ID A0A2A2A9N8_9BURK Unreviewed; 480 AA.
AC A0A2A2A9N8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Exodeoxyribonuclease I {ECO:0000256|ARBA:ARBA00019900};
DE EC=3.1.11.1 {ECO:0000256|ARBA:ARBA00012108};
DE AltName: Full=DNA deoxyribophosphodiesterase {ECO:0000256|ARBA:ARBA00031220};
GN ORFNames=CK625_12850 {ECO:0000313|EMBL:PAT34513.1};
OS Vandammella animalimorsus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Vandammella.
OX NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT34513.1, ECO:0000313|Proteomes:UP000218054};
RN [1] {ECO:0000313|EMBL:PAT34513.1, ECO:0000313|Proteomes:UP000218054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT34513.1,
RC ECO:0000313|Proteomes:UP000218054};
RA Bernier A.-M., Bernard K.;
RT "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT infections in humans.";
RL Submitted (AUG-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 -!- 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:PAT34513.1}.
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DR EMBL; NSJB01000015; PAT34513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2A9N8; -.
DR Proteomes; UP000218054; 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 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};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Reference proteome {ECO:0000313|Proteomes:UP000218054}.
FT DOMAIN 195..354
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51784"
FT DOMAIN 358..477
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51785"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 10
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 480 AA; 54313 MW; 2A4C1824060DA7AF CRC64;
MQTFLWHDYE TFGADPRRDR PAQFAAIRTD LQLNELQAPL EWFCQPPQDY LPDAQACLIT
GITPQRAWQQ GVSEAVFAQH VHDAFSQPGT IGVGYNTIRF DDEFTRFLLW RNLRDPYARE
WRDGNGRWDL LDVARMAYAL RPDGLQWPLG EDGRVSFRLE VLSAANGLAH EAAHDAVSDV
RATIALARRL RQCNERLFEF ALRLRDKRAV AQELGLPAAP AQARPFVHVS GMFPVEQGCL
AVMWPLASHP HNRNELIAWN LAHDPSELVE LDARSIHQRL FTRQANLPEG VQRLPIKTVH
LNKSPMVVGN CKVLTPALQQ RWGLDWAQIE RHAQAARALP DMSAVWAEVF QRPAAPAQPL
PAEQDLYGGF VGDADRQRLQ RLLLQPVAQW PAGNLGFDDA RLDELVFFYR ARNHPESLDE
AQRQRWEQHR KAVLIDGAGG ARTAEQLMEQ VDALSDTATE AQQDILAALY EWADAIVPEA
//
