ID I4VN93_9GAMM Unreviewed; 481 AA.
AC I4VN93;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:EIL88684.1};
GN ORFNames=UU5_16984 {ECO:0000313|EMBL:EIL88684.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL88684.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL88684.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL88684.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL88684.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJXS01000394; EIL88684.1; -; Genomic_DNA.
DR RefSeq; WP_008215431.1; NZ_AJXS01000394.1.
DR AlphaFoldDB; I4VN93; -.
DR PATRIC; fig|1162282.3.peg.3215; -.
DR OrthoDB; 9763470at2; -.
DR Proteomes; UP000004557; 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 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}.
FT DOMAIN 195..349
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51784"
FT DOMAIN 353..474
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 481 AA; 54981 MW; F49DA23F326A9CD9 CRC64;
MQTFFWHDYE TFGADTRRDR PVQFAGIRTT MELEIIGEPV MFFGQPPRDS LPHPEACLIT
GITPQQAERE GVSEAEFAAR VHEQLAEPGT CGVGYNSLRF DDEVTRQLLY RNFYEPYGRE
WANGNSRWDL IDLVRMCEAL RPEGIHWPTR EDGSPSFKLE HLATANHLLQ ERAHDALSDV
HALIDLARLI RVRQPRLWDW HFALRRKQRV FELLDVANMT PLVHISSRYP ASRHCLAIIA
PLALHPSRPG EIIVYDLATD PAELLALDED EIADRVFTSR ADLPEGIERI PLRTVRANRT
PALAPLSTLK GTDLGRLQLD LERNLAHRDT LHAATGLADK VRRIFARASD LPPPEDPELA
LYAGFLPDGD KRLLAEVRAT PPAQLGTRTF PFRDPRYPEL LFRYRARNWP ETLDAAERER
WGHFRRERIS RPTPLTTLTL DDYTAKLALM REDAALADRR PLFDQLQAWG EQLAAETGLS
I
//
