
     RATIALARLL RERQPRLYAW CYQLRSKPQV LEQIRLLQPM VHISGRFSAQ RHFLSVVLPL
     AWHPRNRNAL IVCDLQADIA PLLELPAEVL AKRLYTRREE LGEDELPVPL KLVQINRCPI
     VAPLAVLRPE DRERLGVDML QCTARAQLLE QQRTVWADKL PQIFAENGFA ASADPEQRLY
     DGFIGDRDRG LCVQVRDSDP QQLAKYAGQF TDERLVELLF RYRARNFPQT LSEAEQLRWM
     EFCRLRLSDS SAGAPNTLAQ FEQAMGELPG AADPAQRALL GAWQAHAQGL RQRYGLG
//
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