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Database: UniProt
Entry: A0A363S1T6_9GAMM
LinkDB: A0A363S1T6_9GAMM
Original site: A0A363S1T6_9GAMM 
ID   A0A363S1T6_9GAMM        Unreviewed;       479 AA.
AC   A0A363S1T6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=DCO49_06285 {ECO:0000313|EMBL:PWB28013.1};
OS   Stenotrophomonas sp. SPM.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=2170735 {ECO:0000313|EMBL:PWB28013.1, ECO:0000313|Proteomes:UP000250746};
RN   [1] {ECO:0000313|Proteomes:UP000250746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPM {ECO:0000313|Proteomes:UP000250746};
RA   Frantz D.C., Newman J.D.;
RL   Submitted (APR-2018) 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};
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:PWB28013.1}.
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DR   EMBL; QETL01000017; PWB28013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A363S1T6; -.
DR   Proteomes; UP000250746; 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; 1.10.287.1240; -; 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   PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR30231:SF4; PROTEIN NEN2; 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   Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   DOMAIN          196..351
FT                   /note="ExoI SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51784"
FT   DOMAIN          354..476
FT                   /note="ExoI C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51785"
FT   COILED          322..349
FT                   /evidence="ECO:0000256|SAM:Coils"
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         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
SQ   SEQUENCE   479 AA;  54164 MW;  4C26AEFF4D2CB79E CRC64;
     MADSFLFYDL ETFGQDPRRT RIAQFAAMRT DADLNVIDTP VSFFVRPADD LVPSPMATLV
     TGITPQQAMA EGISEAEAFD RINEQLSRPG TCALGYNTLR FDDEFIRYGL FRNFYDPYER
     EWRNGNSRWD LLDMLRMMRA LRPDGIQWPL REDGATSFKL EHLAEANGVR EGDAHEALSD
     VRATIGMARL FKQSQPRLWE YALKLRDKRF VGSLLDVAAM NPVLHISMRY PASRLCAAPV
     LPLAVHPTIN NRVIVFDLEG ETDDLLELPA DVIAQRLYMR ASELPEGVAR VPLKEVHLNK
     VPALVAWNHL RADDHARLGL DVAAIEAKAA RLREVAAQLA EKVRQVFNQP RPASVSDVDA
     SLYDGFLGAG DKPLLALART SAPQQLAALE GRFRDPRLPE LLFRYRARNH PDSLAPAERE
     RWQDYRRQRL LGESGLGELN LPQYQQQIEA LAAEAPDDAR RTGLLQSLRD WGHHLQETL
//
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