ID K6YCI3_9ALTE Unreviewed; 480 AA.
AC K6YCI3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=sbcB {ECO:0000313|EMBL:GAC14323.1};
GN ORFNames=GLIP_1690 {ECO:0000313|EMBL:GAC14323.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC14323.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC14323.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC14323.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC14323.1}.
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DR EMBL; BAEN01000035; GAC14323.1; -; Genomic_DNA.
DR RefSeq; WP_008844139.1; NZ_BAEN01000035.1.
DR AlphaFoldDB; K6YCI3; -.
DR STRING; 1127673.GLIP_1690; -.
DR eggNOG; COG2925; Bacteria.
DR OrthoDB; 9763470at2; -.
DR Proteomes; UP000006334; Unassembled WGS sequence.
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; 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; 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 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:UP000006334}.
FT DOMAIN 200..354
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51784"
FT DOMAIN 358..480
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51785"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-2"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000977-1"
FT BINDING 184
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; 55253 MW; D8F1B92EFBC69D43 CRC64;
MNNNKHQSIL WHDYETWGVN PQKDFPCQFA GIRTDLDLNI IEKPVKWYSQ IPNDYLPNPY
AALVTGITPQ LTLRDGLVEA EFIKKILEQM AKPGTCSAGY NSIRFDDEVT RNTLYRNLHD
PYAREWQNGN SRWDIIDLVR ACYALRPEGI NWVYKDDGTP SFKLEDLTQA NQISHADAHD
ALSDVYATIA IAKLVKQTQP KLYDYIFNLR TKRNVAEQIN LESQIPLVHI SSKLPAINGC
CTWILPIAYH PINKNAVICL NLALDPQPLF DLDIEQIKTR LYQPNSELEE GQQRLPIKLL
HLNKCPIVAP AKTLTEENAQ RLGIDRNQCL QNLALLKSQV SLADKLISLY SQERKSEDSI
DPDYALYSGG FLSDSDRSKL TQIHQMDPTN LGSKDWGFSD PRLNTLLFRY RARNYPLSLS
EEEVIKWQRH RQYRLTDPDS PASIRLPEYL GLLEELTFEY QNNPDKRAII RALHQYAESL
//
